ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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O17695 | MNSNGPLMEHGKRRVAYYYDSNIGNYYYGQGHVMKPHRIRMTHHLVLNYGLYRNLEIFRPFPASFEDMTRFHSDEYMTFLKSANPDNLKSFNKQMLKFNVGEDCPLFDGLYEFCQLSSGGSLAAATKLNKQKVDIAINWMGGLHHAKKSEASGFCYTNDIVLGILELLKYHKRVLYVDIDVHHGDGVEEAFYTTDRVMTVSFHKYGDFFPGTGDLKDIGAGKGKLYSVNVPLRDGITDVSYQSIFKPIMTKVMERFDPCAVVLQCGADSLNGDRLGPFNLTLKGHGECARFFRSYNVPLMMVGGGGYTPRNVARCWTYETSIAVDKEVPNELPYNDYFEYFGPNYRLHIESSNAANENSSDMLAKLQTDVIANLEQLTFVPSVQMRPIPEDALSALNDDSLIADQANPDKRLPPQITDGMIQDDGDFYDGEREGDDRRNESDAKRAAQFESEGGEKRQKTE | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression. Plays an important role in transcriptional regulation, cell cycle progression and developmental events . Histone deacetylases act via the formation of large multiprotein complexes. Involved in the endoderm determination possibly by repressing end-1 expression. Also involved in vulval development, possibly by repressing lag-2 expression. Required during mitochondrial stress for the activation of genes involved in the mitochondrial unfolded protein response (mtUPR), in concert with homeobox protein dve-1 . Promotes normal hermaphrodite (XX) development, in concert with zinc finger protein tra-4 and nasp-1, perhaps as components of a complex . Plays a role in the regulation of longevity and mtUPR-associated innate immunity . In association with akir-1, plays a role in regulating the transcription of antimicrobial peptide genes in response to fungal infection .
PTM: Sumoylated.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 52138
Sequence Length: 461
Subcellular Location: Nucleus
EC: 3.5.1.98
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Q5A960 | MSTGQEEHLDSKLENQISEEENQSQNQNFPTAIEDSIQASIEKLDEVDDEINPIEVKDEFPTTIGTTYDILHPREPFPKRIKLEETETEPDSNGIADNDQTMVVVPPKKPQLFYTPLKTGLVYDVRMRYHAKVFTSYSEYIDPHPEDPRRIYRIYKKLVEAGIVLDPSLAGINEIGPFMLKIPIREATSEEILQVHSEDHLKFIQSTEDMSRDQLLKETETGDSIYVNNDSYLSAKLSCGGTIEACKAVIEGRVKNSLAIVRPPGHHAEPNTPAGFCLFSNVAVAAKNMLKNYPESVRRIVIVDWDIHHGNGTQKAFYNDPRVLYISLHRFENGKFYPGTKYGDLNQVGEGPGEGFTINIPWRSSGMHDGDYVYAFNKIIQPVISEFDPDLIIVSSGFDAADGDVIGACHVTPAGYGYMTHTLKGIARGKLAVILEGGYNLDSISKSALAVAKVLVGEPPENTITLRPQAEAIEVVDEVIKIQSKYFKSLRNGIPNGIFEDVYDLADVEKSNYKLVNIADPIRSHQVEKLFNEKEFINIPIISSPSNGEKPPFTTDLPDQLEDLIVASPDIYNCTTIILTIHDPPEIWANINPTNGVIETNSTMVLEHPLVQIMDKIQKEKDPENQEKFGYLDINIPSFQLPIPGTTSESSTYNPIIFAQEVLLYIWDNYIAYFQQLKNLVMVGFGDSYQSIVNLYGKRPSNEIKDLIKGTVAFLNRTTLKPLIPVMDESMVDWYYQNSIIFTSNFNTCWTGGSGAGNGNGNGNGNNGNSSNGGGNKSADSNGHDDFSKRPRKKFGRVIKAKTDGLCDVIQEKFDEGVDFILDSIEDYSSSED | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates the YNG2 subunit of NuA4 histone acetyltransferase (HAT) module, leading to the reduction of YNG2 and NuA4 HAT at the promoters of hypha-specific genes. Plays a key role in the regulation of filamentous growth and virulence. Involved in the switch between two heritable states, the white and opaque states. These two cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically at low frequency.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 92913
Sequence Length: 833
Subcellular Location: Nucleus
EC: 3.5.1.98
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P53973 | MDSVMVKKEVLENPDHDLKRKLEENKEEENSLSTTSKSKRQVIVPVCMPKIHYSPLKTGLCYDVRMRYHAKIFTSYFEYIDPHPEDPRRIYRIYKILAENGLINDPTLSGVDDLGDLMLKIPVRAATSEEILEVHTKEHLEFIESTEKMSREELLKETEKGDSVYFNNDSYASARLPCGGAIEACKAVVEGRVKNSLAVVRPPGHHAEPQAAGGFCLFSNVAVAAKNILKNYPESVRRIMILDWDIHHGNGTQKSFYQDDQVLYVSLHRFEMGKYYPGTIQGQYDQTGEGKGEGFNCNITWPVGGVGDAEYMWAFEQVVMPMGREFKPDLVIISSGFDAADGDTIGQCHVTPSCYGHMTHMLKSLARGNLCVVLEGGYNLDAIARSALSVAKVLIGEPPDELPDPLSDPKPEVIEMIDKVIRLQSKYWNCFRRRHANSGCNFNEPINDSIISKNFPLQKAIRQQQQHYLSDEFNFVTLPLVSMDLPDNTVLCTPNISESNTIIIVVHDTSDIWAKRNVISGTIDLSSSVIIDNSLDFIKWGLDRKYGIIDVNIPLTLFEPDNYSGMITSQEVLIYLWDNYIKYFPSVAKIAFIGIGDSYSGIVHLLGHRDTRAVTKTVINFLGDKQLKPLVPLVDETLSEWYFKNSLIFSNNSHQCWKENESRKPRKKFGRVLRCDTDGLNNIIEERFEEATDFILDSFEEWSDEE | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 80070
Sequence Length: 706
Subcellular Location: Nucleus
EC: 3.5.1.98
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Q944K3 | MTHTRVISTWTELTRDLAIYLLFTFFAIKVFKFLFSCNRTSEISSFSMATHPEALRRERILNSKLYFDVPLSKVSIIYSSSYDISFMGIEKLHPFDSSKWGRVCKFLVSDGFLEEKAIVEPLEASKIDLLVVHSENYLNSLKSSATVARITEVAPVAFFPNFLVQQKVLYPFRKQVGGTILAAKLATERGWAINIGGGFHHCTAERGGGFCAFADISLCIHFAFLRLRISRVMIIDLDAHQGNGHETDLGDDNRVYILDMYNPEIYPFDYRARRFIDQKVEVMSGTTTDEYLRKLDEALEVASRNFQPELVIYNAGTDILDGDPLGLLKISPDGITSRDEKVFRFAREKNIPLVMLTSGGYMKSSARVIADSIENLSRQGLIQTRPE | Cofactor: Binds 1 zinc ion per subunit.
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 43804
Sequence Length: 387
Subcellular Location: Nucleus
EC: 3.5.1.98
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Q09440 | MSSDKFKLDTLFDDNDEIIEPDGADVKKRNVAYYYHKDVGHFHYGQLHPMKPQRLVVCNDLVVSYEMPKYMTVVESPKLDAADISVFHTEDYVNFLQTVTPKLGLTMPDDVLRQFNIGEDCPIFAGLWDYCTLYAGGSVEGARRLNHKMNDIVINWPGGLHHAKKSEASGFCYVNDIVLGILELLKYHKRVLYIDIDIHHGDGVQEAFNNSDRVMTVSFHRFGQYFPGSGSIMDKGVGPGKYFAINVPLMAAIRDEPYLKLFESVISGVEENFNPEAIVLQCGSDSLCEDRLGQFALSFNAHARAVKYVKSLGKPLMVLGGGGYTLRNVARCWALETGVILGLRMDDEIPGTSLYSHYFTPRLLRPNLVPKMNDANSAAYLASIEKETLACLRMIRGAPSVQMQNIVGIRLDEIEQIEENERLQKSSKSSIEYEVGKVSEKMEEECFVEEDSKPPSFPPGQDPRRIGQYWGYDRSGLAPPRSHSDVIEEAKYEDRDRRKDLNIPGIP | Function: Probably responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). As a likely component of a histone deacetylase complex, together with saeg-1 and hda-2, functions downstream of the cAMP-dependent kinase egl-4 to regulate the expression of genes required for egg-laying and forgaging .
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
Sequence Mass (Da): 57138
Sequence Length: 507
Subcellular Location: Nucleus
EC: 3.5.1.98
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Q1PW30 | MRKFLKVTLASALIGCGVIGTVSSLMVKEAKAVEIITHWVPHEVYGMPGEPDNSGKVFFSGLKAKYMGYPKDAQRSPYPGKYSKFWKTLPAYRYYIPDYMYNRDEVRPSNPIKGTFKLEQCVACHSVMTPGIVRDYNKSAHSKAEPAPTGCDTCHGNNHQKLTMPSSKACGTAECHETQYNEQGQGGIGSHASCSSFAQVECAWSIERPPGDTAGCTFCHTSPEERCSTCHQRHQFDPAVARRSEQCKTCHWGKDHRDWEAYDIGLHGTVYQVNKWDTEQFDFSKKLSDADYVGPTCQYCHMRGGHHNVQRASIVYTSMGMSMADRGAPLWKEKRDRWVSICDDCHSPRFARENLQAMDESVKDASLKYRETFKVAEDLLIDGVLDPMPKDLCPDWSGQHIWSLKIGAYHDGEAYGGTTGESGEFRMSNCTDVERLCFESVGYFQTYIYKGMAHGSWNDATYSDGSFGMDRWLVNVKQNASRARRLAALEKKVGISWQPEQFWKTGEWLDQLTGPYIVKNHPGKTIFDLCPDPGWLDTHHAPAEEVEYIERKLKELGITAGSHSAHHHESGHDPAARSMKEH | Cofactor: Binds 8 heme c groups per subunit. One of them is an atypical heme c (unusual heme c binding motif CXXXXCH). Catalysis takes place at heme-4, termed P460. The other c-type hemes mediate electron transfer to the external electron acceptor, which is a cytochrome c-type protein.
Function: Catalyzes the four-electron oxidation of hydrazine to N2 . The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane . Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans . Cannot oxidize hydroxylamine to NO .
Catalytic Activity: 4 Fe(III)-[cytochrome c] + hydrazine = 4 Fe(II)-[cytochrome c] + 4 H(+) + N2
Sequence Mass (Da): 65577
Sequence Length: 582
Pathway: Nitrogen metabolism.
Subcellular Location: Anammoxosome
EC: 1.7.2.8
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P84626 | MAEEEPKIGVYICHCGENIAGAVNIEEVKKFAETLPNVVVVRDYLFMCSDPGQELIKQDIKEGRVNRVVVAACTPRTHEPIFRKACEDAGLNKYYFEMANIRDQCSWAHWHEKEKATEKAKQIIAAAVAKARLLEPLEDRYVDITQKVLVIGGGIAGIFAALDIANAGYKVYLVERNPSIGGNMAKLDKTFPTNDCSACILTPLMVEVANHPNIELLTYSEVEAVEGTVGNFKVKVRKKQTWVDWDLCTGCGACTDVCPPKARVPDEFNEGLSKRGAIYIQFPQAVPKKAVIDIDACIECGGRKFGTEPRKTKDGKPILAPCEKVCPTGAADRTKPRNPEGELIELDVGAIIVATGYKVMDKTHFKEFAPDSPNVITALQMERLISATGPTEGKLIVPSDIPKYEEWKKKVAKGEEVELEARKPHRIVYVSCVGSRDERFHTYCSKVCCMYMLKQAMLLKEKYPDLDIYIFFIDVRTPGKDFDEYYMRCRQLGIKVIKGKVGGIRRMPDERLWVRGYDAEIGKPVEVIADLVVLATAIEPSDGTIELARKLGINIGAEGFFRERHTKLYPVDTMTEGIFICGCAQGPKDIPDSVAQAKAAASSAMSLIAPGKMKLEPLVSEVDKEKCSGCGICVPLCPYGAITMTKYNESMRAEINPALCKGCGVCAAACPSKAIKLHGFTFEQVLAQVRTLAKRGIVEVL | Cofactor: Binds 4 [4Fe-4S] clusters per subunit.
Function: Has oxidoreductase activity. The Hdl and Mvh subunits may together mediate electron transfer from hydrogen to an unidentified electron acceptor on the cytoplasmic side of the membrane.
Sequence Mass (Da): 77281
Sequence Length: 701
Subcellular Location: Cytoplasm
EC: 1.8.-.-
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P84623 | MVKYGLFLGCNISFNRPDVEVSMRSIFPALGIELDDLVGQSCCPTWGTMPSVDIVGWCAVAARNLALGEEKGIDLMTACNSCYGSLNEARHKMLTNPEIHRKVNEILATIGKRYEGKAKCRHVAWVLYKDVGLEKLKESIKYTLDGITVAVQPGCHFLWPSEVYPDKEEDPFNPKVLRELCEALGAEAPYYTKLIECCGMGALRSTDPEKSFKLVKEKMENIKEEIDADLIVTTCSSCLIQLDDAQERLRKEGKINFSIPVLHLVQVIALCMGFDPEKVAGICVTPRDEIIKRILENKR | Function: Has oxidoreductase activity. The Hdl and Mvh subunits may together mediate electron transfer from hydrogen to an unidentified electron acceptor on the cytoplasmic side of the membrane.
Sequence Mass (Da): 33460
Sequence Length: 299
Subcellular Location: Cytoplasm
EC: 1.8.-.-
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P84621 | MEMMEEGVPDVINLSYLAEREETELEKRVAEIIKELGAERLMYCMQCGACASICPLARVGFEWYNKKLIKALILGLRDELLDDPTPWACVACNRCTEICPRRVSPFEVMFAMRRLMAEEYAIGSLAIEGLRSLYEYGHAVYMAGREARKKVGLPEKPPSTESDPKALEDLRKILKQTKLAELGLVPME | Function: Has oxidoreductase activity. The Hdl and Mvh subunits may together mediate electron transfer from hydrogen to an unidentified electron acceptor on the cytoplasmic side of the membrane.
Sequence Mass (Da): 21306
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 1.8.-.-
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P08159 | MSSKLATPLSIQGEVIYPDDSGFDAIANIWDGRHLQRPSLIARCLSAGDVAKSVRYACDNGLEISVRSGGHNPNGYATNDGGIVLDLRLMNSIHIDTAGSRARIGGGVISGDLVKEAAKFGLAAVTGMHPKVGFCGLALNGGVGFLTPKYGLASDNILGATLVTATGDVIYCSDDERPELFWAVRGAGPNFGVVTEVEVQLYELPRKMLAGFITWAPSVSELAGLLTSLLDALNEMADHIYPSVFVGVDENRAPSVTVCVGHLGGLDIAERDIARLRGLGRTVSDSIAVRSYDEVVALNAEVGSFEDGMSNLWIDREIAMPNARFAEAIAGNLDKFVSEPASGGSVKLEIEGMPFGNPKRTPARHRDAMGVLALAEWSGAAPGSEKYPELARELDAALLRAGVTTSGFGLLNNNSEVTAEMVAEVYKPEVYCRLAAVKREYDPENRFRHNYNIDPEGS | Cofactor: Binds 1 FAD per subunit . The FAD is covalently bound to the protein .
Function: Involved in the degradation of D-nicotine . Catalyzes the oxidation of (R)-6-hydroxynicotine (6-hydroxy-D-nicotine) to 6-hydroxypseudooxynicotine . Oxidation of the pyrrolidine ring of (R)-6-hydroxynicotine leads to the formation of the optically inactive 6-hydroxy-N-methylmyosmine, which hydrolyzes spontaneously to 6-hydroxypseudooxynicotine . Acts with absolute stereospecificity on the D-form of 6-hydroxynicotine . Shows lower activity with (R)-6-hydroxynornicotine, and weak activity with (R)-4-(1-methylpyrrolidine-2-yl)phenol, (R)-6-chloronicotine and (R)-nicotine .
Catalytic Activity: (R)-6-hydroxynicotine + H2O + O2 = 6-hydroxypseudooxynicotine + H2O2
Sequence Mass (Da): 48786
Sequence Length: 458
Pathway: Alkaloid degradation; nicotine degradation; 6-hydroxypseudooxynicotine from nicotine (R-isomer route): step 2/2.
Subcellular Location: Cytoplasm
EC: 1.5.3.6
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Q1LW01 | MDIRASLSILLLLFGLSQASPLREFEAIFVSEPETVDITTQILETNKGSSEVLFEGDVVLPKNRNALICEDKSCFWKKNANNIVEVPYVVSGEFSINDKSVIANAISIFHAQTCIRFVPRSIQADYLSIENKDGCYSAIGRTGGKQVVSLNRKGCVYSGIAQHELNHALGFYHEQSRSDRDQYVRINWNNISPGMAYNFLKQKTNNQNTPYDYGSLMHYGKTAFAIQPGLETITPIPDENVQIGQRQGLSKIDILRINKLYGC | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloendopeptidase which participates in the breakdown of the egg envelope at the time of hatching. Cleaves the N-terminal regions of the zona pellucia glycoproteins ZP2 and ZP3, where it specifically recognizes the peptide sequences TVQQS-|-DYLIK (major site) and KLMLK-|-APEPF (minor site).
Catalytic Activity: Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val-Tyr-|-7-(4-methyl)coumarylamide.
Sequence Mass (Da): 29448
Sequence Length: 263
Subcellular Location: Secreted
EC: 3.4.24.67
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Q8UW74 | MKGTSEVKPMETHRKLLKPLVEKRRRERINNSLEKLRIFLFQTLKSEKLKNPKVEKAEILECTVQFLQSRKLLPLDREAVDKEYQSGFQHCLETTLHFMNSKPDMNGVTKELLSHQMSSCKSPSDAWSPNCAPLTKHVPSLSYQDSAPHLVSNSISISPTKTLVDSHFTYQSFKTWRPWV | Function: Transcriptional repressor. Represses transcription from both N box- and E box-containing promoters (By similarity). Demarcates the prospective midbrain-hindbrain boundary (MHB) region in the neuroectoderm in early gastrulae embryos by repressing transcription of a number of target genes.
Sequence Mass (Da): 20826
Sequence Length: 180
Domain: Has a particular type of basic domain which includes a helix-interrupting proline.
Subcellular Location: Nucleus
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Q4JSX4 | MSGSTRTGSASVLLVGLSFRSAPVTMLEQATVADADLPKMQLSLVDNDVISESLVLSTCNRMEFYTVANAFHSGLDHVVDTIAQFSGLQTAELEPHLYVHYADSAAEHMLKVASGLDSMVIGEQQIIGQLRSAYQSANETGTVGRTLHDLTQRALRTGKRVHSETAIDSAGASMVSFALDQALRYIEPARALSAVVDDAPLSQPLAGHRALIIGAGAMASLASTHLGKLGIDHVTVANRTLSRAENLVNHARQAGVDASAVPLDGVTDCLSAVDIVVSATGAVGNVVTEQDVRAAVGAAGGVASVAGRRGTKVMIDLSMPADIEHSVAEIDGVKLLNIEELTTMAGDRVQDESPARAIVADELQSFLEQQRAQSVVPTVKALRQKAGEVMAEELMALERLTPDMSEADRAAVVKSMKRVVDKLLHTPTVQAKKLSAGGQQVSYPDALAALFNLPNGMVDSVTQPGQADSSAAQTAGTSARADQIPSAARVGRVVREA | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 52036
Sequence Length: 497
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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Q6AB02 | MTVDHAEQGLGVVSEAAAQVDGLGLALTDHPQIRGALVLSTCNRVCLIVETSPEAVAQGFDEAALRRCIADHGANVLAESAQLVCENDAVWRLFRVAAGMESMVFGEREVAGQMKRALSEARREQTVSYTIGHVVEEALKTSRHVATETALAAEGRTVVAVGLDLVAQRMDLDGARVLVMGTGSYAGASCAQLSSRGVAEIQVHSASGRAAGFARRHRVSEALDIDAALAQADLVVTCRGSGVPALSAEAARRAVDARRGRDLMVLDLAISGDVEEPVPAGVEVIDLETIRQAVPASAEAERAAAEHIIATGVRHFAVDLERRRMAPAVVALRDVISDLVTAELERLPEEGSVPVDEVAASLRRLAASMAHIPSARARMASEQGLGDRWLNSLSDVLGIDVDIAAPVIDMSSFANADCMTCPVTGLRVEDLATDAAPRGEERTS | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46740
Sequence Length: 444
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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P48077 | MNIIVVGLSHKTAPVDFREKLSIPKVRIGEAIRELCNYPHIEEVAILSTCNRLEIYLLTSDTYQGIREATQFLADSSDLSLPELRQHLFILLHQDAVMHLMRVTAGLDSLIIGEGQILSQVKQCYQLGQQYQGIGPVLNNIFKQAISAGKRVRTETQISTGAVSISSAAVELAQIKKQDLRTANITILGAGKMSRLLVQHLLSKRVKDINIVNRSVERAKLLVDQFKEANINIYNLSELKTILQNSDIVFTGTSSQEPIITPELINDCDNLPSELMLFDIAVPRNVDPNVSQFDNIKVFNVDDLKVVVSQNQQTRRKMAKAAEILLEEELSAFNIWWGSLEAIPTINKLREKAEIIRVKELEKAISRLGNEFVSDHQEIVESLTRGIVNKILHDPMVQLRAQQDIEIRGRALKILQTLFNLDTIKNGMSPTL | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 48542
Sequence Length: 432
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Subcellular Location: Plastid
EC: 1.2.1.70
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Q11Y93 | MISNFKSISLTYRKAPLEIRERVALNEAECKSLMLRIKDFTDTAELLILSTCNRTEIYYTSNEDYSNDIIKLLGVEKNITGLIQQKEYFEIYNEQADAVLHLFEVGIGLDSQVVGDMQIVNQVKYAYQWSADLNLAGPFLHRLMHTIFFTNKRVVQETAFRDGAASVSYATVELSEELLSATPNANILIVGLGEIGADVCRNFKANTSFKNITLTNRSPLKSEALAAECGIEHVPFETLWEAVAKADLVISSVAKEEPLFTKEEIQKLSILSHKYFIDLSVPRSVDARAEELPGIIVYDIDHIQNRSNEALENRLNAIPHVRKIILDSIVEFNEWSKEMEVSPTINKLKNALEQIRKEELSRFVKQLSDEEAKKVDEITKSIMQKIIKLPVLQLKAACKRGEAETLIDVLNDLFNLDKQPEQIRD | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 48224
Sequence Length: 425
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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Q1IWG2 | MPPLAPLDFAVIGLNHQTAPVEVREQAAVRAGDEGKVLQHLSRYAREVMLLNTCNRTEVYLAGLQGDPLRAFESGWGRALDGHLYVHRGEAAATHLYRVAAGLDSLVIGETQIQGQVKRAWQEAHARGLSGTLLNKVAQGALAAGKRVRSETGLSDKVVSVSSAAVELAEAALGELRHRTALILGAGETAELTLTHLRAAGVQDVIVVNRTEARARQLADKLGGRACAAEYLHEVLPEADVVIASSAAPHYVLHGEGVRAALAKRPERPIFLIDISVPRILDPDIRAVSGAHLYNLDDLTAIVSRNLQSRRAALPYAEAIIREAVADLLRWHLTREAQLGRRAVALASD | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 37531
Sequence Length: 349
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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Q1D8Z9 | MELICIGLSHRTAPLTVRERLALPESRQVDVLQRLAQAPVEALWVSTCNRVEVYLFAPDAAMARQRALMELQVLGGVEALEHLYEHQGEAALVHLFRVACSLDSMVLGEAQILGQVKEAFERGQGAGAVRGELMRACAAAFSCAKRVRTETAIGRAATSMAAAAVQLASKVFDGLAGKTVLVVGAGEMGELAARHLKQAGASKLYVTNRTLSRAEALAAEVGGQARPFEELLGLVAAADVVVCSTASQAPLFTRDNVGALGRGRRGRPLFMVDLAVPRDIDPAVGTLDWVHAYDVDDIQKFVADNAAARAEEAQKAGVLVAQEVARFVKERALREGTPVLARLRQRAEAIARSEVERTLGALGDGLNEKQRKSIEAMGRAIVNKLLHEPTARLRAVGPEGEGNRLAGAAAELFGLLEEEVGTAAAAPSVMAAPVQVATGGK | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46681
Sequence Length: 441
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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B2A1G4 | MILAVIGINHETASVETREQLAFSSKQVKELVQKLIEGQPIKEASVLSTCNRTEVHFTVNTGQIEAGKNHIMTYLSDFSDLDPREYVDHLYFITDQEAVSHIFKVTAGLNSLVTGETEILGQVKKAYQLSDEAGGVDSIFHGLYQQALRTGKRVHRETGINDNAASVSYASVELATKIFGSLQNRRALIIGAGKMSELAARHLYSNGVKDVIVINRTIERAKNLADKFGGLYASYDQLSEWLNEIDIVITSTGAPHFVIKEEQIKRAMKSRKYSPMFLIDIAVPRDVEPSVNNQDNAYLYTIDDLEAVVESNMQERQEEARNAELIISEEVAEFMVWYKTRDVVPLISALREKAEDVRKMELEKYHKKLKNLSPKEQEAVDKLTKSIVNKILKEPVLRIKEFAVEDKSELYMATLAQLFDLEDEVIPKDGEEHSSSKEVESVTQSSTERGHHESDFHN | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 51692
Sequence Length: 458
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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P56994 | MQLTAVGLNHQTAPLSIREKLAFAAAALPKAVRNLARSNAATEAVILSTCNRTELYCVGDSEEIIRWLADYHSLPIEEIRPYLYALDMQETVRHAFRVACGLDSMVLGEPQILGQIKDAVRVAQEQESMGKKLNALFQKTFSVAKEVRTDTAVGENSVSMASASVKLAEQIFPDIGDLNVLFIGAGEMIELVATYFAAKSPRLMTVANRTLARAQELCDKLGVNAEPCLLSDLPAILHDYDVVVSSTASQLPIVGKGMVERALKQRQSMPLFMLDLAVPRDIEAEVGDLNDAYLYTVDDMVNIVQSGKEARQKAAAAAETLVSEKVAEFVRQQQGRQSVPLIKALRDEGEKARKQVLENAMKQLAKGATAEEVLERLSVQLTNKLLHSPTQTLNKAGEEDKDLVHAVAQIYHLDK | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 45480
Sequence Length: 415
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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Q7RVY5 | MDSVLRQSKAVCPFMKKATASSLRAMTTAARPAASPCGGAISKLQVLAHRCPVMGKAMAVQSARTGGRASAAPASFVHKAKLHTGRPREAQAVEGVFTGQKAGLPPHPPVKPTTATAANPSPAACTVSGNFGTKFNYEKFYENELEKKHKDKSYRYFNNINRLAKDFPRAHMATKEEKVAVWCANDYLGMGRNKHVLEAMHTTLDEYGAGAGGTRNISGHNKHAVELENSLAKLHATDAALVFSSCYVANDATLATLGSKLPDCVILSDSLNHASMIQGIRHSGAKKIIFKHNDVEDLEKKLAALPLHIPKIIAFESVYSMCGSIGPIEKFCDLAEKYGAITFNDEVHAVGMYGPHGAGVAEHLDWEAHQRGETKGTIADRIDIYSGTLGKAYGCVGGYIAGSAKLVDTIRSLAPGFIFTTTLPPAVMAGARAAIEYQMSYDGDRRLQQLHTRAVKEALADRDIPVIPNPSHIIPILVGNAELAKKASDKLLNDHQIYVQSINYPTVPVGQERLRITPTPGHTKQFRDHLVAALDSIWTELGIKRTSDWAAEGGFIGVGEAEAEPVAPLWTDEQLGIADAVAELRAQASDEKKGVINQLLESVALEQEREALNAAEEVADAAKAAAASA | Function: Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
Catalytic Activity: glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA
Sequence Mass (Da): 67447
Sequence Length: 629
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Subcellular Location: Mitochondrion matrix
EC: 2.3.1.37
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A6Q3S5 | MQYLVVSFSHKNTDIVTREKLALSDDNKREDVATTLLQNPVINEAIILSTCNRIEIILSVKDPFSATEAVLKKLSEVSGINYEELEGRADIYEDNGAIHHVFSVASGLDSLVVGETQITGQIKDAYKEAYEKGWCGQKLGRVMHYAFKCSKEVRSSTDITRSPVSVASAAVSMAKEKLGNLGGMSALVVGAGEMGRLAAKHLISHGCNVILVGRDLEKTKTVAQEIDPDIRVEHVSNLQKLINSYRLLFSATSSKNPVITKDMVKEQSFDRYWFDMAVPRDIEEIYVARIHYFAVDDLKEIVNKNMAFREEQARNAYKIVGHHVNEFFKWLQTLEIDPIIKEIRKRAKDSALAELQKAIKKGYIPKEYEKSIEKLLHNAFNRFLHDPTKQLKAIADEPRADTIVEAIKFFFEIEEEVGLNRYKCEYYMNLRS | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 49015
Sequence Length: 432
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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A5GTE8 | MHLAVVGLSHRTAPVEVRERLSIPEHHLETSLQSLRSHEQVLETSILSTCNRLEIYSLLRHPEDGVEAIRDFLANHSGLADPDLQPHLFALHHEEAIQHLLRVSAGLDSLVLGEGQILSQVKKMYRLGQDHKSIGPILNRLLNQAVSTGKRVRSETNLGSGAVSISSAAVELAQLKVGQEQGVDDLVSLSQEKVAVVGAGRMARLLLQHLQSKGARSITVVNRTVAKAEVLAKDFPDLVITCCGLDQLDAQLASNTLLFTSTGADEPIIDRQRLDAITRQARLMLVDIGVPRNISSDAADVSGTLSYDVDDLQEVVERNVAARQQLAQQAEVLLDEDRQAFLDWWDGLEAVPTINRMRQQFEEIRKQELLKALSRMGSDFSQREKQVVEALTKGLINKILHGPTTALRAPQPRQQRLDSMAAAQRLFDLPGDDADRDRSDAK | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 48791
Sequence Length: 442
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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P28463 | MNIAVVGLSHKTAPVEIREKLSIQEAKLEEALTHLRSYPHIEEVTVISTCNRLEIYAVVTDTEKGVVEITQFLSETGNIPLATLRRYLFTLLHEDAVRHLMRVAAGLESLVLGEGQILAQVRTTHKLGQKYKGVGRLLDRLFKQAITAGRRVRTETDIGTGAVSISSAAVELVHRQVDLSSQKTVIIGAGKMACLLVKHLLAKGATDITIVNRSQRRSQDLANQFPQAQLTLCPLTDMFTAIAAGDIVFTSTGATEPILNCENLTGCVINRKSLMLVDISVPRNVAADVHAMEQVRAFNVDDLKEVVAQNQASRRQMARQAEALLEEEIAAFDLWWRSLETVPTISSLRSKVEDIREQELEKALSRLGSEFAEKHQEVIEALTRGIVNKILHEPMVQLRAQQDIEARKQCLRSLKMLFDLEVEEQFG | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 47526
Sequence Length: 427
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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Q47LA6 | MSVLALGLSHRSAPVTLLERVALSGEVRLKLMTEMVNTSAVNEAMVVSTCNRTEVYADVDQFHPGVAAICELLSQYTGVSQEELTQHCYVHYEERAVQHLFSVACGLDSMVVGEGQILGQVRNALKDAQHVGTLGRVLNDLGQRALRVGKRAHTETHLDKAGASMVSFGLTVAGRFLTPDREPQPSAAAAVCPVDGDTGVEVSAALPDPQLLTGRRIMVLGAGSMSALAANTVARHGASTILIANRTFDRAQRLAECLTEGYESVRSSAVPFEDAARHLADIDLVISCTGAQGIVLTAEQVAAGGDRATRPLVFLDLALPHDIDKAVRKLPGVHLVDIEELRDAAEDGTATGQVADLTAVRDIVAEEVAEYQAVRSAERVAPTVVALRSKAQKVVESELERLNGRLPGIDDRTRAEITRTVRRVVDKLLHQPTVRVKQLATGPEGAVYAEALRELFDLDPAIPSAVVKPGTALGEER | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 50977
Sequence Length: 477
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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A6LKW9 | MKLNLVGLGRNTPIYILEKFDFDEQEFFSSLKVKTTEVAVLKTCHRREIYYIGDKEPLTINEIIEPYIIRKSGIDVVRHLFKVSCGLDSMVLGEHQILSQVKNTHKNFCHGKILNKLFNEAVSLGKEARTKTGINKYPLSISYIAVKLIEEQINIEGKKIFVIGTGMMGQKVIKYLVSRGADIYISNRTIKKAYEIKKMFSEVNIVDFEEKYKHISSSDVVISATNAPHYVVEEKKVNSQKNIIFIDLSMPRNIEPSIKEYHTLYTLEDLNEISKKYNKLRQEKISTIQNLIETRIKKFLTWYKLQTVKDDILYIQNLAEKLVYEEIEKLSKKILLDDNSLKQIQKSLKSCTKKIVSYHINYIKEKVI | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 42784
Sequence Length: 368
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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B9L0Q1 | MTMTLSVVAVTHRTAPVTIRERLSLPVEQQCQWLQRWGNQVPEIVLLVTCHRTEVYWLDGEETAHRGVEWLAELGGLTVEELERWVLQRSGAEAVRHAFCVAAGLDSRVVGEPQILGQVRRARDLARAAGTLGPILDRLFSCSLATGRMVRVRAGWSTGKRSLARVAVREAARLCSDLQSARVLVLGAGETGRDVIAALCRCQPAVVWWTNRSPGRLAQIPSEEPVRIVDWSEWPRLVTEADVVFVATNAPEPIVRLEHVTRHARLPRLLVDLAVPRNVDPAISDVPGIRVVTIDDLPADPVPVAAWDGVAVEPYVERAVQRYLRWLEARSIAAEIRAAHETLQSMLERELEKVLRLALRDPARTGEVKRVAAASMARKTLFPLFRALESEPQRVALALRLLAYDR | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 45246
Sequence Length: 406
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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Q5SI68 | MALPLYLVGLSHKTAPLEVRERAALDPVVALPAALSALGKGVVLSTCNRTELYGVGSPEKARAFLLSRGVAPRHLYVKEGVEALRHLYRVAAGLDSLVVGEAQILGQVREALFLARRQGATESLLEKAFQSAIALGKRARSETGIGMGAVSVAYAALDLALAVYGDLSGLSVAVLGAGEMAELFLTHLKAHGVGRILVVNRTEEKAQALAERFGGEAFGLPALPQVLRQADLVVASAAAPHYLVGPEDLPKRAKPLFLIDIALPRNIDPRVGDLPHAYLYNLDDLKRVVDRNLRARAGEIPKVEALIEKALGDYMEWYAGHRVREAIRALEAWARVQAAKAQPEAGPVELEKAAGRLAHPFILGLKRRALDRVGGPPCPEDCLLYRLSRT | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 41937
Sequence Length: 390
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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Q97B68 | MLMNIVTLISWDFKRNNESFQRAIINGYDYWSRILDDHGVEKYVILLTCNRVELYYRGDPFDVQEKGYNIISDDMAINHLFHVAAGLDSMSIGENEVLKQVKQAYEKSSSMGKSDKFLSLIFQRAISVGKLVRSKTGIGKGKVSIPSIVYDIVRKNGGNKILLVGNGMLASEIAPYFSYPQYKVTVAGRNIDHVRAFAEKYEYEYVLINDIDSLIKNNDVIITATSSKTPIVEERSLMPGKLFIDLGNPPNIERGNNVITLDEIYEISKKNEMLREEKINQAEILIENEMKATMNKIKDLMIDDIFSQFYRFASVVQTMEIQKFRKMHPEVNENDLEALAHSIINKILNVPVTTLKAVSRSQGNSDFNRLFESFSSNFNDIVSAALQSYEGLRDTQSLRDRTRQLLQKS | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46691
Sequence Length: 409
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
EC: 1.2.1.70
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P28464 | MKKEIIIGTRSSPLALWQAEFTKAELSKRFPDMNITLKLVKTTGDVLLDSPLSKIGDMGLFTKDIEKHLLAGEIDLAVHSLKDVPTGTPEGLVITSFTEREDTRDVIISKSGKGLMDLPQNAKMATSSLRRMSQLLSLRPDLEIMDIRGNLNTRFKKFDEGDFDAMMLAYAGVYRLEFSDRITEILPHETMLPAVGQGALGIETRTDDAETREIVRVLNDDNTEMCCRAERALLRHLQGGCQIPIGSFGSYIDGTLKLLAFVGSVDGKTGLRNEVTKAVKTPEEAEAVGIELAEILLSMGAEKILADIRKTC | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 34358
Sequence Length: 312
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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Q9Z9C9 | MLSVCYSDPCLSDFCQGKRPLRIASRNSNLAKAQVHECISLLRSWYPKLWFQLSTTETTGDREKKIPLHLVENSYFFTDGVDALVHKGVCDLAIHSAKDLPETPSLPVVAITRCLHPADLLVYADHYVHEPLPLSPRLGSSSLRRSAVLKQLFPQGQILDIRGTIEERLDQLHRGHYDAIVLAKAASLRLHLHHAYSIELPPPYHALQGSLAITAKDHAGKWKQLFTPIHCHSS | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 26244
Sequence Length: 234
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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B3QWI1 | MKKALIIGTRSSPLALWQAEFIKAELSKHYPSLDISLRHIKTTGDKILDAPLAKIGDKGLFTREIEHVMLRNEIDLAVHSLKDLPTETPEGLVITAITEREDNRDVLISKGKYTLKTLPQGAIVATSSLRRRSQLLHLRPDLEVIDMRGNLNTRFKRFEEGDAEAMLLAFAGVHRLEFSEHIAEIISFDDILPAVGQGALGIETRIDDEETRELLKVLNHAETELCTKCERSLLRTLEGGCQIPIGAHARIENGTFHFATYVGSIDGKRAIKKSLSRENVTTVEEAEQIGIEVADAARAAGANEILCEIRTDNA | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 34805
Sequence Length: 314
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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O84301 | MLSAYYNDPFLADFCLGNIPLRLASRQSSLAVLQAHECLRKLQIFFPRLWGQIITTTTQGDLDQETPLCAVENTGFFTDDVDFLVQSGQCDLGIHSAKDLPENPKATVVSITASIDPRDILVFHEKYLSIPLPRRLRIGSSSVRRKELLSLLYPSAIITDIRGTIQTRLKLLEEKNFDAIVMANAAVSRLGLRLPCTKILPPPYHPLQGRLAITASRHIRSWRGLFLTCGITEDVEIMCFS | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 26996
Sequence Length: 241
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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Q6L2G8 | MHIRIGTRSSKLAMIQAMMVKDRLDSLGIETEVKGFTSKGDINLDSPLYSIGGTGVFVDDLNRMILKNEIDIAVHSAKDIPSFIDDSLEISAVLKRDDPRDVLISQHSLNDLEASSVIGTSSLRRIKELKTLRNDILIKDLRGNIDTRLKKLDNGDYDGIIMAKAAYDRMRINRRHFILNYDDFVPAPNQGIIAIISKKDSEINDVLKKINDDETYNDMKAERLILSGLNLGCSKPVGIYAHKNRIFMRFYSLKNDDYKDIVMDYNNIDLEFIRSEIHDYGY | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 32137
Sequence Length: 282
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
EC: 2.5.1.61
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Q8UD80 | MERPILPKGLPEDIEDKKAVAQAWFQHLRDTIVASFETLEDELTGPLSDQEPGRFVQKDWLRDNGEGGGGKMSMMEGRVFEKVGVHTSTVYGEFSPEFRKQIPGAEEDPRFWASGLSLIAHPVNPNVPAVHMNTRMVVTTSHWFGGGADLTPVLGRRRTQQDPDTQLFHRAFEITCNRHPIADYPRYKSWCDEYFFLKHRDEPRGTGGIFFDWLHPDEEKGGWDANFTFVQDVGRAFNLVYPKIVRANFNQNWTEEDRDEQLIRRGRYVEFNLLYDRGTIFGLKTGGNVESILSSLPPVVRWP | Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass (Da): 34800
Sequence Length: 303
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.3.3
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Q7VWE7 | MTAVAIPAVRDYLTDLQGRIVAALEQAGGEAFRTDAWQRAEGGGGVSRLLEGGQLFERAGVLFSHVKGTRLPPSASAHRPELAGRGWEAMGVSMVLHPRNPYVPTTHMNVRMFVAAARPGHAESDVFWFGGGLDLTPYYPFEDDARHFHRACRDALDPHGADYYPRYKQWCDEYFFLKHRNETRGIGGIFFDDLNEPGFDASFALTCSVGDSFLPAYLPIVQARRDMPYGERERDFQAYRRGRYVEFNLVFDRGTLFGLQSGGRTESILLSMPPLAQWRYDWQPQAGTPEAALAEFLRPREWV | Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass (Da): 34185
Sequence Length: 303
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.3.3
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Q8DL15 | MTVATSASTAVPSDSRQRVATFLKDLQDQICQGLEAADGGAQFQEDTWQRPEGGGGRSRVMKNGQLLEQGGVNFSEVWGEQLPPSILAQRPEAAGYGFYATGTSMVLHPRNPYVPTVHLNYRYFEAGPVWWFGGGADLTPYYPFAEDAKHFHQVHQAACDRHHREYYPVFKRWCDEYFYLKHRGETRGVGGIFFDYQDGSDRELYRGPNPDGEAARYSQRVGSIGSRSWEDLFAFIQSCGQAFLEAYLPIVERRRHLTYGDRERQFQLYRRGRYVEFNLVYDRGTIFGLQTNGRTESILMSLPPLVRWEYGYTPEPNSREAELYSTFLKPQDWVNWPV | Function: Involved in the heme and chlorophyll biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass (Da): 38882
Sequence Length: 338
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.3.3
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P07976 | MERTVIALAIISVVKGDQICIGYHANNSTKQIDTIMEKNVTVTHAQDILEKKHNGKLCSLKGVKPLILKDCSVAGWLLGNPMCDEFLNAPEWSYIVEKNNPINGLCYPGDFNDYEELKHLVSSTNLFEKIRIIPRNSWTNHDASSGVSSACPHLGRSSFFRNVVWLIKKNNVYPTIKRTYNNTNVEDLLILWGIHHPNDAAEQAKLYQNLNAYVSVGTSTLNQRSIPKIATRPKVNGQSGRMEFFWTILRPNDTISFESTGNFIAPEYAYKIVKKGDSAIMRSELEYGNCDTKCQTPLGAINSSMPFHNVHPLTIGECPKYVKSDKLVLATGMRNVPQKKKRGLFGAIAGFIEGGWQGMVDGWYGYHHINGQGSGYAADKKSTQKAIDGITNKVNSIIDKMNTQFEAVGREFNNLERRIENLNKKMEDGFIDVWTYNAELLVLMENERTLDLHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYNYPKYSEESKLKRKEIDGIKLESMGTYQILSIYSTVASSLALAIMVAGLSFWMCSNGSLQCRICI | Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
PTM: Palmitoylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63577
Sequence Length: 564
Subcellular Location: Virion membrane
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P12590 | MKAKLLVLLCAFTATDADTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCRLKGIAPLQLGNCSIAGWILGNPECESLFSKKSWSYIAETPNSENGTCYPGYFADYEELREQLSSVSSFERFEIFPKESSWPNHTVTKGVTAACSHKGKSSFYRNLLWLTEKNGSYPNLSKSYVNNKEKEVLVLWGVHHPSNIGDQRAIYHTENAYVSVVSSHYNRRFTPEIAKRPKVRGQEGRINYYWTLLEPEDTIIFEANGNLIAPWYAFALSRGFGSGIITSNASMDECDAKCQTPQGAINSSLPFQNVHPVTIGECPKYVRSTKLRMVTGLRNIPSIQSR | Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
PTM: In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in lungs by club cells (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38434
Sequence Length: 344
Subcellular Location: Virion membrane
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A0RNU4 | MKKVVILLNMGGADDLSQVELFLKNMFNDPYILGIKNRKIRSVLAWLITKMRLKSATRNYTELGGKSPIGDITRSLIDKLNIKFGNENLTFDYAMNYTPPFAIDSLKKYKYADEILLFPLYPHHSRTTIVSSLDSANRAIKELSIKSNIKVINYFYKDERYNKIITSSIKEKIAEMNSSQIDLIFSSHSLPKKIIEKGDLYETHTNEHVKIISDMLAKDGVKFNSISLAYQSRLGPVEWLGPNLSEVLSNLKSKKALIYPISFCIDNSETDFELDIEYRKIADQKEFDYYEVVKAPDDSEAFVDYIAYKVKELV | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 36077
Sequence Length: 314
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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Q9PI08 | MKLVLFLNMGGATNLQDCEVFLKNMFNDPYILGIKNRFLRKFVAWIITKARVKAMQENYKKMGGKSPLNELTQSLCDKLNLKQDEFKFDFVNLYVPPFATEILQKYTLNASDEIILFPLYPHHSCTTVTSSLEVLQNEISKQKIQAKVKTIDIFYKNELYNEMIVSHILAKKSKFDAKILIFSAHSLPQSIIDKGDLYEKHVNDHVEILKEKLKDHFDEFILAYQSKLGPVKWLEPNTSDVLANLNDKALIYPISFCIDCSETIFELGMEYKHLSKYNYDLISCPNDSDEFMEFILKYLSDLN | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 35202
Sequence Length: 303
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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P57777 | MTQKLAVVLFNLGGPDGPDAVRPFLFNLFRDPAIIGAPALIRYPLAALISTTREKSAKANYAIMGGGSPLLPETEKQARALEAALALAMPGVEAKCFIAMRYWHPLTDETARQVAAFAPDQVVLLPLYPQFSTTTTGSSLKAWKKTYKGSGVQTTVGCYPTEGGLIEAHARMIRESWEKAGSPTNIRLLFSAHGLPEKVILAGDPYQKQVEATAAAVAAHLPPQIEWTVCYQSRVGPLKWIGPSTDDEIRRAGGEDKGVMITPIAFVSEHVETLVELDHEYAELAEEVGAAPYLRVSALGTAPEFIDGLAKAVRDSVGKAPGTVSSACGWRCGADWSKCPCREGASA | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 37121
Sequence Length: 347
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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O42479 | MAAAGRAARPLVAGGRQLRVPLRWRGQVAAAAPSTKPQAEPETRKPKTGILMLNMGGPERLDDVHDFLLRLFLDRDLMTLPAQNKLAPFIAKRRTPRIQEQYSRIGGGSPIKKWTAVQGEGMVKLLDSMSPQTAPHKYYIGFRYVHPLTEEAIEEMEDDGIERAIAFTQYPQYSCSTTGSSLNAIYRYYNKKGKKPKMKWSIIDRWPTHPLLIQCFADHIQKELDLFPPDKRKDVVILFSAHSLPMSVVNRGDPYPQEVGATVQRVMEKLNHSNPYRLVWQSKVGPMPWLVPQTDETIKGLCQRGKKNMLLVPIAFTSDHIETLYELDIEYAQVLANECGVENIRRAESLNGNPLFSKALADLVCSHIQSNEICSKQLTLCCPLCVNPVCRETKAFFTNQQL | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45430
Sequence Length: 402
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Mitochondrion inner membrane
EC: 4.98.1.1
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A1ASJ7 | MVIDRTAVLLLQMGGPDSIEAVEPFLRNLFSDRDIIRIGPAFLQPLIARLIARRRSKRVAEQYRQIGGGSPLRKLTEQQAAELEKVLGEGYRCFVAMRYWKPDTSQALEAVVQAGITRIVALSLYPHYSRATSGSSFNELERVRARSATPFQVTCVRQFHDHPLYITSLCDRIGQALSGYADPGDVHLLFTAHGLPQSFIDSGDPYLDQIRATVALVMERFGGINHHLAFQSRAGPVKWLEPSTEKKIRELAGQGVKKLLMVPVSFVSDHIETLHEIDMQYRHEALELGIEDFRRVESLNSSPLFIDCLAELVRGGDRTEET | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 36169
Sequence Length: 322
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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Q4FNS1 | MKKAVILFNLGGPDKIENVEPFLFNLFNDPAILNLPTILRYPLAKLISNRRAPVAKKIYKELGGSSPILKLTMAQSKALETKLNQTEIDSEYKCFIVMRCWNPRANDVIKDVQSFNPEEIILMPLYPQYSAATSGSSIKEWRDVCKKNNYHVKTNTICCYPTDQNFINAHTKEIIKKIKDLKNFKLIFSAHGLPEKNIKKGDPYQWQVEQSVKKIVENLNIENLDWILSYQSRVGPLKWIGPSTEDIIVENSKLAKHIVLVPIAFVSEHSETLVELDIEYKEIADANGCKNYTRVPALGTNEDFIKAMSELIIKKNEYKFSENLYPPKIQCPSNFKKCPCLNYE | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 39436
Sequence Length: 344
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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B2RHB4 | MADRRRTDDNKGAREVVLLLNIGSPDSPEVKDVARYLNSFLTDRRIITLPFLLRQLLVRGIITPFRKKSSAQKYRTVWDESTRSFPLISHTKAIARALAHTGRDVHVAMRYGKPTVADVLKELPHGRSLVVLPLFPHYAMSSYETAVEHCKAEIRRLCPNLSFRVVQPFYAHEAYIRVLADNIRPYLTKPFDKLILSYHGIPRDHLDKTTRQALDLRHPEGCCTEEDPTANVCYRYQTYRTTALIREALCLAEEQVEQVFQSRVGHTEWLRPYLIERLSAWPQEETKRILIACPSFVCDCLESLEEVADHGQSIFKKAGGADFTYIPCLNSGANWIDALRNILEE | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 39594
Sequence Length: 345
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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Q7MXP4 | MADRRRTDDNKGAREVVLLLNIGSPDSPEEKDVARYLNSFLTDRRIITLPFLLRQLLVRGIITPFRKKSSAQKYRTVWDESTRSFPLISHTKAIARALAHTGREVHVAMRYGKPAVADVLKELPHGRSLVVLPLFPHYAMSSYETAVEHCKAEIRRLCPNLSFRVVQPFYAHEAYIRVLADNIRPYLTKPFDKLILSYHGIPRDHLDKTTRQALNLRHPEGCCTEEDPTANVCYRYQTYRTTALIREALGLAEEQVEQVFQSRVGHTEWLRPYLIERLSAWPQEETKRILIACPSFVCDCLESLEEVADHGQSIFKKAGGADFTYIPCLNSGANWIDALRNILEE | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 39561
Sequence Length: 345
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.98.1.1
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P16645 | MIDTAMARLNEGTIVIYALSVLFYFIDFLQHNRKAGKMAFWLLSIVWTLQTVYLAYFMWVTGRFPVLNVTEALYFYAWVLVTLSLVLTKLLRVDFIVFFTNVIGFSMIAIHTFSPTEQQSAAFSGQLVSELLVIHITMAILSYGAFSLSFVFSVLYMFQYHLLKKKKWGKWLLRIEDLSKLDYMAYVLNVIGVPMLLLSLILGVIWAYVSLETLYWFDAKVLGSFVVLLLYSYYLYIRLIKELQGKVAALWNTACFLVLMINYFLLGSLSQFHWFS | Function: Required for HemL synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32051
Sequence Length: 276
Subcellular Location: Cell membrane
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O69103 | MAEVRWIYDLTIFLYAASVLFYFNDFLQSNRKVNRLAFGLLVVVWALQTAFFVSQAVMKGYFPVITLFETLFFYSWVLVGLSLAIHYFFRIDLLVFLPNIIGFVVLVMSMFLPETPIEAVSSILTSELLLTHVTLAMFSYGAFSLSMIFSAMYLLQHKMLKGRRWSPLLRRLPSLDQLEGYAYRMNMLGVPMLLLSIVLGIIWGKMVLGEKFLLDSKVLLSELVLAIYSLWLYQRYRIRCRCADSSQWNVLAFLLLLINFLGFTTSTFHDWW | Function: Required for HemL synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31643
Sequence Length: 272
Subcellular Location: Cell membrane
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B2AXJ5 | MPTKTSQHAFAGSERWVVPRYSSKPGTLIRLGSVLTDPEDLESSLNLDSIPPIPPHLLRDATPEVRMSVQTELSKSDSTLAKAAPALEGILTLGGGVEASRSQGVSSSLNISGTVKATVFRADKSYMDVLLKDKNVISYAKRGLGKPMFVVVGVATAGRVEMKETRHVTRKAGVSGKVGVEVIGEGEVGLERERSDKSCNEVRGEGGLDFAYRVREFGYSRVRGTVKDKGDWTGKVLFAGGKGPVVEKGGEVVPVFKEFKEGEVKLRATGSFDVAAKA | Function: Gasdermin-like protein involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition) . In P.anserina, the het-q locus exists as 2 incompatible alleles, het-Q1 (this entry) and het-Q2 (AC P0DW09) . This form constitutes the precursor of the pore-forming protein: during the allorecognition process, it is cleaved by het-Q2, releasing the N-terminal moiety (Gasdermin-like protein het-Q1, N-terminal) that binds to membranes and forms pores, triggering cell death .
PTM: The precursor form is cleaved by het-Q2, generating the pore-forming protein (Gasdermin-like protein het-Q1, N-terminal).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29695
Sequence Length: 278
Subcellular Location: Cell membrane
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P0DW09 | MSAISHHSLSHLNSTVSKRLMPTYSDPVVRIAVLDTGFDGSHPDFSHPRTAYFTGPFSDLPQPEKDEEPQLTRIKAYHDFCQPSPPGDRQGPPPQPHSMVDLAGHGTAIAGLILRLAPRAELVIGRVCHGVDSNELSAPDPSRVAAAIRWAITQKVHIINLSLGYRNQPLKELLPLRAALLEAQRSNILVFASTSNQGSHEPAAWPASDARFAIGVHSCNDMGSAPSGSSCKASENGYNFMAVGENLLVHRLAQKGGGFELVSGSSFATPVVVSVAALVLAFVWQEECKRERDEVGREVMLEDLGSLGGMGRVLMALGEKTAGSYWAVGMKLFWAGYREGDGRDPEKEEKEARRWAWGVLRGAVAY | Function: Serine protease involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition) . In P.anserina, the het-q locus exists as 2 incompatible alleles, het-Q1 (AC B2AXJ5) and het-Q2 (this entry) . Prevents cell fusion with strains containing the gasdermin-like protein het-Q1 by mediating proteolytic cleavage and maturation of het-Q1 during the allorecognition process, thereby triggering cell death .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 39643
Sequence Length: 366
Subcellular Location: Membrane
EC: 3.4.21.-
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P27709 | MSNDIDLIKRLGPSAMDQIMLYLAFSAMRTSGHRHGAFLDAAATAAKCAIYMTYLEQGQNLRMTGHLHHLEPKRVKIIVEEVRQALMEGKLLKTLGSQEPRYLIQFPYVWMEQYPWIPGRSRIPGTSLTSEEKRQIEHKLPSNLPDAQLVTSFEFLELIEFLHKRSQEDLPPEHRMELSEALAEHIKRRLLYSGTVTRIDSPWGMPFYALTRPFYAPADDQERTYIMVEDTARYFRMMKDWAEKRPNAMRALEELDVPPERWDEAMQELDEIIRTWADKYHQVGGIPMILQMVFGRKED | Function: Controls heterocyst differentiation. Dimerization is required for DNA-binding. Has both a protease and a DNA-binding activity.
PTM: Probably autodegrades.
Sequence Mass (Da): 34969
Sequence Length: 299
Domain: Has an N-terminal DNA-binding domain that inserts into the DNA major groove, a central flap domain and C-terminal hood domain. The hood domain binds the PatS6 peptide. Upon PatS6 binding the flap domain probably moves considerably.
EC: 3.4.21.-
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Q03689 | MSEPFGIVAGALNVAGLFNNCVDCFEYVQLGRPFGRDYERCQLRLDIAKARLSRWGEAVKINDDPRFHSDAPTDKSVQLAKSIVEEILLLFESAQKTSKRYELVADQQDLVVFEDKDMKPIGRALHRRLNDLVSRRQKQTSLAKKTAWALYDGKSLEKIVDQVARFVDELEKAFPIEAVCHKLAEIEIEEVEDEASLTILKDAAGGIDAAMSDAAAQKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDN | Function: Responsible for heterokaryon incompatibility, a process that ensures that during spontaneous, vegetative cell fusion only compatible cells from the same colony survive (non-self-recognition). Forms a prion for the non-Mendelian trait [het-s]. Interacts with het-S from incompatible cells to trigger a lethal reaction that prevents the formation of viable heterokaryons. It is unknown if the native, soluble protein has a cellular function.
Sequence Mass (Da): 31978
Sequence Length: 289
Domain: The globular domain is dispensable for prion formation and incompatibility function. However, the het-S globular domain, but not the het-s globular domain, is essential for programmed cell death.
Subcellular Location: Cytoplasm
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P43082 | MKIRLSITIILLSYTVATVAGQQCGRQGGGRTCPGNICCSQYGYCGTTADYCSPTNNCQSNCWGSGPSGPGESASNVRATYHFYNPAQNNWDLRAVSAYCSTWDADKPYAWRSKYGWTAFCGPAGPRGQASCGKCLRVKNTRTNAAVTVRIVDQCSNGGLDLDVAMFNQIDTDGFGYQQGHLIVDYQFVDCGNELIGQPDSRNMLVSAIDRV | Function: Fungal growth inhibitors. Neither CB-HEL nor CD-HEL have chitinase activity, but both have antimicrobial activities. CD-HEL has RNase, but no DNase activity.
Sequence Mass (Da): 22937
Sequence Length: 212
Domain: The C-terminal vacuolar sorting signal (VSS) (194-212) is required for vacuolar localization.
Subcellular Location: Vacuole
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D4AUH6 | MLWIWVPGILGLFGRVEALWPQPSEYSHGNKTLWLSPSVRFTYTNNQRSFIYTRPSYAGINWIPGGWLNLLQNPWGSAEQTVAEPLPNVEQFVEDAIKRTKHAIINSKFVPWKFHPRHQKFEPLVDGQHPTIEEVIINEASKTSQEWSPRNYVNGDEKYEIRISEDGEVQISSRSPIGTIRALQTFQQLFYSHSHSKSYTPFAPISISDSPKWRHRGLNLDISRNVIRPEDVKRTIDAMASVKLNRLHAHAADSQSWPLDIPSIPELAAKASYHPSQVWSSSELEAVQLYGLERGVSVFLEIDLPGHTAAVGHAFPDLVAAYHMDQWEKYAAEPPSGQIKLNSSAVYQFLDLLMADLIPRVSPLTEYFHTGGDEFNLNTYLLEINLGSNDRRVLTPFLDRMITHVHSSLRSSGVTPIVWEELVLDWDLNLPSHKTAGETGGVIVQAWRNSSAVKHVLQKGYQTIFGTGDAWYLDCGVGTFLNPRPGSKAVQNPYLDWCAPTKNWKHMYVYNPLKDIPVELQSLLVGGETHMWSELVDPVNMDQMIWPRAAAAAEVLWTGPRSPDNIQDASYRLAKWRERVVNDAGIRAAMVQMTYCLMRESGCEL | Function: Beta-hexosaminidase that shows a broad substrate specificity (By similarity).
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 68518
Sequence Length: 605
Subcellular Location: Secreted
EC: 3.2.1.52
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P43077 | MVLDKMIIFHLLLWLCNVVVHAAKVEILPAPQSVTWENDTAIIINPRLLQANTSCPLLEDAFVRTVSAIEKSKWHPFPIDDFNTANGKNIKTSLVHIQVDDATVDLQLGVNESYTLKINTDGINIHAATTWGALHGLVSLQQLIIHTSEDKYVVPSSVTISDFPNFKHRGLMIDSGRNFLTVDSILEQIDIMALSKMNSLHWHLADSQSWPVALESYPHMIKDAYSNDEVYSKNDLKYIVDYARARGVRVIPEIDMPGHARAGWKQVDPTIVECADAFWTDAAVEPPPGQLNIESEKTYEVISNVYNELSDIFIDDVFHVGNDELQEKCYSAQLSPNNTVTDLLKRYLKKALPIFNKVNHRKLTMWDDVLLSDVSADKIPSNITLQVWHEISGVKNLTSRGYDVVVSSSDFLYLDCGNAGWVTNDPRYVETPENVDFNTGQGGSWCGPYKSYQRIYNFDFTANLTETEKNHVLGREAALWSEQVDSTVLTTKIWPRTAALAELTWSGNKDSNGHHRGYEFTQRILNFREYLVKLGYGVSPLVPKYCLLNPHACDLYKNPPVY | Function: Has a broad substrate specificity.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 63491
Sequence Length: 562
EC: 3.2.1.52
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P96155 | MNYRIDFAVLSEHPQFCRFGLTLHNLSDQDLKAWSLHFTIDRYIQPDSISHSQIHQVGSFCSLTPEQDVINSNSHFYCEFSIKTAPFPFHYYTDGIKAAFVQINDVEPRVRHDVIVTPIALASPYRERSEIPATDAATLSLLPKPNHIERLDGEFALTAGSQISLQSSCAETAATWLKQELTHLYQWQPHDIGSADIVLRTNPTLDEGAYLLSVDRKPIRLEASSHIGFVHASATLLQLVRPDGDNLLVPHIVIKDAPRFKYRGMMLDCARHFHPLERVKRLINQLAHYKFNTFHWHLTDDEGWRIEIKSLPQLTDIGAWRGVDEVLEPQYSLLTEKHGGFYTQEEIREVIAYAAERGITVIPEIDIPGHSRAAIKALPEWLFDEDDQSQYRSIQYYNDNVLSPALPGTYRFLDCVLEEVAALFPSHFIHIGADEVPDGVWVNSPKCQALMAEEGYTDAKELQGHLLRYAEKKLKSLGKRMVGWEEAQHGDKVSKDTVIYSWLSEQAALNCARQGFDVILQPGQFTYLDIAQDYAPEEPGVDWAGVTPLERAYRYEPLVEVPEHDPLRKRILGIQCALWCELVNNQDRMDYMIYPRLTALAGSGLDTKIPA | Function: Hydrolyzes aryl-N-acetyl-beta-D-glucosaminide (aryl-beta-GlcNAc), aryl-beta-GalNAc and chitin oligosaccharides. Can hydrolyze rapidly the artificial substrates p-nitrophenyl-N-acetyl-beta-D-glucosaminide (PNP-beta-GlcNAc) and 4-methylumbelliferyl-beta-GlcNAc, and is slightly active on p-nitrophenyl-beta-GalNAc. This enzyme is not processive, i.e. when it hydrolyzes (GlcNAc)n, both products, (Glc-NAc)n-1 and the terminal GlcNAc, are released before the enzyme attacks a second molecule of (GlcNAc)n or (GlcNAc)n-1.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 69502
Sequence Length: 611
Pathway: Glycan degradation; chitin degradation.
Subcellular Location: Periplasm
EC: 3.2.1.52
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Q7WUL4 | MPDVAVIPRPVLLETTDGPPFVLTAATILVVDSAPELVAVGVLAADLLGRLSGRPVEVRYTEGGAPSVVRLRLSEDLPAGDEAYRLVVSEHRVDIDARSAAGLVRAVVTLRQTVSSLGDGTLTVPALRVEDHPRYAWRGLSIDVARHFFTVDDLKAIIGLLAHYKLNVLHLHLTDDQGWRVHLPSRPHLTRASAGTSVGGGPGGFYNPAQLAEIVVARAARGIRVVPEIDVPGHVNAATHAYGDLTPSGEPTDVYTGIEVGFSRLHDDLPATRPFLRDVFTDLAAMTPGEYVHIGGDEVLTMDHDKYARLVGYAASVVRDAGKKVVGWQEISSTPLEPGTVVQYWDINADPAPFVAAAQAGAHVLMSPGSRAYLDMKYDATTELGLEWAGHIELRDAYDWEPSTLIPGVPPESVIGVEAAVWTETLTDLGELTSMLLPRLAAVAEVAWTAPQDRDWDDFSGRVAQHAPFWDRVGFRWHASPQVSWPGPGSAPGAAF | Function: Catalyzes the cleavage of beta-N-acetylglucosaminides and beta-N-acetylgalactosaminides. Also catalyzes the hydrolysis of N-acetylchitooligomers. May be involved in chitin degradation. It is not able to cleave beta-glucosides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 53326
Sequence Length: 496
Pathway: Glycan degradation; chitin degradation.
EC: 3.2.1.52
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Q7XHZ0 | MAFLVERCGEMVVSMEMGPHGGGGAAAGKPVPAPFLTKTYQLVDDPCTDHIVSWGEDDTTFVVWRPPEFARDLLPNYFKHNNFSSFVRQLNTYGFRKIVADRWEFANEFFRKGAKHLLAEIHRRKSSQPPPPPMPHQPYHHHHHLNPFSLPPPPPAYHHHHLIQEEPATTAHCTVAGDGGEGGDFLAALSEDNRQLRRRNSLLLSELAHMKKLYNDIIYFLQNHVAPVTTTTTTPSSTAMAAAQHHLPAAASCRLMELDSPDHSPPPPPPKTPATDGGDTVKLFGVSLHGRKKRAHRDDDDGVHDQGSEV | Function: Transcriptional activator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 34451
Sequence Length: 310
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Nucleus
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Q67U94 | MERCGSWSDCEAAAAAAQKAVPAPFLTKTYQLVDDPATDHIVSWGDDRVSTFVVWRPPEFARDILPNYFKHNNFSSFVRQLNTYGFRKVVPERWEFANEFFRKGEKQLLTEIHRRKTSSASTASPSPPPFFAPPHFPLFHHPGVAAAQHHHAFVGDDGVVAAHGIGMPFPQPHWREPNLPVATRLLALGGPAPSPSSAEAGGAGRAATAAVLMEENERLRRSNTALLQELAHMRKLYNDIIYFVQNHVRPVAPSPAAAAFLQGLGMQARKKPAAANVLNNSGGSTTSSSSLTIAEEPSPPPQQQHLAGEKSGGEAGNSSAARSSAPTKLFGVHLSAAPCGAGSKRASSPEEHPPTSPATKPRLVLECDDLSLTVAPSSSSQQQLSAASSPTSTS | Function: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 42036
Sequence Length: 394
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Cytoplasm
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Q10KX8 | MAFLVERCGGEMVVSMERSHGRSTTTAAAVTAAPAPFLSKTYQLVDDPSTDDVVSWGEDEATFVVWRPPEFARDLLPNYFKHNNFSSFVRQLNTYGFRKIVADRWEFANEFFRKGAKHLLSEIHRRKSSSCSQPQPPPPFPMHQHYPLSLFSPPTTPRSPPVGAAAAAAYHFQEEYCSSPADYAGGGGDLLAALSEDNRQLRRRNSLLLSELAHMRKLYNDIIYFLQNHVEPVAPPPLAAATSCRLVELGPSTTERRRCAASPSGDNDDDAAVRLFGVRLDDDHGKKRRVQLVQEDEGDEQGSEG | Function: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 33951
Sequence Length: 305
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Nucleus
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Q6VBA4 | MDGLHTELALGLIGCCGGDGQQQTAPFVAKTYQMVCDPRTDALVRWGRDNNSFVVVDPAAFSQLLLPCFFKHGNFSSFVRQLNTYGFRKVHPDRWEFAHESFLRGQTHLLPRIVRRKKRGEGGGGGGGASCSFGGGAGEHQVAAAAASVGMSGEEEDAAEDVLAKEAALFEEVQRLRHEQTAIGEELARMSQRLQATERRPDQLMSFLAKLADDPNAVTGHLLEQAAERKRRRQHLPSHEPTVCPLPPAPPPQPPQPLLALAGAAAMDGTYWWTTEHHHHHHHQMKPMTVLPSLEPPTASCGVHQVPELGGGGVMGLTTDGEAKVEPPFPFCLLGQAFF | Function: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 36863
Sequence Length: 339
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Nucleus
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Q942D6 | MMGGECKVHQLQAAGDGGPGAVAPFVAKTFHMVSDPSTNAVVRWGGAGNTFLVLDPAAFSDFLLPSYFKHRNFASFVRQLNTYGFRKVDPDRWEFAHESFLRGQAQLLPRIVRKKKKGGAAPGCRELCEEGEEVRGTIEAVQRLREEQRGMEEELQAMDQRLRAAESRPGQMMAFLAKLADEPGVVLRAMLAKKEELAAAGNNGSDPCKRRRIGADTGRGGVATGGDAAEMAQSRGTVPFPFSVLGQVFY | Function: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 27219
Sequence Length: 250
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Nucleus
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Q0DBL6 | MAAAAGGGAAPFVWKTYRMVEDPGTDGVIGWGKGNNSFVVADPFVFSQTLLPAHFKHNNFSSFVRQLNTYGFRKVDPDRWEFAHASFLRGQTHLLRNIVRRGSAAAGGGGGGGGGKRRDASADGGGGGGDEDMTMVATEVVRLKQEQRTIDDRVAAMWRRVQETERRPKQMLAFLLKVVGDRDKLHRLVGGGGNGNGAATAAAADNGFADAARAGCGEKRARLLLDGDNTGAFGPDAVDFAGFYTGADMFPDVAVDAAAAAAGGSAGCSFAFGVDSGY | Function: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 28971
Sequence Length: 278
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Nucleus
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Q04458 | MSNDGSKILNYTPVSKIDEIVEISRNFFFEKQLKLSHENNPRKKDLEFRQLQLKKLYYAVKDHEEELIDAMYKDFHRNKIESVLNETTKLMNDILHLIEILPKLIKPRRVSDSSPPFMFGKTIVEKISRGSVLIIAPFNFPLLLAFAPLAAALAAGNTIVLKPSELTPHTAVVMENLLTTAGFPDGLIQVVQGAIDETTRLLDCGKFDLIFYTGSPRVGSIVAEKAAKSLTPCVLELGGKSPTFITENFKASNIKIALKRIFFGAFGNSGQICVSPDYLLVHKSIYPKVIKECESVLNEFYPSFDEQTDFTRMIHEPAYKKAVASINSTNGSKIVPSKISINSDTEDLCLVPPTIVYNIGWDDPLMKQENFAPVLPIIEYEDLDETINKIIEEHDTPLVQYIFSDSQTEINRILTRLRSGDCVVGDTVIHVGITDAPFGGIGTSGYGNYGGYYGFNTFSHERTIFKQPYWNDFTLFMRYPPNSAQKEKLVRFAMERKPWFDRNGNNKWGLRQYFSLSAAVILISTIYAHCSS | Function: Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid . Involved in coenzyme Q (CoQ) biosynthesis, catalyzing the last step in the tyrosine to 4-hydroxybenzoate (4-HB) pathway. Oxidizes 4-hydroxybenzaldehyde (4-Hbz) to 4-HB, the aromatic precursor for coenzyme Q .
Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59979
Sequence Length: 532
Subcellular Location: Lipid droplet
EC: 1.2.1.3
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Q30201 | MGPRARPALLLLMLLQTAVLQGRLLRSHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDHESRRVEPRTPWVSSRISSQMWLQLSQSLKGWDHMFTVDFWTIMENHNHSKESHTLQVILGCEMQEDNSTEGYWKYGYDGQDHLEFCPDTLDWRAAEPRAWPTKLEWERHKIRARQNRAYLERDCPAQLQQLLELGRGVLDQQVPPLVKVTHHVTSSVTTLRCRALNYYPQNITMKWLKDKQPMDAKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQVEHPGLDQPLIVIWEPSPSGTLVIGVISGIAVFVVILFIGILFIILRKRQGSRGAMGHYVLAERE | Function: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40108
Sequence Length: 348
Subcellular Location: Cell membrane
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Q09906 | MDNEIVALCGFFVAIALVLSCISIITHLKNYKKPVLQRSVVRILMMIVIYSSVSFLSVYNEKIGSIFEPFREIYEAFALYCFFCLLIDYLGGERAAVISLHGHLPRPRLWPLNYLQDDIDLSDPYTFLSIKRGILQYTWLKPFLVIAVLLTKVTGVYDREDQPVYASADLWIGLVYNISITLSLYSLTTFWVCLHEELAPFRPFPKFLSVKAIIFASYWQQTVLSITNWLGLLNGTGWIYSLLNQNVLMCLEMPFFALSHWYAFRIEDYDTPTWLSCARLPLLKAFKDVIGLKDVWCDSLQTLHGDRYVYQNFEPGENLIPSRNDGRINRTSHGLRYSQGGQSKYWISRYDQSRVRLINNSQNSPQSNKSYFSIPGMSTSHFENGLQFEIDDEMEPLYNQAKQMRYGDYNYPVLLVNNTHASSSYT | Function: Vacuole membrane protein that recruits ATG8 to facilitate the degradation of vacuolar integral membrane proteins during early-stationary vacuole turnover (EVT) when cells enter stationary phase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49290
Sequence Length: 426
Subcellular Location: Vacuole membrane
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P49235 | MAPLLAAAMNHAAAHPGLRSHLVGPNNESFSRHHLPSSSPQSSKRRCNLSFTTRSARVGSQNGVQMLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGESNWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEMGMDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLLLENGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTYFAKVCFDNFGDKVKNWLTFNEPQTFTSFSYGTGVFAPGRCSPGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKRDDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFLEPVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGLNYYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPIGPPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGDVDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNVQGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKESAKWLKEFNTAKKPSKKILTPA | Function: Is implicated in many functions such as ABA metabolism, hydrolysis of conjugated gibberellins, conversion of storage forms of cytokinins to active forms. Also acts in defense of young plant parts against pests via the production of hydroxamic acids from hydroxamic acid glucosides. Enzymatic activity is highly correlated with plant growth. The preferred substrate is DIMBOA-beta-D-glucoside. Hydrolyzes the chromogenic substrate 6-bromo-2-naphthyl-beta-D-glucoside (6BNGlc) and various artificial aryl beta-glucosides. No activity with cellobiose, arbutin, gentiobiose, linamarin or dhurrin as substrates.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 64237
Sequence Length: 566
Subcellular Location: Plastid
EC: 3.2.1.182
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Q9FYS3 | MALLVGGTLNPTTHLSLRSRAGRNSENVWLRSAASSQTSKGRFCNLTVRAGTPSKPSEPIGPVFTKLKPWQIPKRDWFSKDFLFGASTSAYQIEGAWNEDGKGPSTWDHFCHTYPERISDGTNGDVAANSYHMYEEDVKALKDMGMKVYRFSISWSRILPNGTGKPNQKGIDYYNNLINSLIRHGIVPYVTIWHWDTPQALEDKYGGFLDKQIVNDYKYFAELCFQSFGDRVKNWFTFNEPHTYCCFSYGEGIHAPGRCSPGLDCAVPEGDSLREPYTAGHHILLAHAEAVELFKAHYNKHGDSKIGMAFDVMGYEPYQDSFLDDQARERSIDYNMGWFLEPVVRGDYPFSMRSLIGDRLPMFTKEEQEKLGSLCDIMGLNYYTSRFSKHVDISSDYTPTLNTDDAYASSETTGSDGNEIGPITGTYWIYMYPKGLTDLLLIMKEKYGNPPIFITENGIADVEGDPEMPDPLDDWKRLDYLQRHISAVKDAIDQGADVRGHFTWGLIDNFEWGSGYSSRFGLVYIDKEDGNKRKLKKSAKWFAKFNSVPKTLLKTTNNNATVTASVSV | Function: Involved in defense of young plant parts against pests via the production of benzoxazolinones (hydroxamic acids) from hydroxamic acid glucosides. The preferred substrate is DIBOA-beta-D-glucoside. Can also use esculin and genistein glucoside as substrates, but no activity with salicin, p-nitrophenyl-alpha-glucoside or substrates related to cell wall components.
Catalytic Activity: DIMBOA beta-D-glucoside + H2O = D-glucose + DIMBOA
Sequence Mass (Da): 64212
Sequence Length: 568
Subcellular Location: Plastid
EC: 3.2.1.182
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Q7XB14 | MQAVTAAAAAGQLLTDTRRGPRCRARLGTTRLSWTGRFAVEAFAGQCQSSATTVMHKFSAISQAARPRRNTKRQCSDDYPALQAGCSEVNWDQNGSNANRLEEIRGDVLKKLRSFYEFCRPHTIFGTIIGITSVSLLPMKSIDDFTVTVLRGYLEALTAALCMNIYVVGLNQLYDIQIDKINKPGLPLASGEFSVATGVFLVLAFLIMSFSIGIRSGSAPLMCALIVSFLLGSAYSIEAPFLRWKRHALLAASCILFVRAILVQLAFFAHMQQHVLKRPLAATKSLVFATLFMCCFSAVIALFKDIPDVDGDRDFGIQSLSVRLGPQRVYQLCISILLTAYGAATLVGASSTNLFQKIITVSGHGLLALTLWQRAQHFEVENQARVTSFYMFIWKLFYAEYFLIPFVQ | Function: Involved in the synthesis of tocotrienol (vitamin E). Catalyzes the condensation of homogentisate and geranylgeranyl diphosphate to form 2-methyl-6-geranylgeranylbenzoquinol . Possesses low activity with phytyl diphosphate as substrate .
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate + H(+) + homogentisate = 6-geranylgeranyl-2-methylbenzene-1,4-diol + CO2 + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45092
Sequence Length: 408
Pathway: Cofactor biosynthesis; tocopherol biosynthesis.
Subcellular Location: Plastid
EC: 2.5.1.116
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P73726 | MATIQAFWRFSRPHTIIGTTLSVWAVYLLTILGDGNSVNSPASLDLVFGAWLACLLGNVYIVGLNQLWDVDIDRINKPNLPLANGDFSIAQGRWIVGLCGVASLAIAWGLGLWLGLTVGISLIIGTAYSVPPVRLKRFSLLAALCILTVRGIVVNLGLFLFFRIGLGYPPTLITPIWVLTLFILVFTVAIAIFKDVPDMEGDRQFKIQTLTLQIGKQNVFRGTLILLTGCYLAMAIWGLWAAMPLNTAFLIVSHLCLLALLWWRSRDVHLESKTEIASFYQFIWKLFFLEYLLYPLALWLPNFSNTIF | Function: Involved in the synthesis of tocopherol (vitamin E) . Catalyzes the condensation of homogentisate and phytyl diphosphate to form dimethylphytylhydrquinone .
Catalytic Activity: H(+) + homogentisate + phytyl diphosphate = 2-methyl-6-phytyl-1,4-benzene-1,4-diol + CO2 + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34410
Sequence Length: 308
Pathway: Cofactor biosynthesis; tocopherol biosynthesis.
Subcellular Location: Membrane
EC: 2.5.1.115
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P73276 | MAGSISSMYSPSAGLISLCQSQVRLLQQGLRVDWCGVYLNQEETEQGLVPLVVSHGSTLVESESYGLISLPQGEVSPPMDDFSLPAVPVGVGQLSRRSRLEPPPFDADKRLVLPLVYGEEMVGLLVIHRSQGQWHGEEMMQLEAIAKSLAVACLLDQQQDWYRQAWEEQNQQYQWERQHWADLLHQLRNPLTALKTFSKLLLKRWHGDNKSQQVVEGIVRQGEHLQELLQSFEASQSQGPEAVPLLSSSPVTTIQVLPPADRVETMPLANFSLGEVLPPILLAHQAIAAERNITLTAQIALIDTVVMANRLALREVVNNLLDNGIKYTPNGGLVEVSLALEKVSSSGMDWATLAIADTGYGIPPEDQQKIFERNYRGVQGRGSINGTGLGLAIVADLVAQMGGKITVTSPNGLSRDPDQPGSTFTLWLRSGEQV | Cofactor: The 3Fe-4S cluster is redox-responsive, binds 1 cluster per monomer. It is coordinated by Cys-19 and other non-Cys residues.
Function: Member of possibly 2 two-component regulatory system(s) Hik2/Rre1 and Hik2/RppA. Transduces PQ (plastoquinone) redox signals to photosystem gene expression machinery during the adjustment of photosystem stoichiometry. Reduced PQ suppresses its autophosphorylation activity (i.e. kinase activity is higher under oxidizing conditions) (Probable). Member of two-component regulatory system Hik2/Rre1, controls expression of sigB (sll0306), sll0528, slr1119, slr0852 and ssr3188 in response to hyperosmotic stress (Probable). Activity responds to high salt (with a linear response as concentrations rise to 0.5 M NaCl); detects Cl(-) levels . Autophosphorylates and transfers phosphate to Rre1 . May transfer phosphate to RppA in a possible Hik2/RppA two-component system (Probable).
PTM: Autophosphorylates, probably on His-185.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 47575
Sequence Length: 434
Domain: The N-terminal GAF domain activated by Cl(-).
Subcellular Location: Cytoplasm
EC: 2.7.13.3
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Q8DMC5 | MLWPASEEFAALCRTQLELVVNSLGASSLAVYLSETLNDSPSWSPVAVYPEAASLLSLAIPPTLPPPTQVPETSLSHYPQQVVSSLANQLILPLMYQNWVLGVLVAQRQHRPWLAAEQAQLQQVAQTLAIACVLDQRQQWLSHSPAQPLDQRQQRFDDLLHQLRNPVAAIRTFVKLLLKRLEPDHKGRPLAEGIAKETERLMALLEDYRQQRNDIPALTGSQPLPLAGKPLDLAETLLPLISAAQARAEMEGKTFVVEIPPQLPPIWLEERVLQEVVGNLLDNAFKYTPKGGTIGLRLMLSSPALELTVWDTGCGIPKEAQPRLFERGYRGVQADSGIEGSGLGLAIAQDLLRPYGLSLRVTSPYAGDRGTAFTLAIPWQMKVEP | Cofactor: The 3Fe-4S cluster is redox-responsive, binds 1 cluster per monomer.
Function: Member of 2 two-component regulatory system(s) Hik2/Rre1 and Hik2/RppA. Transduces PQ (plastoquinone) redox signals to photosystem gene expression machinery during the adjustment of photosystem stoichiometry. Reduced PQ suppresses its autophosphorylation activity (i.e. kinase activity is higher under oxidizing conditions). As part of a two-component regulatory system with Rre1, controls expression of sigB and several other genes in response to hyperosmotic stress. May transfer phosphate to RppA in a possible Hik2/RppA two-component system.
PTM: Autophosphorylates, possibly on His-161.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 42417
Sequence Length: 385
Domain: Oligomerization seems to be mediated by the histidine kinase domain (residues 142-386) which forms tetramers and hexamers. The DHp subdomain (dimerization and phosphotransfer, residues 142-270) forms hexamers and octamers. NaCl treatment reduces the histidine kinase domain to tetramers and the DHp domain to hexamers, suggests the DHp domain senses NaCl.
EC: 2.7.13.3
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P74199 | MNEVCLKLSDLFVSSGWGGYDRGRAPQWAHPRAQQQWFGAIAALEPFLRQTLPNVGGELPGICLTGPAPVLKDAVLVRNFYQGIATPWEEFSPWPCLAGEESEWSAVPPMREIPLFPQDPLAEEQFCWLMTPQFGLLLLLGKNEQGLAQFYWTFDPEILQQAWLSLQARLKYGLSPDLSLLQKTIAAFNFPQPDFRLVTYFGQLMLDYQPNPYNLPPCQEQESAEPSPDVELLQALTHEVRTPLTSIRTLTKLLLRRKDLSPEVLKRIESIDRECSDQISRMDLIFRATELESTPLPELVVPLTVTSLEAVFQAGIPRWQKQAQRYNVNLQAQIPHSLPQVWSNPSLLDQVLGGMIEKFVRNFNGGGEINLQITTAGDQLKVQFHTQSVHQANPVRALGELLMFQPQTGCLSLNWDVTKNLFQLLGGKLIVRRRSPSEEILTIYLKCEQRTVPVANYDRQFTMV | Function: Member of a two-component system Hik34/Rre1, controlling expression of at least 20 genes in response to hyperosmotic stress (0.5 M sorbitol) or salt (0.5 M NaCl) . Represses expression of heat shock genes under normal growth conditions . Required for survival of long-term heat shock exposure .
PTM: When expressed in E.coli autophosphorylates at 18 to 30 degrees Celsius; less phosphorylation occurs at 36 and none occurs at 42 or 48 degrees Celsius.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 52623
Sequence Length: 464
EC: 2.7.13.3
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A0A0H3L1B8 | MTDLLTLEPTQTILTGSKKTNFGYLESTDGVINFSIVKNIILNGHHHGNVLYVIRNYASKAVCEKLAKNFDYRVTQSGGNRADDGFVLTNQIGATQFSRNGEQYIHEVNRVNQSVADLMKATSAEDSESLFLNLTLEKEFLERGIHFGPARFKNGYACFATFRRWLDNGVMSLMPHEDMAQVDFAKEDGFEIANTQTVTAYNVCLEAAQGGGQLKIWNLIPDQVCRETLGVTRTGYPYPPHLLNETESLSVQLNAGDLYFMNACHLHGVSSVSEGSRLTAGRFIGKLNDRKVVYWT | Cofactor: Binds 1 ascorbate molecule per subunit.
Function: Catalyzes the hydroxylation of L-isoleucine at the C-4' position to form L-4'-hydroxyisoleucine (4'-HIL) . Exhibits low activity with L-valine and L-methionine .
Catalytic Activity: 2-oxoglutarate + L-isoleucine + O2 = 3(1)-hydroxy-L-isoleucine + CO2 + succinate
Sequence Mass (Da): 33019
Sequence Length: 296
EC: 1.14.11.74
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Q6ZIV7 | MGQALGLVQVDQSTVAIKESFGKFDEVLEPGCHFLPWCIGKQIAGYLSLRVQQLDVRCETKTKDNVFVNVVASVQYRALAEKASDAFYRLSNTREQIQSYVFDVIRASVPKMNLDDAFEQKNEIAKAVEDELEKAMSMYGYEIVQTLIVDIEPDEHVKRAMNEINAAARLRVAANEKAEAEKILQIKRAEGDAESKYLAGLGIARQRQAIVDGLRDSVLAFSENVPGTSAKDVMDMVLVTQYFDTMKEIGASSKSSSVFIPHGPGAVKDIAAQIRDGQLQAKLI | Function: Positive regulator of hypersensitive response (HR)-like cell death. May be involved in potassium ion channel regulation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31380
Sequence Length: 284
Subcellular Location: Cell membrane
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Q97KI3 | MDKNKTIRIALTKGRLEKAAVEIFENIGLDCSELKDKGRKLIFHDFKNSIDFVLVKAPDVLTYVEHGAADIGIVGKDTLLEMKKDFYEVLDLKVGKCKFSLASISSFKLNEGFNRMKIATKYPNVTREYFREKGIDVEIIKIEGSVELAPILNLADAIVDIVETGTTLKENGLVIFDDICDISARMIVNRASMKLNKDRITDIIQKVKNYVERES | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 24294
Sequence Length: 215
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
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Q18C67 | MDYLTIALAKGRIEGESFKKFKKMGLGDSIDTDTRKLIFKDEENKIIYIHVKPSDVVTYVEKGVADLGIAGKDTILENETDVYEIYDLGFGKCKFAVAGLKGDSIYREDEYLKVATKYPNIAKKYFKEKGQKIEIIKLNGSVELAPIVGLSDVIVDIVETGNTLKANGLEILEDICNISARIISNRASYRFKYEQIQNIIRLFEELDN | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 23491
Sequence Length: 208
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
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C3PG93 | MIKIAVPNKGSLSEAALEILKEAGYKGRGHNKSLNVVDEENGVEFFFLRPKDIAIYVAQGVLDLGITGRDLALDSRAKFNEVLALNFGGSTFRYAAPAGEEWDVAKLQGKRIATSYPNVVRDHLAANGIDAEVIRLDGAVEISIHLGVADVIADVVSTGTTLRQQGLEPFGEPIVTSEAVVIKREGEDVTADENVVLSRIRGILNARHYVMLDYNVAEEKLPNVEAVTPGLTGPTISPLAREGWVAVRVMVPRKLANQVMDSLEELGAEAILASDLRIARF | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 30382
Sequence Length: 281
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
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Q88P87 | MLTIALSKGRILDDTLPLLAEAGIVPTENPDKSRKLIIPTTQDDVRLLIVRATDVPTYVEHGAADLGVAGKDVLMEYGGQGLYEPLDLQIAQCKLMTAGVVGAAEPKGRLRVATKFVNVAKRYYAEQGRQVDIIKLYGSMELAPLINLADKIIDVVDTGNTLRANGLEPQELIATISSRLVVNKASMKMQHARIQSLIDTLRAAVESRHRG | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 22939
Sequence Length: 211
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
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Q4FQF7 | MTEVTNSLPTSGLLNEANDEFLGLTLALSKGRILEETMPLLRAAGVELLEDPEASRKLIFPTSNPNVRVLILRASDVPTYVEHGAADFGVAGKDVLLEHGANHVYELLDLKIAQCKLMTAGVKDAPLPNRRLRIATKYVNVARAYFASQGQQVDVIKLYGSMELAPLVGLGDLIVDVVDTGNTLRANGLEARDHICDVSSRLIVNQVSYKRKFALLEPILDSFKNSINSTS | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 25156
Sequence Length: 231
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
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A1RTU8 | MLLAIPSKGRLQEPTLRLLEAVGIKPLASDERALVLPTSWNDVNIIKARPEDIPYLVDSGRIWAGITGHDYIIESGSNVVEVLDLEFGKGKLVVAVPKTSGIKSIDELPPGARVATKFVNIAYNYFAELGKRVRIVRVAGSVEILPQLGIADAILDVMATGTTLEIHGLTPIATVLETSARLIVHPNYVNHELTKKLVTFIKGYYAAQGRKMIFLNVPATKLEDVLSILPAMEAPSVTKLAKGDVYEVFSVVPEDILPDLVMKLKNAGAKDIVVTSIEKLIS | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 30597
Sequence Length: 282
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
|
Q7URL0 | MVPMTTLAPLGSGSDPDSFLRLGIPSKGRLSELATGLLNQAGLSFRRQNRGLFARVSGLPIDLIFLRTDDIPTLCAEGAIDMGITGSDLIEEAGANVEQRMAFGVGRCRLAFCVPDDEDYTDAAQLNGKRIATSFPHVTEQYLATKNAKAHLVSLSGSVEAMIRLGVADAIVDLVETGSTLAANRLRILEEIGHYETVLIQNGTHRCKEVADRLVSRLEGVVLARDYSLVEYNIPRSRVSEAEKITPGFNSPTINSLEDKDWCAVQVMVRRGEVVEVMERLKEIGASGIFEMTINNCRL | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 32594
Sequence Length: 299
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
|
O34912 | MKQADELRFNEDGLIPAIVQDAASKEVLTLAYMNKESYEKTLETKETWFYSRSRQALWHKGETSGNTQAVKGIRYDCDQDALLVLVEPSGPACHTGSYSCFTKEQTEEQAADRFGIMNELERVIAERQAEMPEGAYTTYLFREGVDKILKKVGEEASEVIIAAKNRDHEELKWEAADLLYHLLVLLREQSLPLDDVLDVLKKRHSEIEE | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 23901
Sequence Length: 209
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
|
Q8A7Z7 | MELDFDKMNGLVPAIIQDNETRKVLMLGFMNKEAYDKTVETGKVTFFSRTKNRLWTKGEESGNFLHVVSIKADCDNDTLLIQADPAGPVCHTGTDTCWGEKNEEPVMFLKALQDFIDKRHEEMPQGSYTTSLFESGINKIAQKVGEEAVETVIEATNGTNERLIYEGADLIYHMIVLLTSKGYRIEDLARELQERHSSTWKKH | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 23078
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
|
B3DS06 | MKTFESLFAELSEKAQTRPEGSLTVDELDKGTHFIGKKIIEEAGETWMAAEYEGADRTAEEMSQLLYHVQVMMIKHGLTLEDVYKHL | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 9933
Sequence Length: 87
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
Q7VQW4 | MLTTEKYQGLNWSKNHGLIPAIIQHSISGEVLMLGYMNQESMAITEKTGYVTFFSRSKNRLWIKGESSGNVLKLINWYPDCDFDSLLILVLPQGFTCHKNTNSCFHPALTDFSFLFQLENIISIKKNHTSSHGNQQSSYTSDLYTSGIERIAQKVGEEGLETALAAVSRNSKSLIDEASDLIYHLLVLLQHESLNFHDVIQELRVRSKLKKKH | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 24176
Sequence Length: 213
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
|
Q3IU57 | MSGDGHDGDEVLDELFEVIESRKEELPDGSYTASLFTHEKGENAVLEKLGEETTELLLAAKDDDDEELAHEAADIVYHLLVLLSMKDMELADLRAELRKRR | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 11386
Sequence Length: 101
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
Q9K0J4 | MGDSVLSAIQQTITQRKSANPSESYVAQLLHKGEDKILKKVIEEAGEVLMASKDKNPSHLVYEVADLWFHTMILLTHHDLKAEDVLDELARRQGLSGLVEKAARTES | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 11924
Sequence Length: 107
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
P07685 | METTLPLPFLVGVSVPPGLNDIKEGLSREEVSCLGCVFFEVKPQTLEKILRFLKRHNVEFEPYFDVTALESIDDIITLLDAGARKVFVKTEQLADLSAYGSRVAPIVTGSSAALLSSATESGLLLSGFDQTASEAAQFLEEARDKKITPFFIKPVPGADLEQFIQVAAKANAIPILPSTGLTTKKDEAGKLAISTILSSVWKSDRPDGLLPTVVVDEHDTALGLVYSSAESVNEALRTQTGVYQSRKRGLWYKGATSGDTQELVRISLDCDNDALKFVVKQKGRFCHLDQSGCFGQLKGLPKLEQTLISRKQSAPEGSYTARLFSDEKLVRAKIMEEAEELCTAQTPQEIAFEAADLFYFALTRAVAAGVTLADIERSLDAKSWKVKRRTGDAKGKWAEKEGIKPAASALAATSAPVTKEAAQETTPEKITMRRFDASKVSTEELDAALKRPAQKSSDAIYKIIVPIIEDVRKNGDKAVLSYTHKFEKATSLTSPVLKAPFPKELMQLPEETIAAIDVSFENIRKFHAAQKEEKPLQVETMPGVVCSRFSRPIEAVGCYIPGGTAVLPSTALMLGVPAMVAGCNKIVFASPPRADGTITPEIVYVAHKVGAESIVLAGGAQAVAAMAYGTESITKVDKILGPGNQFVTAAKMFVSNDTNAAVGIDMPAGPSEVLVIADKDANPAFVASDLLSQAEHGVDSQVILIAIDLDEEHLQAIEDEVHRQATELPRVQIVRGSIAHSITVQVKTVEEAMELSNKYAPEHLILQIKEAEKAVDLVMNAGSVFIGAWTPESVGDYSAGVNHSLPTYGFAKQYSGVNLASFVKHITSSNLTAEGLKNVGQAVMQLAKVEELEAHRRAVSIRLEHMSKSN | Cofactor: Binds 1 zinc ion.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 93836
Sequence Length: 870
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
|
Q0AET9 | MTSSSTILQRLTQTIEARKSADPAHSYIAKLLSSNEDKVLKKIAEEAAETIMACKDNDREQIIYETADLWFHCLIMLARHDISPEAILSELERREGVSGIEEKLSRSQNQPEPTKAE | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 13214
Sequence Length: 117
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
B0T5D0 | MTVSSIFPPAADKTALERGAAIMPRFDANGLVAAIAQHADTGEILMFAWMNDEALKLTLDTGIAHYFSRSRNSLWKKGETSGQLQIVTELRIDCDQDAVLIKVRPQGDGGACHVGFRSCFYRVWENGALVEREA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 14729
Sequence Length: 134
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
|
A0RZ79 | MEKKIDEIDFEKAGGIVPVIVQDNNTHEVLTLAYSNRESLELTRKTGLSWFWSRSRSKLWQKGEESGNTQQVKKILVDCDQDALIYLVEPSGPACHTGERNCFHHSLL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 12316
Sequence Length: 108
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
|
Q53158 | MAFDPASLTFDANGLIPAVAQDHATGEVLMMAWMNAEAVARTVETGCVTYWSRSRQAFWVKGETSGHVQRLIELRIDCDRDCLLLLIEQEGPACHTNRRSCFYTALREGEERIILDPMV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 13389
Sequence Length: 119
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
|
A1B9F2 | MFDTASLKYDANGLIPAIAQDHQSGEVLMMAWMNAEAVRQTLDSGRVTYWSRSRQGFWVKGESSGHVQKLVELRVDCDRDCLLLLVDQTGPACHTNRRSCFYTAIREGQEVVIMAPQNPSA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 13547
Sequence Length: 121
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
|
A5CZ72 | MPFDLDSLKYNEAGLVPAIVQDAGTGAVLMMAYMNREALEKTLATGETWFWSRSRKAFWHKGETSGNVQRVKEVLYDCDRDTLLVKVEQHGAACHEGYYSCFHYRLERDGSVTVVGEKQFDPEQVYGKR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 14731
Sequence Length: 129
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
|
A1VK43 | MNWLDTVRWDDKGLVPVIAQEAASGDVLMFAWMNREALQKTAELGQAVYFSRSRGRLWHKGEESGHLQTVHEIRLDCDSDVVLLKVTQLGHEPGIACHTGRHSCFFSLYKDGQWVATEPVLKDPASIYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 14597
Sequence Length: 129
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
|
Q02EV1 | MKDWLDEIHWNADGLVPAIAQDHETGRVLMMAWMNREALALTASENRAIYWSRSRGKLWRKGEESGHVQKLHELRLDCDADVVILMVEQVGGIACHTGRESCFYRVFENGAWKTIDPVLKDPDAIYEHAGHHHE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 15389
Sequence Length: 134
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
|
Q1I3S7 | MKDWLDEIKWNSDGLVPAIAQDHKTGRVLMMAWMNRESLALTAAEHRAIYWSRSRGKLWRKGEESGHVQKLHEMRLDCDADVIILMVEQLGHIACHTGRESCFYRVFEDGQWKTVDPVLKDPNAIYSAGH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 15005
Sequence Length: 130
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
|
Q87UY9 | MKDWLDEIHWNSDGLVPAIAQDRKTGRVLMMAWMNREALSLTASENRAIYWSRSRGKLWRKGEESGHVQKLHELRLDCDADVIILMVEQIGGIACHTGRESCFYRVYEQSGWKTVDPVLKDPDAIYPAGH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 14927
Sequence Length: 130
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
|
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