ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9JXY2 | MSFKTDAEIAQSSTMRPIGEIAAKLGLNADNIEPYGHYKAKINPAEAFKLPQKQGRLILVTAINPTPAGEGKTTVTIGLADALRHIGKDAVIALREPSLGPVFGVKGGAAGGGYAQVLPMEDINLHFTGDFHAIGAANNLLAAMLDNHIYQGNELNIDPKRVLWRRVVDMNDRQLRNIIDGMGKPVDGVMRPDGFDITVASEVMAVFCLAKDISDLKERLGNILVAYAKDGSPVYAKDLKANGAMAALLKDAIKPNLVQTIEGTPAFVHGGPFANIAHGCNSVTATRLAKHLADYAVTEAGFGADLGAEKFCDIKCRLAG... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 59062
Sequence Length: 558
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
Q04FS6 | MKSDIEIDHSIKALPITEIGKQIGLSDSQLIPYGHDKAKIDAYSIANMPRQGKLVLVTSINPTPAGEGKTTVTIGLVDAINRLGKSAIGALREPSMGPVFGLKGGATGGGYAQVIPMEDINLHFTGDIHAVSAAHNLLAAVIDNHLHQGNELKIDPENIYWRRVLDMNDRALRQITLGKGRVNGPERNSGFDITASSEIMAVLTLSKNLFDLKKRLSRIVVALDVQGKPVTVADLKVAGALTAILKDAINPNLVQSLEHSPFIIHGGPFANIAQGTNSVVATDAALKLADFAVTEAGFGSDLGGEKFMDVKVPVLGKEPD... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 59483
Sequence Length: 553
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
Q5XZD9 | MKTDVQIAQEAKMLPIMEVAKQIGLGEDDIELYGKYKAKISLDVYKRLADKPDGKLVLVTAINPTPAGEGKTTTNVGLSMGLNKIGKKTITALNEPSLGPCFGVKGGAAGGGYAQVVPMDDINLHFTGDIHAITTAHNLLAALMDNHIKQGNALGIDINKITWKRVLDMNDRALRDIVIGLGGTANGIPRQDGFDITVASEIMAIMCLATSLSDLKDRLSRMIVGYTSRRLAVTADSLTLRGALALLLKDALKPNLVQTLENTPAIIHGGPFANIAHGCNSVTTTKTALKIADYVVTEAGFGADLGAEKFFDIKCRFADL... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 59161
Sequence Length: 556
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
A9BIV8 | MLSDIEIARSAKLKKIDLIANELDIPEEYYNLYGKNIAKVSHKYLNELNFKNDGNLVMVTAITPTPAGEGKTTTSISLSMALNKIHKRSIVTLREPSLGPVMGIKGGAAGGGYSQVLPMEDINLHFTGDIHAVTSAHNLISAILDDYIKYNKYDIDSTQVSWPRTMDMNDRALREIIVALGGKKNGYPRQDGFIITAASEIMAILCLIENLEDLKKKLSNIVVAKNKKGEPVTVKDLEITGALSVLLKDAINPNLVQTIENTPAFVHGGPFANIAHGTNSILATKLALKLSDYVVTETGFGSDLGGEKFYDFVSPTFGLK... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 60679
Sequence Length: 554
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
Q6KZM3 | MKNISEIINIPEDYYDLYGRYIAKVSLNVLDYLKNKRYGKLILVTAMTPTPAGEGKTTTAIGLGNALKLLGKNAGIAIREPSLGPCFGVKGGATGGGKSTVEPSNKINLMFTGDFPAVSAAHNLLSAVINNHMYHGNELKLDPKNIVFPRTIDMDDRSLRSIIVGSGDRSTGVMMNDKYVITAASEVMAILALSRNYNELKQRLGNIMIGYNLNKAPIFARDLKVHGAMASLLVDALRPNIAQTSEHVPAIIHTGPFGNIAHGTSSILGDIIGLKMFDYLVTEAGFGSDLGFEKFIDIVLRLSDFKLSAVVLVATVRAMR... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 58003
Sequence Length: 535
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
Q8CNP5 | MLSKELLAALNEQMNQEYFAAHAYMAMAAYCDKESYDGFANFYIEQAKEERFHGKKIYDYINDRGEHAIFDTIKAPKVEFSSILETFKDSLAQERDVTQRFYNLSELARNDKDYATISFLNWFLDEQVEEESTFETHIDYLTRIGDDCNTLYLYEKELAARSFNEQ | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
Sequence Mass (Da): 19612
Sequence Length: 166
Subcellular Location: Cytoplasm
EC: 1.16.3.2
|
Q9C0B1 | MKRTPTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTLHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNTRLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDAVPLCMSADFPRVGMGSSYNGQDEVDIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDPDIWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSST... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis . Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent int... |
Q8BGW1 | MKRVQTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLVFREAGSIPEELHKEVPEAFLTLHKHGCLFRDVVRIQGKDVLTPVSRILIGDPGCTYKYLNTRLFTVPWPVKGCTVKYTEAEIAAACQTFLKLNDYLQVETIQALEELAVREKANEDAVPLCMAEFPRAGVGPSCDDEVDLKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGSEDESEDESSFEGRDPDTWHVGFKISWDIETPGLTIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis . Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent int... |
I1BRD6 | MSQDLFNVPIFFILFRETTEAAIIISVLLSFLKRMFNTESPVYKRLRNQVWIGGAAGLFICLCIGAAFIAVYYTVLNDLWGNSEDIWEGVFSLVAVIMITAMGLAMLKTERMQEKWKVKLAKAMQKSNSEKSSFKEKLQKYAFFVLPFITVLREGLEAVVFIGGVSLGIQGKSIPIAAIMGIICGCLVGFLIYRGGSLIQLRWFFVFSTVVLYLVAAGLMAKGVGYLEQNAWNQVIGGEAADVISYRVSTAVWHVSWGDPEANNDTSGGWQIFNAILGWNNTATYGSIISYCLYWLFVCCYLVFSYFKEKRAAIRKAEAG... | Function: High affinity iron permease required for iron uptake in iron-depleted environments . Required for full virulence in mice .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41125
Sequence Length: 368
Subcellular Location: Cell membrane
|
A1URA3 | MNSNFRSLMIWGLIALFLIVLFSFFNGNRQRASNGEVSYSEFLQKIDNNELKTVTIQGQKLTGQTADRRMISTYAPRDPGLVQRLNTNKVNIRAVPESSGNSIFLNLLFSLLPVLIIVGAWIFFMRQMQGGSRGALGFGKSKAKLLTEAQGRVTFKDVAGVEEAKQDLQEIVDFLREPQKFQRLGGRIPRGVLLVGPPGTGKTLLARSIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEPNESIILIAATNRPDVLDPALLRPGRFDRQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82521
Sequence Length: 764
Subcell... |
B7J0N5 | MNGNNNMNNNGKSNNKKKNKNWILGLVVVFLISAIFMSYFIRGGESYKNVPYSTFQSYLDNGLVESVVIIDKNLIQFVVKGSNFAKSYFSTSIPYLDINLLSELKNKKVELSSGKSQASLIGVLLQTLPWILFFIFFFFIFRQTQGGGGKVFTFGKSNAQKYEAGKNKITFKDVAGQEEVKQELREVVEFLKNPKKFEKIGAKIPKGVLLVGSPGTGKTLLAKAVAGEAGVSFFHMSGSDFVEMFVGVGASRVRDLFDNARKNSPCIIFIDELDAVGRSRGAGLGGGHDEREQTLNQLLVEMDGFGTHTNVIVMAATNRP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70802
Sequence Length: 639
Subcell... |
C7MC16 | MADSAKTPRGKKRRPFTGLALWIIVALLLGMAMFSLFGRDGYQQIDTQQGLELLAGDTVEQAKIIDGNQQRVDLVLTEDFKDGDEDKGTQVRFSYVDARGDAVVQAVEDAAPAKGYTDEIASSSWWSTLLLSFLPLLIFIGLFWFLIMNAQGGGKAMQFGKSKAKLFNKEAPKVTFADVAGADEAVEELDEIKQFLVDPGRYQAVGAKIPKGVLLYGPPGTGKTLLAKAVAGEANVPFYSISGSDFVEMFVGVGASRVRDLFNTAKENAPAIIFIDEIDAVGRHRGAGMGGGHDEREQTLNQMLVEMDGFEENQNVILIA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75758
Sequence Length: 704
Subcell... |
Q89AF2 | MAKNLMLWLVIAVVLMSIFQNFSANNINNRKIDYSTFLSDVNQDQVREVHISGREMNIIRKDNGRYITYIPISDPKLLDNLLVKNVKIIGAAPEEQSFFTAIFISWFPMLLLIGVWVFFMRQMQVGGGKGAMSFGKSKARMLPEDQVKITFSDVAGCDEAKEEVQELVEYLKEPSRFQKLGGKIPKGILMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEHSRKVAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFDGNEGIILIAATNRPDVLDPALLRPGRFDRQIFVA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68020
Sequence Length: 610
Subcell... |
Q3JMH0 | MKSETGYMGFVVVLVFMVLLALQLATLSAPATQIAYSDFRKLAAAAQLDDLEVSPTRITGVLRSASAAAALPASDAEAIKRAGTPWRFSTKRVTDERLIDTLAATGTRYRGADDDTWIGTLASWIVPIAVFALVWNLMLRRPRGGLQDWSGVGKSKPRVYVEAKTGIDFDDIAGIDEAKAELQQIVAFLRAPARYQRLGGKIPKGVLIVGAPGTGKTLLAKAVAGEAGVPFFSTSGSSFVEMFVGVGAARVRDLFEQAQQKAPCIIFIDELDALGKVRGAGLASGNDEREQTLNQLLVEMDGFQANSGVILMAATNRPEI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71914
Sequence Length: 666
Subcell... |
B9MPK5 | MRNLFKTATIYILIALVILLLVDIFSGGLSYNQFFSNLSERREVIYSELINDINDGKVTRIVLSYNNVSGQYADGTKFDNVFVPSPDKFLDQIQPAIQAKKIQIVTKEPPQVPWWLSTFLPMLIFAGLMIFVWIFMLQQTQGGGSKIMSFTKSRAKTIQDLKKKVTFADVAGADEEKEELKEVIDFLKNPRKYIELGARIPKGILLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGAARVRDLFDQAKRNAPCVVFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFGTNEGIIVMAATNRPDILD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68457
Sequence Length: 616
Subcell... |
B8H444 | MNFRNLAIWLVIVAVLGGVFVVSQNSRTKSSSEISYSQLLKDVDAGKIKSAEIAGQTVLAKTADNKTLTVNAPMNSEELVNRMVAKNADVKFKSGSISFLAILVQLLPILLVVGVWLFLMRQMQGGAKGAMGFGKSKARLLTENKNRITFEDVAGVDEAKEELQEVVDFLKDPAKFQRLGGKIPKGALLVGPPGTGKTLIARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQVVVPN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67693
Sequence Length: 626
Subcell... |
Q3B6R3 | MAKNSLKPSNPYNSEPETPQPRPKLPMIYYVVVIALLIGLQLAFFWSGSSREIPYSTFRTFITENKVESVRIAPEKIYVTLKPGVDSGLPKQEEGNDTTRKLLPGAKTPENEVTVNPVRDESLTALLETHGVRYEGSPGTTWISELIQWVLPFALLFGLYFFIFRRMGAGGPGAQFMNIGKNKAALYENLDEHTRITFKDVAGLDEAKAEVMEVVDFLKDPKKYTRLGGKLPKGVLLVGPPGTGKTLLAKAVAGEADVPFFSISGSDFVEMFVGVGAARVRDLFRQAKEKAPCIIFIDEIDAVGRSRGKGAMMGGNDERE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77720
Sequence Length: 706
Subcell... |
A0PXM8 | MGGINVKKRLSSATIWIVLLIVLFFAAITVLESSKTSGAISYNEFKKYWIENKVSRVEIKQDGRTVAGELNDKAKTQFQVVVPQSLLVQDILVNNPKSSVNVKFEPASSMPMWISWIPTIILILVMVGFWVMFMQQSQGGGGGNRGVMNFGKSRAKLATPDSQKVTFKDVAGADEEKGELEEIVDFLKEPKKYLDMGARIPKGILLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNSPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGVNEGIILVAATNRPDILD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74487
Sequence Length: 676
Subcell... |
Q0TTK8 | MFKDKKMLKYIVIYSIIAFGILLTFNMVKDEMLYEKVDYSTFMQMLDKKEVKSVNFSGNQIEITPSDSSNLKGKILYTTNPAVAGITQPELIKDLTVAGVEFNVTKPENYQLLGLLMSWVFPLILIFFVGRMMFSKMNNKMGGGVMSFGKNNAKLYAENETGITFKDVAGQDEAKESLVEIVDFLHDTRKYVEIGAKLPKGALLVGPPGTGKTLLAKAVAGEAKVPFFSMSGSDFVEMFVGMGAARVRDLFKQAEEKAPCIVFIDEIDAIGKSRDGAIQGNDEREQTLNQLLTEMDGFDSSKGVVILAATNRPEVLDKAL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79891
Sequence Length: 717
Subcell... |
Q6M2F0 | MKNKKYLQFGGIAAVILIVLFLVSLFSSDTRNFQEVDTSVAMAQLDAGNVAEAQIDDREQRVRLTLREPITVDEREGVEEILAQYPARTAPAIFEKVEASNTDSYTTNVTQESFLMSMLSFILPMVIIFGLLMFFLTRMQGGGMFGIGGSKAKQLTKDMPTNTFADVAGAEEAVDELHEIKDFLEDPTRYEALGAKIPRGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFKQAKENSPCIIFVDEIDAVGRARGSGMGGGHDEREQTLNQLLVEMDGFGDRQGVILMAATNRPDVLDPAL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92253
Sequence Length: 853
Subcell... |
Q1LLA9 | MQCSYPLARQLERSSALNNNLFQKAAIWLVIALVLFTVFKQFDKPRAQDSVTYSQFMDDAKNGKVSRVDVQGRNLVVSPKEGSKYTIISPGDIWMVGDLMKYGVQVTGKADDEPNVLVQALYYLGPTLLIIVFWFYMMRQMQGGGKGGAFSFGKSRARLIDENQNAVTFADVAGCDESKEEVVELVDFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71260
Sequence Length: 649
Subcell... |
D4HA34 | MKNASRIFKGPLIWILLCIGLIIVFLQFAGSGNGYKDIPTSEAVSIINSSKKLDSVTLTDGDQVIKITENENKKYRSYWVGNQSDQLVDRLNDRVKAKTLKSWQGENPGQSIWKALLINFLPFVIILLFFLWAMNAAQGMGGRGGVMGFGKSKAKVGSKDTPKSTFADVAGCQEAIDELQEIREFLAEPAKFQRVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKEAAPAIIFIDEIDAVGRHRGAGMGGGHDEREQTLNQLLVEMDGFDVHGGVILIAATNRPDVLDP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77231
Sequence Length: 717
Subcell... |
O22993 | MASIDNVFSLGTRFSIPENPKRSILKHATTSSFSARTQTRWRAPILRRSFTVLCELKTGSSSSGETNNSPAADDFVTRVLKENPSQVEPRYRVGDKLYNLKEREDLSKGTNAATGAFEFIKRKFDSKKKTETDKSEESVYLSDILREYKGKLYVPEQVFGPELSEEEEFEKNVKDLPKMSLEDFRKAMENDKVKLLTSKEVSGVSYTSGYRGFIVDLKEIPGVKSLQRTKWSMKLEVGEAQALLKEYTGPQYEIERHMTSWVGKVADFPNPVASSISSRVMVELGMVTAVIAAAAVVVGGFLASAVFAVTSFAFVTTVYV... | Function: Functions in chloroplast biogenesis and chloroplast division . Required for plastid development during embryogenesis . Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105543
Sequence Length: 9... |
A8MPR5 | MACRFPLHSSSPSQFLSPENRQRLPRNYPSISCQNNSATNVVHEDGDDNDKAKTNQVNLLAIPITLTIISASLAKPSFAAAKVTERKRTQKKPQEALTLEQLKAWSKDLPVVSNRIPYTDILSLKAEGKLKHVIKPPNLSLRQKAEPVLVVLEDSRVLRTVLPSLEGNKRFWEQWDELGIDVQCVNAYTPPVKRPPVPSPYLGFLWKVPAYMLTWVKPKKESKRAAELKRMREDFKRQRKEEIETMKEERVMMEKTMKAQKKQQERKKRKAVRKKKYEESLREARKNYRDMADMWARLAQDPNVATALGLVFFYIFYRVV... | Function: Required for plastid development during embryogenesis . Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99864
Sequence Length: 876
Subcellular Location: Plastid
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Q9I1K1 | MSSQRRNYRFILVVTLFVLASLAVSGRLVYLQVHDHEFLADQGDLRSIRDLPIPVTRGMITDRNGEPLAVSTEVASIWCNPREMAAHLDEVPRLAGALHRPAAALLAQLQANPNKRFLYLERGLSPIEASEVMALGITGVHQIKEYKRFYPSSELTAQLIGLVNIDGRGQEGTELGFNDWLSGKDGVREVAINPRGSLVNSIKVLKTPKASQDVALSIDLRLQFIAYKALEKAVLKFGAHSGSAVLVNPKSGQILAMANFPSYNPNNRASFAPAFMRNRTLTDTFEPGSVIKPFSMSAALASGKFDENSQVSVAPGWMTI... | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin .
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass me... |
Q9M895 | MATFNVLCSNRFRFNGGYSPEKFNRKVSSRSSELNVCVSRIRTQSFSCRRLGGFMEIGETRLGVIRVHGDSRNRFSCNSEIKRLVTGDYGDKETRIGENGRNKGKRRRFSLRLRPRLRLVRMRLGRFDFRASMEDFRYFLKKNLKRVILSTGVALIFGLCYLFLRLTAVPSPSIVPYSDFVTNLRGGSVSKVLLEEGSRRIYYNTDENVEVVDDVHKSETLEDPAIQIDGGTVTEAVTKDDTPRKVRALPPVWKYVTRKVDHDEKFLLSLMREKGITYSSAPQSALMSMRTTLITIISLWIPLTPLMWLLYRQLSASNSP... | Function: Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69410
Sequence Length: 622
Subcellular Location: Plastid
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F4KF14 | MTFYISSSLTPTHFSKPLNPSNTLFPSQFRGSLSSFVRRRKPTEAKLSSKFNLFPSRRNGLITCCSTSSFESTESSVSQEEDAESNRLFEKLRETERERLSNMEELERKANVQLERQLVMASDWSRTLLTMRGKLKGTEWDPETSHRINFSDFMKLLDSNSVQYMEYSNYGQTISVILPYYKDGEPLGEEEDSKKEIIFRRHIVDRMPIDGWNDVWKKLHQQIVNVEVFNVDVVPAEVYTTVATFVVWSMRLALFVSLYVWIDSITRPIYAKLIPCDLGTPTKKIRQPLKRQALGSLGKSRAKFISAEEKTGVTFDDFAG... | Function: Functions in chloroplast biogenesis and chloroplast division. Required for plastid development during embryogenesis . Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 96854
Sequence Length: 85... |
A2CI41 | MKPYEPKSWVTRVFLVWWLTALSCFFISGRLIYLQLLKGKWLKEKALKQQTVTLKTFQPRRNICDRNGIPLAIDTLAYDVFAHPLYFSISIEEVANKLSPILCIDSLSIQKLLKPTSTGICLASQLPENTGKLIASLRLDGIDLIKHPKRYYPYKEIVGNVIGYVDTSHQGQAGIELSCQESLQLNSPTLTSSIDGRGVLISHQIPKELFIQDNLSLQLTLDLELQKIAYKALKQGLENCKGKRGTVLILDPKTGGILTLVALPSYDPNIYYDFPIERFKPWPVTDLYEPGSTFKPLNIAIALETKAISPEDSFYDEGCI... | Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75878
Sequence Length: 679
Subcellular Location: Plastid
EC: 3.4.16.4
|
Q9TL36 | MIYNYPMKYRRQFRRLPKHLQGIYYAFLSISTMIKIALDPYSKRPMKWMHSGTPFQYENERMVMIKLSLATVGLLFATRLSGLQFNKYTELKSVAERQQIGQVNDPQQRKIILDHHGDIVAIDLPAYDLYVHPRMCSISLERIAELLSPILDLSSQYLYNRLDEGDSGICLMHQIDTNTSAQIRRLGVDGIELVHHPQRVYPKRGSFESILGYVDTEGYGQAGLESSLDDWMKSTYQDVPCWMDGHGNFLGIRFPKQILFHQESALQLTIDCGLQEKVSQLITNAMNRFGAKRIAAIIMEAHSGAIRCLATSPSYDPNCY... | Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 79946
Sequence Length: 709
Subcellular Location: Plastid
EC: 3.4.16.4
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P57317 | MYKKEKNRFLKSKQINYINWRFFLLYGFIFLSLFILTLRVIFLQIISSNRLITEGDRRTLRTQSLLSTRGAIKDRRGYPLAVTVLVNAICADPSVILKTKNIKNHKRWQALSEILSIPLKKMFLRINSHKKSKFIYLARQINPEISEYIKKLQLPGIFLLEESKRYYPFKEISAQLVGFTNIDGIGIEGIEKSFDLLLTGKPGKRKIRQDNKGHVIEKISLVHKRASNNLNLSIDTKLQTIVYNELQEGVKKSQSDSGTAILINIKSGEVLAMANSPSYNPNNIRHIIQKNVRNKAITDLFEPGSTVKPIVIIEALKLGI... | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): ... |
Q89AQ0 | MKYFFQNKKNIHIKNETFNNRITILLSLIIITIILVLSRITFLQIIVSKKLIYKSNLRSLRTQIEFNQRGNITDRLGYPLAINIPVKNICIDPKLLFSKQTHIYPNLKWKMLSTVLSIPLSEIFYRIKYSKNNHFIYLAHKVNPEISEYISQLHIPGIYILDDFKRFYPFGKLTSQLIGFTNIDNEGIEGVEKSFNKLLMGKPGKKQIITDRYGRIIEQHNLVNKIQSHDIILSIDCSFQKFIYHILNQAVMSNKAKFGVAILVNIPTGEILSMVNTPSYDPNNSSELFKNNPLIRNKAITDIFELGSTVKPMIIMKALE... | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): ... |
B8H0A0 | MSLSNLGPGGVHSPLWRWVVERVWRLEHAFERSRAAARPEDDTRIRIFLVMGFFGFCFVGVSLGAGWSALFSRAGQGGGYAQGVEGARGDVVDRNGKLLAVDLAHYALYVDPREVWDAKETRAALGRALPQVPAKRLDKAVFGDHRAFVLGGLTPDEKDAIFNLGLPGVTFEEQERRMYPLGPTAAHLIGFVDSGGKGLAGAERALDDPIRKAAGGEGGPAQLSIDVRVQAALEDELRKAAEEFTPKGAVGLVTNVHTGEILGMASWPDYDANKAGGATDDQRLNRAAASVYEMGSTFKAFTVAIGLDTGVATAASTFDA... | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): ... |
P0AD69 | MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMRSLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIPLDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTITDVFEPGSTVKPMVVMTALQR... | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): ... |
P45059 | MVKFNSSRKSGKSKKTIRKLTAPETVKQNKPQKVFEKCFMRGRYMLSTVLILLGLCALVARAAYVQSINADTLSNEADKRSLRKDEVLSVRGSILDRNGQLLSVSVPMSAIVADPKTMLKENSLADKERIAALAEELGMTENDLVKKIEKNSKSGYLYLARQVELSKANYIRRLKIKGIILETEHRRFYPRVEEAAHVVGYTDIDGNGIEGIEKSFNSLLVGKDGSRTVRKDKRGNIVAHISDEKKYDAQDVTLSIDEKLQSMVYREIKKAVSENNAESGTAVLVDVRTGEVLAMATAPSYNPNNRVGVKSELMRNRAIT... | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): ... |
G3XD46 | MKLNYFQGALYPWRFCVIVGLLLAMVGAIVWRIVDLHVIDHDFLKGQGDARSVRHIAIPAHRGLITDRNGEPLAVSTPVTTLWANPKELMTAKERWPQLAAALGQDTKLFADRIEQNAEREFIYLVRGLTPEQGEGVIALKVPGVYSIEEFRRFYPAGEVVAHAVGFTDVDDRGREGIELAFDEWLAGVPGKRQVLKDRRGRVIKDVQVTKNAKPGKTLALSIDLRLQYLAHRELRNALLENGAKAGSLVIMDVKTGEILAMTNQPTYNPNNRRNLQPAAMRNRAMIDVFEPGSTVKPFSMSAALASGRWKPSDIVDVYP... | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin .
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass me... |
Q9JU31 | MTEKSHKKTAKGRAGSPSPTSARNKKADNGARGNKVSERLKAVKELQKTETKKARPEHVVNLIGDALWLMGLAATLYLVISLISFDMGDPSWSHSSPVVEDVANWGGLFGAYVADVGYYLFGWSFWWWIAAACVMLYKNFRLHAKQTENEAYNHKIAAAALFVLTVFSPVLEYFVLGGKYADSLPVGAGGMVGIRVGAVFAWLLGKSGSLLIILVVLLLSLSLLVQISWLEFLNGAGRAVQNRLSALSGKVMALGKRRPNTKTDGVDTQNTRRMVKEAKNITAKPVALPEGSSSNRKSVAVSVAPPPKIQVSLFEDDEPR... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q8XRH0 | MGLGWFGISSVWLLPMVWRYVARVMAGERGLKGPGTVRIWLATLAVLCASASLEALTSGRDLHGKAGGAVGRGLASLFGHMLGWTGAFLLMLGVLLWVAPMVFGHSWRQLLARLRQAGEAPPVQADARHDEADDGLKPTALGLGGAEQAMGSGHAGASRRHGIEAGSAWRQPAWQPPPRTRESPPQPGEIWPLLNAQGRPEMPLPVAAQPAPVPVPAPAATPKAATQAPSSRSALRATIVSSPFHRPQPSDGDQPPSSPEADDAPSAPVEDAAPAISPAAEPDAPASAPPEPAEPSPPTVDLEAVRQEAEALLAELRGLM... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
C6XMG3 | MSQVRSKSQQGKRQAKPQEVVPATILTEQLSTYAFGTVTAGAVMVAVAAWMGGSLASIDERIQGGLDATAKSAGFTVTKISIEGLDPRTKADVLNAVAIPVDSNMFRADPFVIKERIEASVENVSEVRVLRQWPNDIWILAENRRPLALWQTDGEWKVVDQVGKPMDGEDPAEYVELPRVVGPAGGYAAPELLAQLKLHPQISEHLEVAMRVGGRRWDLRLDSGLEIALPEDAQVDEALLAVYNLDEATGVLAEDSEVTRIDARDLERFAVGLGEARAAYDQSSQIDDKSGGA | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31760
Sequence Length: 293
Subcellular Location: Cell inner membrane
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Q28NP3 | MTTRSPARPLIARRSTPAPTPAPHDPAPSRLSYRVTRLWLTPIFRKALHLGIPVFALFAAVTWYLGDETRVAELFEAVQEIRREVENRPEFRVNVLGIDGASDDVTEQVRAALALDLPISSFDLDLDELRGRLEALPPVRTADLRIQSGGYLAVRIDERIPAAVWLTHEGLSIVDGDGIFVAGFGTRELAAPLPLLGGEGANLAVPEALALMEASSILDDRVHGLVRMGERRWDVVLTNGSRILLPEIGAAAALDRVLALDDMGEILSRDVTAVDVRNPGRLTVRLTDAAMEELQRLQTLAAERPDGDTRG | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33933
Sequence Length: 311
Subcellular Location: Cell inner membrane
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E3EYX6 | MRPVDKKPVDRKIERETRYLRRDPAPSRWSYRYQRLMLTPAFRAGVRLGTPVIIIALAVAVVFGRADSRDWIMGHYNAAIAAVTQRPEFMVGSFAITGASPDLALAIEGLVDIPFPISTFNLDLQDLRTNIAALSPVRNVNVQAGGGVLQIVIEERQPVAVWRHVDGLRLMDGEGIATGMILNRADRPELPLIAGDGAQAAIPEAMELFRIASPLGARVLALVRMGERRWDLVLDREQIVQLPAVDAVAALQRVIAQEEAQQLLSRDVAVVDMRNDARQTIRMTQRARDALRSMPGRSAGRG | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33349
Sequence Length: 302
Subcellular Location: Cell inner membrane
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Q1IKZ6 | MARNGNPQFPDERSTATRAKATEPEELDDRFSDLEPEEDSPFLRSQKRVPVRRGPLPSKKAANRVKIALIVLGVLVVIGGVWMALSAYGEHSWRFRLESSDSIEVGGNEHMSRGEITRVFGGDISRNIFAVPLDERKKQVEELPWVESATVMRILPDRIRVQVTERKPVAFAQIGSRVQLIDAHGVLMEMPFSTTNKYSFPVISGMHENEPLSTRSARMKIYQELVKELDASGEHNSKSLSEVDVSDPDDVKVTVEDADGAVLVHLGSQNFADRFHLYVTHLKEWRSQYQHLDSVDLRYDRQVILNPDSHPSAAKPTAPA... | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 38706
Sequence Length: 347
Subcellular Location: Cell inner membrane
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F9ZZP5 | MKFILFALLVSAGSWYGWKQLHSQDAVSKPIRYVKIEGAFQYTNKETLKRILTPEMKRGFYHVDMDAIHQLISQLPLVAAVDVNRVWPDAVHIKITEQKPIVRWGDKAVLNKQGEVLIPDDIDEFKNLPLITGPEGQEKKLLEIMKGVYIVLKDKSMQLAEFHVNDRRAWRIKLASGLEMQLGRKAPLENMQRFLKTMDLLGEEQVAMMASVDTRYPNGYAVTWKPDTPEIDWKAIAENYKNVMKERRI | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Location Topology: Single-pass type II membrane protein
Sequence ... |
A0R014 | MTGTGPHGDPAEDPAGPDDTAAETDGPAEPTEPVDASEAEMTDTTETTAQTGTTAEADASEEFEGPRRRARRERAERRAARDRAMAIEQARREAKRRAVAGALDPTKSVPRNTIRGLKVLMWAALVSVLAVALGLLLYFTPIMSARNVEVSGLAEIPQEEVLTAAAVAPGTPLLQVDTDAVAERVATIRRVATARVQREYPSTLKISIVERVPVVVKDYPDGPHLFDRDGVDFATGPAPLALPYLDADNPGPNDPATRAALDVMMALPPDVAAQVGRIAAPSVASITLTLIDGRVVVWGTDDRTQEKALKLAALLTQPGT... | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35307
Sequence Length: 333
Subcellular Location: Cell membrane
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F8CLT8 | MAFGKSKNRRRQDAAQQKEAVRGAVRSQGPRALKVLGLTLGTGLLVWGGAALREWTLTSPRFELEAVSFSGLQRASRVELLRLAALTKGQNLWTLDVDALERAMDQHPWLRTVEVTRRFPNRVSVEVTEHTPVAMAVLGELYVLDEEGEPFKRVTPGDGLDLPLVTGLDREGYVADPAAARERLRSALAVASAYARLSPDQAEQLSEVRLEAQSLALVTASGQEVRLGEGDSEVKLQRLARVRRELGARGLAAEIIHLDNRARPGWVAVKISSPASERSGASMR | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31057
Sequence Length: 284
Subcellular Location: Cell inner membrane
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Q9K0X9 | MERLTRWLLVMMAMLLAASGLVWFYNSNHLPVKQVSLKGNLVYSDKKTLGSLAKEYIHGNILRTDINGAQEAYRRYPWIASVMVRRRFPDTVEVVLTERKPVARWGDHALVDGEGNVFEARLDRPGMPVFRGAEGTSAEMLRRYDEFSTVLAKQGLGIKEMTYTARSAWIVVLDNGITVRLGRENEMKRLRLFTEAWQHLLRKNKNRLSYVDMRYKDGFSVRYASDGLPEKESEE | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Location Topology: Single-pass type II membrane protein
Sequence ... |
Q2Y642 | MWDNHQALNQVADWLFTLAGLTTIYLMVQWTIHLPLLPLKEVHIRSNSGSGELRHVTREQVSDVVHREVGGNFLTIDLEAARHTFEKLAWVRVASVRRIWPNGLDVVVEEHVPLAHWGDSALVNRQGEIFNATSDEPMPIFEGPRESVREMVHQHAVFTKLLQPLKQDVEQVELSPRRAWRVRLGNGTILELGREHLEKRLERYVQTHDLVVARLNQRLSYVDLRYVSGFAARGTR | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Location Topology: Single-pass type II membrane protein
Sequence ... |
Q2G991 | MAQTIKRGGKGVRRATAARSAQRKVQTARQQTGSVLDSVLRWLPFSEETLHRILMTLILAAAAGLVWTVAVMAGIPALVSEQAAIIASDAGFKVSHLEVRGVNRMNEAKIYERILGQNDRAMTTLDLAALRDELNQLPWVKDARVSRKLPDTLVIDIVERTPHAVLRKPDRMVLIDDTGVELESVRADRAKGMLVLSGMGVGQRVEDLTRLLDAAPALKPQVSEAEWVGNRRWNLTFKTGQVLALPEGDETAASALLSFARMDGVNRLLGGKVAAFDMRAPDRIYMRVPGHADEVAAEKRAEEQARAEAKRAASAKSDEG | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34941
Sequence Length: 320
Subcellular Location: Cell inner membrane
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A1BAK9 | MQGLNPFHRDQGAGGRPAPVRPAPARPAPVAPRTPRKDPAPSRLAYRLNRMMLRPLVRRLVHVGLPAFLAALVAGIWLSDDTRRANLTGGIDAIVDRIQHRDEFMVKMMTIEGASPVVDKGLRAMLPVELPASSFEIDLEKLRERVLKLDAVETVDLRIKPGGVLSAVVTERVPVVLWRHARGIELLDKTGHRVASVTSREVRGDLPIIAGEGADRAAPEALALIDAAGPILPRLRGLERMGERRWDVVLDHGQRIKLPEDKALQALERAIALNGALHMLDRDISVVDLRQEARPVVRLGLEAQNAIRQARGQPELGPDG... | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36986
Sequence Length: 340
Subcellular Location: Cell inner membrane
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G3XDA7 | MNGVLLRHQQPGGLGRAPRKPMPRGASRLVAKEPLSVRLPKADFSFLKYLAWPLLLAVLGYGAYRGAEYILPYADRPIAKVSVEGDLSYISQRAVQQRISPYLAASFFTIDLAGMRGQLEQMPWIAHAEVRRVWPDQVVIRLDEQLPIARWGDEALLNNQGQAFTPKELANYEHLPRLHGPQRAQQQVMQQYQLLSQLLRPLGFSIARLEMSDRGGWALTTAQGVEIQIGRDHVVDKIRRFVSIYDKALKDQISNIARIDLRYPNGLAVAWREPVTPATVATASAVQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Location Topology: Single-pass type II membrane protein
Sequence ... |
O30993 | MLALRGRRGKRVRYPADGVAEADEAFVLPRPLRRGVRFLISLGAGRIRFPNHTGTVAAAAFMVATGLYGMSLGGHTQSFAQVSTTAAGFAIEDVRVSGNAQTSEIDILQQLGLDGTTSLVALDIEEARRLIGELPWVETVTVRKVYPGTIEVVLKEREAFGIWQHGSDLSLIERSGSVIAPLRDNKFASLPLFVGRDAETAAAAFYDEFSRWPEFRSRVKAFVRVAGRRWDLRLNNGVVVKLPEKDVARAMSVLAGMQDTHQLLERDIAAVDLRLEDRTTVQLTPEAVKRREVALKAREKMLKAQEKRI | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34205
Sequence Length: 309
Subcellular Location: Cell inner membrane
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P11553 | MKQEVILVLDCGATNVRAIAVNRQGKIVARASTPNASDIAMENNTWHQWSLDAILQRFADCCRQINSELTECHIRGIAVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISAQRLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHDTQFALFGAGAEQNEPVLSSGTWEILMVRSAQVDTSLLSQYAGSTCELDSQAGLYNPGMQWLASGVLEWVRKLFWTAET... | Function: Catalyzes the phosphorylation of L-fuculose. Can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose.
Catalytic Activity: ATP + L-fuculose = ADP + H(+) + L-fuculose 1-phosphate
Sequence Mass (Da): 52259
Sequence Length: 472
Pathway: Carbohydrate degradation; L-fucose degradation; ... |
P44399 | MAIALIFDCGATNLRTIAINEKGQILASHHLANNTKQGIESSDYHIWDIEEIWQKLTSCATQTLNQLMQQGIDLKDIVGISVTTFGVDGAPFDENDQQLYPIISWKCPRTIPVMENLSNQLDIKSLYQRNGIGQYSFNTLFKLHWLKTHKPDVFQKMAKFVFISSMLTQRLTGQFTTDHTMAGTSMMTNLTSGNWDPSILASLGLSNNHFPPMRYAGEKVGKLRTPLAQKWGLNPVPVISCGHDTQFAVFGSGAGLNQPVLSSGTWEILMARTQHAEPRFEFVSQGLTTEFDAQSNCFNPAVQWVGSGVIEWLGKLLFSD... | Function: Catalyzes the phosphorylation of L-fuculose.
Catalytic Activity: ATP + L-fuculose = ADP + H(+) + L-fuculose 1-phosphate
Sequence Mass (Da): 51949
Sequence Length: 470
Pathway: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 2/3.
EC: 2.7.1.51
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Q9FBN6 | MSEYRIEHDSMGEVRVPADAKWRAQTQRAVENFPVSGQRIERAHIEALARIKSAAAKVNAELGVLDEDVAGAIQEAAGEVAEGKWDEHFPVDVFQTGSGTSSNMNTNEVVATLATERLGRDVHPNDHVNASQSSNDVFPSSIHIAATAAVTRDLIPALDHLAGALERKAGEFADVVKSGRTHLMDATPVTLGQEFGGYAAQVRYGIERLQASLPRLAELPLGGTAVGTGINTPPGFSAAVIEEVARATGLPLTEARDHFEAQGARDGIVETSGQLRTIGVGLTKIANDLRWMASGPRTGLAEISLPDLQPGSSIMPGKVN... | Function: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 49068
Sequence Length: 461
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular Location: ... |
O66271 | MEYRIERDTMGEVRVPADKYWGAQTQRSLENFRIGTDRFRMPLEIIRAYGMLKKAAARANLELGELPEEIAKAIIQAAEEVVQGKWDDHFPLVVFQTGSGTQTNMNVNEVIANRASEILGKPLGSKYVHPNDHVNRGQSSNDTFPTAMYVAVALALHQRLYPAVEGLIRTFTAKAQAFDQIVKVGRTHLMDAVPITLGQEIGSWAAQLKTTLAAVKEMEKGLYNLAIGGTAVGTGLNAHPRFGELVAKYLAEETGLPFRVAENRFAALAAHDELVNVMGAIRTLAGALMKIGNDVRWLASGPYAGIGEITIPANEPGSSI... | Function: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 50882
Sequence Length: 466
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular Location: ... |
Q9PD25 | MEMQMSNSDRYRIEHDSMGDLRVPIDALWGAQTQRAIENFPISGRSMPQGFIHALGFIKAAAAKVNAELGLLPKPMAKEIEAAALDVAAGRYDADFPVDIYQTGSGTSSNMNANEVIATLAMRATKEPIHPNDHVNLGQSSNDVVPTAIRISATLAVQGRLLPALKHLRKMINKRARGLGSVVKTGRTHLMDAMPLTFAQEFGAWSAQIVSAEARLNDTLKRLHRLPLGGTAIGTGINTDPHFGRNAVKVLSALTGIHFESANNKFEGLAAQDDLVELSGQFNALAVALMKIANDLRWMNAGPLAGLGEIELPALQPGSS... | Function: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 50505
Sequence Length: 473
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular Location: ... |
Q8ZEB6 | MATTRSEKDSMGSIDVPANQLWGAQTQRSLAHFRISQEKMPTELIHALALTKRAAAQVNMDLGLLPAERAKAIMRAADEVLDGAHPTEFPLAIWQTGSGTQTNMNMNEVLANRASELLGGARGNNRLVHPNDDVNKSQSSNDVFPTAMHVAAVMGVSEHLLPELKVLQKTLADKAEAYRDIVKIGRTHLQDATPLTLGQEISGWAAMLSHSVRHIEATLPHLCELALGGTAVGTGLNTHPEYAVRVANEIATLTRQPFITAPNKFESLGTCDALVHGHGALKGLAASLMKIANDVRWLSSGPRCGIGEISIPENEPGSSI... | Function: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 50129
Sequence Length: 465
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular Location: ... |
P0ACX7 | MGNRTKEDELYREMCRVVGKVVLEMRDLGQEPKHIVIAGVLRTALANKRIQRSELEKQAMETVINALVK | Function: In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 7907
Sequence Length: 69
EC: 4.2.1.2
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P35637 | MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQP... | Function: DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response . Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling ... |
Q8V3T9 | MAFLTILVLFLFKEVLCEPCICENPTCLGITIPQAGFVRSAPGGVLLTETITERPQLTEWTTSRPKLEETLWLDGETKNGKVSQTLFEAIQGTQMENCAVKAVLDTTFVNLTKQDIVLGKIKVSEFGGDSDISKCGRKGLKVFICGGTVGYVTRGCPPEECKGKKGRMMALEPTTDCGVEKGLTTDRIKTGMLDITSCCTQHGCTKGIRVEVPSPVLVSSKCQEVTFRVVPFHSVPDKLGFARTSSFTLKANFVNKHGWSKYNFNLRGFPGEEFIKCCGFTLGVGGAWFQAYLNGMVQGDGAASADDVKEKLNGIIDQIN... | Function: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, p... |
Q786F3 | MGLKVNVSAIFMAVLLTLQTPTGQIHWGNLSKIGVVGIGSASYKVMTRSSHQSLVIKLMPNITLLNNCTRVEIAEYRRLLRTVLEPIRDALNAMTQNIRPVQSVASSRRHKRFAGVVLAGAALGVATAAQITAGIALHQSMLNSQAIDNLRASLETTNQAIEAIRQAGQEMILAVQGVQDYINNELIPSMNQLSCDLIGQKLGLKLLRYYTEILSLFGPSLRDPISAEISIQALSYALGGDINKVLEKLGYSGGDLLGILESRGIKARITHVDTESYFIVLSIAYPTLSEIKGVIVHRLEGVSYNIGSQEWYTTVPKYVA... | Function: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, p... |
P56959 | MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYGQSADTSGYGQSSYGSSYGQTQNTGYGTQSAPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGGSSQSSSYGQPQSGGYGQQSGYGGQQQSYGQQQSSYNPPQGYGQQNQYNSSSGGGGGGGGGNYGQDQSSMSGGGGGGGYGNQDQSGGGGGGYGGGQQDRGGRGRGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTD... | Function: DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response. Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling t... |
P35949 | MIPGRIFLVLLVIFNTKPIHPNTLTEKYYESTCSVETAGYKSALRTGWHMTVMSIKLSQINIESCKSSNSLLAHELAIYSSAVDELRTLSSNALKSKRKKRFLGLILGLGAAVTAGVALAKTVQLESEIALIRDAVRNTNEAVVSLTNGMSVLAKVVDDLKNFISKELLPKINRVSCDVHDITAVIRFQQLNKRLLEVSREFSSNAGLTHTVSSFMLTDRELTSIVGGMAVSAGQKEIMLSSKAIMRRNGLAILSSVNADTLVYVIQLPLFGVMDTDCWVIRSSIDCHNIADKYACLARADNGWYCHNAGSLSYFPSPTD... | Function: Inactive precursor that is cleaved by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.
PTM: The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed by a host furin-like protease probably in the Golgi.
Location Topology: Single-p... |
P11236 | MKVFLVTCLGFAVFSSSVCVNINILQQIGYIKQQVRQLSYYSQSSSSYIVVKLLPNIQPTDNSCEFKSVTQYNKTLSNLLLPIAENINNIASPSSGSRRHKRFAGIAIGIAALGVATAAQVTAAVSLVQAQTNARAIAAMKNSIQATNRAVFEVKEGTQRLAIAVQAIQDHINTIMNTQLNNMSCQILDNQLATSLGLYLTELTTVFQPQLINPALSPISIQALRSLLGSMTPAVVQATLSTSISAAEILSAGLMEGQIVSVLLDEMQMIVKINIPTIVTQSNALVIDFYSISSFINNQESIIQLPDRILEIGNEQWSYP... | Function: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, p... |
Q96IV6 | MKGEAGHMLHNEKSKQEGHIWGSMRRTAFILGSGLLSFVAFWNSVTWHLQRFWGASGYFWQAQWERLLTTFEGKEWILFFIGAIQVPCLFFWSFNGLLLVVDTTGKPNFISRYRIQVGKNEPVDPVKLRQSIRTVLFNQCMISFPMVVFLYPFLKWWRDPCRRELPTFHWFLLELAIFTLIEEVLFYYSHRLLHHPTFYKKIHKKHHEWTAPIGVISLYAHPIEHAVSNMLPVIVGPLVMGSHLSSITMWFSLALIITTISHCGYHLPFLPSPEFHDYHHLKFNQCYGVLGVLDHLHGTDTMFKQTKAYERHVLLLGFTP... | Function: Promotes megakaryocyte differentiation by enhancing ERK phosphorylation and up-regulating RUNX1 expression.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39002
Sequence Length: 333
Subcellular Location: Cytoplasm
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Q9GKT2 | MKGEAGHMLHNEKSKQEGYIWGSMRRTAFILGSGLLSFVAFWNSVTWHLQRFWGASGYFWQAQWERLLTTFEGKEWILFFIGAIQVPCLFFWSFNGLLLVVDTTGKPNFISRYRIQVGKNEPVDPVKLRQSIRTVLFNQCMVSFPMVVFLYPFLKWWGDPCRRELPTFHWFLLELAIFTLIEEVLFYYSHRLLHHPTFYKKIHKKHHEWTAPIGVISLYAHPIEHVVSNMLPAIVGPLVMGSHLSSITMWFSLALIITTISHCGYHLPFLPSPEFHDYHHLKFNQCYGVLGVLDHLHGTDTMFKQTKAYEKHVLLLGFTP... | Function: Promotes megakaryocyte differentiation by enhancing ERK phosphorylation and up-regulating RUNX1 expression.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38885
Sequence Length: 333
Subcellular Location: Cytoplasm
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O75084 | MRDPGAAAPLSSLGLCALVLALLGALSAGAGAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGPGGGPTAYPTAPYLPDLPFTALPPGASDGRGRPAFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFS... | Function: Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC an... |
Q61090 | MRGPGTAASHSPLGLCALVLALLGALPTDTRAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGAGGSPTAYPTAPYLPDPPFTAMSPSDGRGRLSFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFSDD... | Function: Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC an... |
Q9IA03 | AGAAELQPELAVAEHVRYESTGPALCTVVFLLVYFFGMASSIWWVILSLTWFLAAGMKWGNEAIAGYAQYFHLAAWLLPSVKSIAVLALSSVDGDPVAGICYVGNQSLENLRGFVLAPLVVYLFTGSLFLLAGFVSLFRIRSVIKQGGTKTDKLEKLMIRIGIFTVLYTVPATIVIACYIYEQHNREAWEQAQNCSCPGDPHRPKPDYAVFMLKYFM | Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC... |
Q61091 | MEWGYLLEVTSLLAALAVLQRSSGAAAASAKELACQEITVPLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVCERAKAGCAPLMRQYGFAWPDRMRCDRLPEQGNPDTLCMDYNRTDLTTAAPSPPRRLPPPPPPGEQPPSGSGHSRPPGARPPHRGGSSRGSGDAAAAPPSRGGKARPPGGGAAPCEPGCQCRAPMVSVSSERHPLYNRVKTGQIANCALPCHNPFFSQDERAFTVFWIGLWSVLCFVSTFATVSTFLIDMERFKYPERPIIFLSACYLFV... | Function: Receptor for Wnt proteins. Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes (By similarity). The beta-catenin canonical signaling pathway leads to the activation of disheveled proteins, in... |
O93274 | MESLSLSLLLLVSWLQGSQCAAAKELSCQEITVPLCKDIGYNYTYMPNQFNHDTQDEAGMEVHQFWPLVVIHCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVCERARAGCAPLMRQYGFAWPDRMRCDRLPEQGNPDTLCMDYYNRTEQTTAAPSHPEPPKPPARSVPKGRTRVEPPRSRSRATGCESGCQCRAPMVQVSNERHPLYNRVRTGQIPNCAMPCHNPFFSPEERTFTEFWIGLWSVLCFASTFATVSTFLIDMERFKYPERPIIFLSACYLLVSTGYLIRLIAGHEKVACSRGELDLEHIIHYETTGPALC... | Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC... |
Q9IA02 | ACDNPEKFQYVEKSLSCAPRCSPGVDVYWSREDKDFAFVWMAVWSTLCFVSTAFTVLTFLLDPHRFQYPERPIIFLSMCYNVYSVAFIIRSVAGAETIACDRENGELYIIQEGLESTGCTIVFLILYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEAHSSYFHMAAWGIPAMKTIVILTMRKVAGDELTGLCYVGSMDVSALTGFVLIPLSCYLVVGTSFILTGFVALFHIRKIMKTGGTNTEKLEKLMVKIGVFSILYTVPATCVIVCYFYERLNVDYWNLRALERACVPLPGRRAADCSLEASVPTVAVFMLKIFM... | Function: Receptor for WNT2 that is coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43899... |
Q9R216 | MAVPPLLRGALLLWQLLATGGAALEIGRFDPERGRGPAPCQAMEIPMCRGIGYNLTRMPNLLGHTSQGEAAAQLAEFSPLVQYGCHSHLRFFLCSLYAPMCTDQVSTPIPACRPMCEQARLRCAPIMEQFNFGWPDSLDCARLPTRNDPHALCMEAPENATAGPTEPHKGLGMLPVAPRPARPPGDSAPGPGSGGTCDNPEKFQYVEKSRSCAPRCGPGVEVFWSRRDKDFALVWMAVWSALCFFSTAFTVFTFLLEPHRFQYPERPIIFLSMCYNVYSLAFLIRAVAGAQSVACDQEAGALYVIQEGLENTGCTLVFLL... | Function: Receptor for WNT2 that is coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). Plays a role in neuromuscular junction (NMJ) assembly by... |
Q1KPV0 | MRTLISHRQCVTSPFLISAASPPFPGRCFKLSSFTPPRHRRFSSLSIRNISHESADQTSSSRPRTLYPGGYKRPELAVPGLLLRLDADEVMSGNREETLDLVDRALAKSVQIVVIDGGATAGKLYEAACLLKSLVKGRAYLLIAERVDIASAVGASGVALSDEGLPAIVARNTLMGSNPDSVLLPLVARIVKDVDSALIASSSEGADFLILGSGEEDTQVADSLLKSVKIPIYVTCRGNEEAKEELQLLKSGVSGFVISLKDLRSSRDVALRQSLDGAYVVNNHETQNMNELPEKKNSAGFIKLEDKQKLIVEMEKSVLR... | Function: Probable membrane-remodeling GTPase that plays a unique role in the in the determination of thylakoid and chloroplast morphology and regulates organization of the thylakoid network. Not involved in the determination of mitochondrial morphology or ultrastructure.
Location Topology: Multi-pass membrane protein
... |
Q23424 | MSGTASLVHTLPASGDSNHRGLHSLKNSRRAADNEPLLRFREAKKVLGDVYGELKDNVAELEGVYKDIKENDFVSSEQREEIEAIGDSIKTIMDTFQRDNMKVVFFGRTSNGKSTTINAMLHEKVLPQGMGHTTCCFLQVEGSEGEVGHLQLDDNPQKIDMKMLGKIGHALSDENSDLPAMGQDSLLKVFHPKKSESGECRLLQNDVVILDSPGVDLSPEFDSWIDKHCLDADVFVLVSNAESTLTQAEKNFFLRVAKKLSKPNVFILNNRWDASAAETENIEDVKKQHLTRFRQFLVDELEVCSEREVNDRIFFVSSRE... | Function: Probable transmembrane GTPase (By similarity). Mediates mitochondrial fusion . Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission (By similarity). Dispensable for normal apoptotic processes during embryoni... |
Q9USY7 | MEKSARQLSVAEQNGESGRLNNGYTSNNIQQYKDETNRHQFEYNQNRNQLLRSIHIIQNLLNELDNYVDRSDCLFHSVWRTDKEKSKFSGNYYPFSPSKMNVITIDLSLRSSSTADEKLISQLGEEAHESLLKVHIEKANKHLFSLFSRVEDTSSKILITGDLNAGKSTLCNALVHKDILPEDQQPCTEVFCEVHDAELNDGKDCVHAIPHGLTYSHTDSSTYKVFPIEDLKRLVYETENWSMLIVYVNDGRPAHESLLHNGITDIALIDAPGLNTDSMKTTSVFACQEEIDVVVFVVNAENHFTLSATDFLRNASTEKS... | Function: Probable transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondrial morphology, which is balanced between fusion and fission (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topo... |
P38297 | MSEGKQQFKDSNKPHKDSTDQDDDAATIVPQTLTYSRNEGHFLGSNFHGVTDDRTTLFDGEEGRREDDLLPSLRSSNSKAHLISSQLSQWNYNNNRVLLKRSILKTQAFMDQLQEENNIRPIFIAANDEREKLHVLQLNIKLDGQYNTKEKNGFNIEKKALSKLFHSQIVSVTNHLNALKKRVDDVSSKVFITGDVNTGKSALCNSLLKQRLLPEDQLPCTNVFSEILEARENDGIEEVHAIPLNIAPTLKEAIDMYSIQNPKTYEIHTLKELPDLVPQNGKYALLKIYIKDDKRPASTSLLRNGTVDISLIDSPGLNMD... | Function: Essential transmembrane GTPase, which mediates mitochondrial fusion . Fusion proceeds through several steps; first mitochondria are tethered together, then brought into close contact, followed by the formation of a docking ring around contact areas, and finally membrane fusion . Fusion of mitochondria occurs ... |
O18412 | MAESDSGESTSSVSSFISSSSSSRLSEFVDAKTELQDIYHDLSNYLSNFLTILEETVLLKDRQMLEHLCAFSSRVEAIAKVLSRDRMKVAFFGRTSNGKSAVINALLHEKILPSAMGHTTSCFCQVQANGSNETEHVKVEQEDEHMELSALSQLASAHSPGALKPSTLLQVNMAKNRCSILDYDVVLMDTPGVDVTAQLDDCLDSYCMDADVFILVLNAESTVSRVERQFFKDVASKLSRPNLFILNNRWDKASSLEPEMEQKVKDQHMERCVNLLVDELGVYSTAQEAWERIYHVSALEALHIRNGQITNPSGQTQQRY... | Function: Essential transmembrane GTPase, which mediates mitochondrial fusion during spermatogenesis . In early spermatocytes, fusion of mitochondria give rise to two organelles named Nebenkern and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission . Essential for fer... |
Q96UF1 | MSTINTGINGFRSHWPYCLACSLENPKVKVVAINDPFIDLEYMVYMFKYDSTHGRFKGTVEHKDGKLVVNGHEIAVHAERDPAQIPWGSHGADYVIESTGVFTTKDAASAHLKGGAKKVIISAPSADAPMFVVGVNLDKYTSDLTVISNASCTTNCLAPLAKVIHDNYGILEGLMTTVHATTATQKTVDGPSNKDWRGGRGAGANIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPDVSVVDLTVRLEKPASYDEIKATIKKASESEELKGILGYTEDQVVSTDFVGDAHSSIFDAKAGIQLSPTFVKLISWYDNEFG... | Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 36302
Sequence Length: 339
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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P58559 | MKVRVGINGFGRMGRLALRAAWDWPELEFVHINEIKGGAVAAAHLLKFDSVHGRWTPEVEAEGERVLIDGTPLSFSEYGKPDDVPWEDFGVDLVLECSGKFRTPATLDPYFKRGVQKVIVAAPVKEEALNIVMGVNDYLYEPEKHHLLTAASCTTNCLAPVVKVIHEGLGIKHGIITTIHDNTNTQTLVDAPHKDLRRARATSLSLIPTTTGSATAIALIYPELKGKLNGIAVRVPLLNASLTDCVFEVTRPTTVEEINALLKAASEQAPLQGILGYEERPLVSIDYKDDPRSSIIDALSTMVVDETQVKILAWYDNEWG... | Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester,... |
P25856 | MASVTFSVPKGFTEFSGLRSSSASLPFGKKLSSDEFVSIVSFQTSAMGSSGGYRKGVTEAKLKVAINGFGRIGRNFLRCWHGRKDSPLDIIAINDTGGVKQASHLLKYDSTLGIFDADVKPSGETAISVDGKIIQVVSNRNPSLLPWKELGIDIVIEGTGVFVDREGAGKHIEAGAKKVIITAPGKGDIPTYVVGVNADAYSHDEPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKTFAEEVNA... | Function: Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-diphosphoglycerate by NADPH (By similarity).
Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Location Topology: Pe... |
P50362 | MAAMMQKSAFTGSAVSSKSGVRAKAARAVVDVRAEKKIRVAINGFGRIGRNFLRCWHGRQNTLLDVVAINDSGGVKQASHLLKYDSTLGTFAADVKIVDDSHISVDGKQIKIVSSRDPLQLPWKEMNIDLVIEGTGVFIDKVGAGKHIQAGASKVLITAPAKDKDIPTFVVGVNEGDYKHEYPIISNASCTTNCLAPFVKVLEQKFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTTTGAAKAVSLVLPSLKGKLNGIALRVPTPTVSVVDLVVQVEKKTFAEEVNAAFREAANGPMKGVLHVEDAPLVS... | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 40304
Sequence Length: 374
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 1.2.1.13
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P09315 | MASSMLSATTVPLQQGGGLSEFSGLRSSASLPMRRNATSDDFMSAVSFRTHAVGTSGGPRRAPTEAKLKVAINGFGRIGRNFLRCWHGRGDASPLDVIAINDTGGVKQASHLLKYDSTLGIFDADVKPVGDNAISVDGKVIKVVSDRNPSNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADQYNPDEPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKT... | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 42867
Sequence Length: 403
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 1.2.1.13
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P12858 | MASATFSVAKPAIKANGKGFSEFSGLRNSSRHLPFSRKSSDDFHSLVTFQTNAVGSSGGHKKSLVVEAKQLKVAINGFGRIGRNFLRCWHGRKDSPLDVIAINDTGGVKQASHLLKYDSTLGIFDADVKPVGTDGISVDGKVIKVVSDRNPANLPWKELGIDLVIEGTGVFVDREGAGRHITAGAKKVLITAPGKGDIPTYVVGVNADAYTHADDIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPTLKGKLNGIALRVPTPNVSVVDLVVQVSK... | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 43338
Sequence Length: 405
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 1.2.1.13
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P19866 | MASNMLSIANPSLRVYNKGFSEFSGLHTSSLPFGRKGSDDLMAFVSFQTNAVGGKRSSQNGVVEAKLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVINDTGGVKQASHLLKYDSILGTFDADVKTAGDSAISVDGKVIKVVSDRNPVNLPWGDMGIDLVIEGTGVFVDRDGAGKHLQAGAKKVLITAPGKGDIPTYVVGVNEEGYTHADTIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAACLNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKTFA... | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 43023
Sequence Length: 401
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 1.2.1.13
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A0QWW2 | MTIRVGVNGFGRIGRNFYRALATQKAEGKNTDIEIVAVNDLTDNATLAHLLKFDSILGRLPQDVSLEGDDTIVIGDTKIKALEVKEGPAALPWGDLGVDVVVESTGIFTNAAKAKGHLDAGAKKVIISAPATDEDITIVLGVNDDKYDGSQNIISNASCTTNCLGPLAKVLNDEFGIVKGLMTTIHAYTQDQNLQDGPHKDLRRARAAALNIVPTSTGAAKAIGLVLPELKGKLDGYALRVPIPTGSVTDLTAELAKSASVEDINAAMKAAAEGPLKGILKYYDAPIVSSDIVTDPHSSLYDAGLTKVIDNQAKVVSWYD... | Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester,... |
P83601 | VKVGINGFGRIGRXVFRA | Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 1958
Sequence Length: 18
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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O42259 | MSDLCVGINGFGRIGRLVLRACLQKGIKVVAINDPFIDLQYMVYMFKYDSTHGRYKGEVSMEDGKLIVDDHSISVFQCMKPHEIPWGKAGADYVVESTGVFLSIDKASSHIQGGAKRVVVSAPSPDAPMFVMGVNEDKFDPSSMTIVSNASCTTNCLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSVVELTCRLSRPGSYAEIKGAVKKAAEGPMKGYVGYTEYSVVSSDFIGDTHSSMFDAGAGISFNDNFVKLISWYDNEFGY... | Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate... |
Q8X1X3 | MVVKVGINGFGRIGRIVFRNAVEHDDVEIVAVNDPFIETKYAAYMLKYDSTHGQFKGDIQHSSSNNLTVNNKTIHFYQERDPANIPWGKHGVDYVVESTGVFTTTEKAKAHLSGGAKKVIISAPSADAPMFVMGVNEKSYRPDISVLSNASCTTNCLAPLAKVIHDNFGIAEGLMTTIHSYTATQKTVDGPSHKDWRGGRTAAQNIIPSSTGAAKAVGKVIPALNGKLTGMAMRVPTANVSVVDLTCRTEKPVTYDQIKAAVKAASEGELKGILGYSEDALVSTDLNGDPRSSIFDASAGIALNDRFVKLISWYDNEWGY... | Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 36470
Sequence Length: 338
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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Q5R2J2 | MVKIGVNGFGRIGRLVTRAAFTCDKVQIVAINDPFIDLNYMVYMFKYDSTHGRFHGTVKAENGKLVINGQAITIFQERDPANIKWGDAGAEYVVESTGVFTTTEKASAHLKGGAKRVVISAPSADAPMFVMGVNHEKYDNSLKVVSNASCTTNCLAPLAKVIHDNYGMVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLQKPAKYDDIKKVMKAASEGPLKGILGYTEDQVVSSDFNGDSRSSIFDAAAGIALNDNFVKLVSWYDNEFGYSN... | Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate... |
Q6L125 | MIKVGINGYGTIGKRVAYAASIQDDIHVSGIVKNTPDYMAYLASRSFNIYVPDDDKIKEFEDHGIKVKGTLNDLMESSDIIVDATPEGMGMENIKIYKKKRVKAIFQGGEKSNIGDASFNAYSNYNESFKREYTRVVSCNTTALARTLYPILNDYGIENLNVTLIRRATDPNDNRKGPINAIEPSMSFPSHHADDLKTVLNLNNVYTVALKAPTTLMHVHSIEVLLKDDAKIDDIMESWLKYNRILLIEGKDNFKSTAQIMDMARELRRDRGDLYEIAIWRDSVKVIDKRLYYVQAVHQESDVIPENIDAIRSLSGIDKN... | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 38559
Sequence Length: 341
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.59
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Q43793 | MVTLYSSPSTHSSGPVASYSNSSIGLYNYHHNKQIAVSSILSRKFGSLQINQKPFWNAVRMQDGAVATPPSKIENETPLKKLKNGILPVAPPKEQKDTIDFDSNKAKSTVSITVVGASGDLAKKKIFPALFALYYEGCLPEHFTIFGYARSKMTDAELRNMVSKTLTCRIDKRENCGEKMEQFLERCFYHSGQYDSLENFAELDKKLKEHEAGRFSNRLFYLSIPPNIFINAVRCASLSASSAHGWTRVIVEKPFGRDSESSAALTRSLKQYLNEDQIFRIDHYLGKELVENLSVLRFSNLIFEPLWSRQCIRNVQFIFS... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are invo... |
P48826 | MASTIARTEERQNAGTMELKDDTVIIVLGASGDLAKKKTFPALFGLYRNKFLPKGIKIVGYARTNMDHEEYLRRVRSYIKTPTKEIEEQLDSFCQFCTYISGQYDKDDSFINLNKHLEEIEKGQKEQNRIYYMALPPSVFTTVSDQLKRNCYPKNGVARIIVEKPFGKDLQSSRDLQKALEPNWKEEEIFRIDHYLGKEMVKNILIMRFGNEFFNATWNRHHIDNVQITFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQVLTLLAMERPISFSAEDIRDEKVRVLRAMDAIEPKNVIIGQYGKSLDGSKPAYKEDETVPQ... | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity... |
P54547 | MKTNQQPKAVIVIFGATGDLAKRKLYPSIHRLYQNGQIGEEFAVVGVGRRPWSNEDLRQTVKTSISSSADKHIDDFTSHFYYHPFDVTNPGSYQELNVLLNQLEDTYQIPNNRMFYLAMAPEFFGTIAKTLKSEGVTATTGWSRLVIEKPFGHDLPSAQALNKEIREAFTEDQIYRIDHYLGKQMVQNIEVIRFANAIFEPLWTNRYISNIQITSSESLGVEDRARYYEKSGALRDMVQNHIMQMVALLAMEPPIKLNTEEIRSEKVKVLRALRPIAKDEVDEYFVRGQYHAGEIDGVPVPAYTDEDNVAPDSNTETFVA... | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 55632
Sequence Length: 489
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate fr... |
O51581 | MKERSVSNFDIVIFGVTGNLSRKKLIPSLFNLFKNKCISNFRVIGFSRKIFTDKEFRLYIKDSLWQEETDSLIEIFLNFFVYVFGDFNEKESYKNLFKFLDRSRETIYYLSTSPAFYGPIINHLKKYFLSEKLTLSKIVLEKPFGSSLETAKKLNSLLYSAFKEDQIYRIDHYLGKETVQNIFTFRFGNSIFENIWNNRYVDFVQITVAEELGLDGRVEYYDSVGALKDMVQNHILQLLSLVAMESPIKFDSEFIHDEKVKVLKSLRKISKEDIKNYIVKGQYIGSQVQGVFKKGYKDETEFLGNSNTETYLAMKVFINN... | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 56113
Sequence Length: 478
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate fr... |
Q27464 | MACKRHSVSDPISKDLVECLRESMQRDLKFETPYVFVIFGASGDLAKKKIYPTLWWLFRDNLLPVNIKFIGYARSDLTVFKLRESFEKNCKVRENEKCAFDDFIKKCSYVQGQYDTSEGFQRLQSSIDDFQKESNNQAVNRLYYLALPPSVFNVVSTELKKNCMDHGDSWTRVIIEKPFGHDLKSSCELSTHLAKLFKEDQIYRIDHYLGKEMVQNLMVMRFGNRILAPSWNRDHIASVMISFKEDFGTGGRAGYFDTAGIIRDVMQNHLMQILTLVAMEKPASLNAEDIRDEKVKVLKAAKVVELKDVVVGQYIASPEF... | Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty a... |
Q9Z8U6 | MTNVVQETIGGLNSPRTCPPCILVIFGATGDLTARKLLPALYHLTKEGRLSDQFVCVGFARREKSNELFRQEMKQAVIQFSPSELDIKVWEDFQQRLFYHRSEFDNNMGYTSLKDSLEDLDKTYGTRGNRLFYLSTPPQYFSRIIENLNKHKLFYKNQDQGKPWSRVIIEKPFGRDLDSAKQLQQCINENLNENSVYHIDHYLGKETVQNILTTRFANTIFESCWNSQYIDHVQISLSETIGIGSRGNFFEKSGMLRDMVQNHMMQLLCLLTMEPPTTFDADEIRKEKIKILQRISPFSEGSSIVRGQYGPGTVQGVSVL... | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 58740
Sequence Length: 512
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate fr... |
Q23711 | LWWLFRDNLLPSVTKFVGYARTKLTVAELKEKCHPYMKVDAAHEEKYDEFWALNFYVAGSYDGRRDFELLNQEIGKFEVGKTANRLFYLRLPPSVFETVTVHIRNTCMGLKGWNRIIVEKPFGRDADSSNKLSEHLAKLFTEDQLYRIDHYLG | Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty a... |
P37986 | MAVTSTAQACDLVIFGAKGDLARRKLLPSLYQLEKAGHIHPETRIIGVGRAEWDRDAYIKVVREALETFLKEPLDPALWTTLSNRLDFCNLDVEDTEGFKRLGTMLDQQNRTTINYFAMPPSTFGAICRGLGQAGLNKEPARVVMEKPLGTNLASSRVINNQVAEFFNECQVYRIDHYLGKETVLNLLALRFANSLFANNWDNRTIDHVQITVAEEVGIEGRWGYFDQAGQMRDMIQNHLLQILTMIAMSPPADLSTDRIRDEKVKVLRSLRRIDRSNVHEVTVRGQYTSGFVQGKKVPGYLEEEGANKTSNTETFVAIR... | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 56034
Sequence Length: 491
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate fr... |
Q557D2 | MTSTPDSRSVLTVIILGASGDLAKKKTYPALFGLYLRDLLPSNTIIYGYARSHIEIGDFKARISKGLKGDEEKKKQFLNLLHYHSGKYDEKASYDEFEKLILAEEKKQQGVDKFNRLFYMAIPPSIFIEVSIGIHGSLISKNGWSRVIVEKPFGRDLASSRELVSELGKLFKEKDLFRIDHYLGKEMVQNLMVLRFANAVFEPLWSKSHISSITITFKEDIGTEGRGGYFDQFGIIRDVMQNHLLQVLSLVAMEPPVSLNADDITNEKVKLLRCIQPIKMSEVVLGQYTSDPEGKIPAYLDDEGVPKDSTTPTYAAAVFH... | Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty a... |
P15588 | MAEQVALSRTQVCGILREELYQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIEPASFQRLNTHMNSLHHGAQANRLFYLALPPIVYEAVTKNIKETCMSQDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKDELQEAWRIFTPLLHHIEREKTQPIPYVYGSRGPPEADELMKRVGFQYEGTYKWVNPHKL | Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty a... |
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