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Full Name
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sequence
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2.75k
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5.51k
AlphaFoldDB
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10
A8EZP5
FPG_RICCK
DNA-(apurinic or apyrimidinic site) lyase MutM
belli group
MPELPEVETLKNSLKDKLIGLIIKNIELKRDNLRYNLSPLLTTEILNTNILNVRRRAKYLIIDFGNYYSLVIHLGMSGRFTVQPANYKIQKHDHVIFDLNNCEKLIFNDTRRFGMVYSFKTNFLEEKFFYNLGIEPLSDLLTLEYLKSKLITRTIAIKNLIMDNKIIVGVGNLYASESLHLARIHPHKLGRNLKDDEIENLIKSIREVLTKAITAGGTTLKNFVNGDSKPGYFTQQLRVYGREGQKCFNCSSTILKTKNSGRSTFYCKTCQYT
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
A8EZP5
Q82AG6
END4_STRAW
Endonuclease IV
Streptomyces
MNNQQSRGALGTSGATPDLPDATPGLSRNPVGGHVPVAGGLHSVGLAYARDLAAEAVQVFVANPRGWATPAGNPRQDEEFRAACAAESIPAYVHAPYLINFGSHTEATVEKSVESLRHSLRRGREIGALGVVVHTGSATGGRERSVALAQVREHLLPLLDELTHDDDPYLLLESTAGQGASLCSRTWDFGPYFEALDAHPKLGVCLDTCHIFAAGHDLTGPSGMHQTLDLLVDTVGEGRLKLIHANDSKDVVGAHKDRHENIGSGHIGEDPFRALMTHPATEGVPLIIETPGGKEGHAADVEQLKKLRDG
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Q82AG6
Q4ZM01
METK_PSEU2
Methionine adenosyltransferase
Pseudomonas syringae
MSEYSLFTSESVSEGHPDKIADQISDAVLDAIIAEDKYARVACETLVKTGVAIIAGEVSTSAWVDLEDIVRNVILDIGYNSSDVGFDGATCGVMNIIGKQSVDIAQGVDRSKPEDQGAGDQGLMFGYASNETDVLMPAPITFSHQLVQRQAEARKSGLLPWLRPDAKSQVTCRYENGKVVGVDAIVLSTQHNPDVSYKDLREGVMELIVKHVIPAHLLHKDTQFHINPTGNFIIGGPVGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAGRYVAKNIVAAGLAERCEIQVSYAIGVAQPTSISLNTFGTGKLSDDKIIKLVRDNFDLRPYAITTMLDLLHPMYQATAAYGHFGRIPVEMTVGDDTFTAFTWEKTDRADALRAAAGL
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Q4ZM01
Q72M34
COBS_LEPIC
Cobalamin-5'-phosphate synthase
Leptospira
MNKLQEEWNRFCASWMFNTRLPILPFYVYSESTLSRSSRYFPLIGWIVSAGTSYSTYFLSWILPIEISIILGMILSVLITGGFHEDGLADVCDAFGGGWSKEKILEIMKDSRIGTFGSIGLILSLGLKYLLLVNLFKISPWIFLFTSWFSHSASRWFALLLMMLIPYARENDLSKSKPMIKKLPPFDFALSTFFGCFPAVYFLYQFQNQIPNVLLGFFLSSIFVFYFRNYFNKWIEGFTGDCLGFIQQGTELLFYLGITVSWNSI
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Q72M34
C3K1G9
TRMD_PSEFS
tRNA [GM37] methyltransferase
Pseudomonas
MANLRIEVISLFPEMFSAISEYGITSRAVKQGLLQLTCWNPRDYTTDRHHTVDDRPFGGGPGMVMKIKPLEDALAQAKAAAGEKAKVIYLSPQGRQLKQAGVRELANEEALILIAGRYEGIDERFIEAHVDEEWSIGDYVLSGGELPAMVLIDAVTRLLPGALGHADSAEEDSFTDGLLDCPHYTRPEVYADQRVPDVLLSGNHAHIRRWRLQQSLGRTYERRADLLESRSLSGEEKKLLEEYILARDDS
Specifically methylates guanosine-37 in various tRNAs.
C3K1G9
Q9PWI3
PLIGB_ELAQU
Phospholipase A2 inhibitor gamma subunit B
Elaphe
MKFLLFCCLFGTFLATGMCIDCEHCVVWGQNCTGWKETCGENEDTCVTYQTEVIRPPLSITFTAKTCGTSDTCHLDYVEANPHTELTLRAKRACCTGDECQTLPPPVLEPQVNRPNGLQCPGCIGLTSTECNEYLVSCQGSENQCLTIILKKPDFSLSEMSFKGCASENLCLLFEKKFWRFLEASEVDVKCTPAVPQTSQ
Inhibits the enzymatic activity of phospholipase A2 (PA2).
Q9PWI3
C0STK6
PLIAL_ELACL
Phospholipase A2 inhibitor alpha-like protein
Elaphe
MQLILLSSLLLLGLSLANGHETDPEGQILNSLVETVSRLEKKIDKVENAFLTVHRARSFGSGSERLYVTNKQVGNFEAVRNTCVQAGGRIPSPQLLNENKAFASVLERHNKAAYLVVQNSAKFTNWAAGEPNNADGNKLCVKADAQGAWHSASCDEDLLVVCEFSFI
Has no PLA2 inhibitory activity.
C0STK6
Q6LPG9
FABV1_PHOPR
Enoyl-[acyl-carrier-protein] reductase [NADH] 1
Photobacterium
MIIKPKIRGFICTTAHPVGCEENVKEQIAYTKAQGPIANAPKRVLVVGSSSGYGLSSRIAAAFGGDAATIGVFFEKPSTEKKPGTAGWYNSAAFDKLAKEEGLYSKSLNGDAFSHEAKQKTIDLIKADLGQIDMVVYSLASPVRKMPETGEVVRSSLKPMGETYTATAVDTNKDVLIEASIEPATEQEIADTVTVMGGQDWELWINALSEAGVLADGCKTVAYSYIGTEITWPIYWHGALGKAKMDLDRAASELNNKLSATGGSANVAVLKSVVTQASSAIPVMPLYIAMVFKKMREEGVHEGCMQQIYRMFTQRLYKADGTAPEVDEENRLRLDDWELREDIQKHCRDLWSSVTNENLFEVADYQEYKDEFIKLFGFGIDSIDYDIDVNTLIEFDVESI
Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP).
Q6LPG9
A8ACU7
WECG_CITK8
UDP-N-acetyl-D-mannosaminuronic acid transferase
Citrobacter
MTDNTTAPLYSLRGLQLIGWRDMQHALNYLFADGQMKQGTLVAINAEKMLTAEDDPEVRALIDAAEFKYADGISVVRSVRKKFPQAQVSRVAGADLWEELMARAGKEGTPVFLVGGKPEVLAQTEAKLRAQWNVNIVGSQDGYFKPEQRQALFERIHASGAKIVTVAMGSPKQEILMRDCRVIHPQALYMGVGGTYDVFTGHVKRAPKMWQTLGLEWLYRLLSQPSRITRQLRLLRYLRWHYTGNL
Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA (Lipid II), the second lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis.
A8ACU7
B8I2B3
YIDD_RUMCH
Putative membrane protein insertion efficiency factor
Ruminiclostridium
MLKRILISIIRFYQRFISPIKVRPTCRFYPTCSQYAIEAVTKYGCVKGTFLALKRILKCHPFHPGGFDPIK
Could be involved in insertion of integral membrane proteins into the membrane.
B8I2B3
B7KGN0
GATB_GLOC7
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Gloeothece citriformis
MVTATPVKTEYEAIIGLETHCQLNTHSKIFCNCSTKFDSPPNTNVCPICLGYPGVLPVLNLEVLASAVKMGLAINGKIASYSKFDRKQYFYPDLPKNYQISQYDLPIVEQGSLEIEVVDKETKEVTRKTIGITRLHMEEDAGKLVHAGSDRLAGSTYSLVDFNRTGVPLLEIVSEPDLRSGQEAAEYAQELRRLVRYLGISDGNMQEGSLRCDVNISVRPKGQKKFGTKVEIKNMNSFSAIQKAIEYEIERQIEAIENGEPIRLETRLWEEGKQRTVTMRLKEGASDYRYFPEPDLPPIEVSQEQIETWKAQIPELPAQKRTRYETELGLSAYDARVLTDEREVAEYFETAVATGANAKLVANWVTQDIAAYLNNNKLNIGEIALKSEGLGELVNLIEEGTISGKIAKDILPELLTDGGSPKTLVEKKGLIQISDTGELEKIIDEVIASHPKELEKYRSGKKNLKGFFVGQVLKKTGGRADPKLTNQLLDKKLEA
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
B7KGN0
B6EJS8
DAPE_ALISL
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Aliivibrio
MPDTPTLTLAKDLLSRQSVTPEDAGCQELMIKRLKALGFTIEIMVFEDTTNFWARRGTEAPLFTFAGHTDVVPTGSLTQWNTDPFEPTIIDGMLYARGAADMKGSLACMIVAVERFISEHPEHKGSLSFLITSDEEGPFINGTTRVVDTLKERNEIIDMCIVGEPSSTQYVGDVVKNGRRGSLTGNLTVKGIQGHVAYPHIARNPIHQSMAALLELTMTEWDLGNAYFPPTSFQIPNMNSGTGASNVIPGTAEIMFNFRFSTESTVEGLQQRVIELLDKHNLEYDLDWIINGLPFLTDTGDLLTAVVDAVATVNQQKPELLTTGGTSDGRFIAQMGSQVIELGPVNATIHKVNECVKVDDLEKLTDMYQEVLNNLLA
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
B6EJS8
Q255H0
BIOD_CHLFF
Dethiobiotin synthase
Chlamydia
MHIIIAGIDTEVGKTFVSAILATLFQAEYWKPIQSGSLDRSDSTIVRELSGAVCHRETYRLTHPLAAHQAARVDNIPIHAENFSLPVTEAPLIIETSGGFLSPCSQDSLQGDVFSKWPCQWVLVSKAYLGSINHTCLTVEAMRTRNLNILGMVLNQYPKEEEDWLLNMTGIPYLGRLNYENIISKETVKNYANLWKETWEDREAKLCS
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Q255H0
A7MU26
GUAA_VIBC1
Glutamine amidotransferase
Vibrio
MTKNIHDQRILILDFGSQYTQLVARRVREIGVYCELWSWDVEEADIREFNPDGIILSGGPESVTEDNSPRAPQYVFDSGVPVLGVCYGMQTMAEQLGGKVAGSTEREFGYAQVKVSGESALFKDLELTQDVWMSHGDKVVEIPADFVKVGETDTCPYAAMANEEKKYYGVQFHPEVTHTKGGLQMLENFVLGVCGCERLWTSESIIEDAVARIKEQVGDDEVILGLSGGVDSSVVAMLVHRAIGDKLTCVFVDNGLLRLNEGQQVMDMFGDQFGLNIIKVDAEDRFLKALEGKSDPEEKRKTIGHVFVDVFDEESKKLKNAKWLAQGTIYPDVIESAASKTGKAHVIKSHHNVGGLPDDMEMGLVEPLRELFKDEVRKIGLELGLPYNMLYRHPFPGPGLGVRVLGEIKKEYCDLLRRADAIFIEELHAADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGKVSNRIINEVDGISRVVYDISGKPPATIEWE
Catalyzes the synthesis of GMP from XMP.
A7MU26
A6NMU1
O52A4_HUMAN
Olfactory receptor 52A4
Homo
MALPITNGTLFMPFVLTFIGIPGFESVQCWIGIPFCATYVIALIGNSLLLIIIKSEPSLHEPMYIFLATLGATDISLSTSIVPKMLDIFWFHLPEIYFDACLFQMWLIHTFQGIESGVLLAMALDRCVAICYPLRRAIVFTRQLVTYIVVGVTLRPAILVIPCLLLIKCHLKLYRTKLIYHTYCERVALVKLATEDVYINKVYGILGAFIVGGLDFIFITLSYIQIFITVFHLPLKEARLKVFNTCIPHIYVFFQFYLLAFFFIFYSQIWILYPIICTYHLVQSLPTGPTIPQPLYLWVKDQTH
Odorant receptor.
A6NMU1
A5FPS8
PYRG_DEHMB
UTP--ammonia ligase
Dehalococcoides
MSKFIFVTGGVVSSVGKGITVASLGNILKSRGLSVSVQKLDPYLNVDPGTMSPYQHGEVFVTQDGAETDLDLGSYERFIDIELTADSTVTSGQVYSEVINKERRGDYLGGTIQVVPHVTQEIKARIQRLADRSKADVVIVEVGGTVGDIEGQPFLEAIRQMRNDTGRDNVLYIHVTLLPYIQSTQELKTKPTQHSVNELRRIGIQPDIIVCRADYPISEGIRDKISLFCDVERKAVIFMPTVSTIYEVPLKLESEGVGDLLVSRLHLNASPSDLSVWRGLVEKIKEPTPTVRIALVGKYVELKDAYYSVRESLCHAAIHNGRDIQIDWVHAEDIEKNGPEEYLKHVQGIIIPGGFGIRGIEGMISAVKYARENGIPYLGLCLGMQVMVIEFARYVLGSDKAHSTEFEPDSPYPVIDLLPEQRGVDSKGGTMRLGNYPCVIQPGTMAGQAYGNNLINERHRHRFEFNNDYRDTLSKAGMLFSGLSPDGKLVEICEVTGHPFMMGSQFHPEFLSRPNRPHPLFREFINAAKKVIRDGEQPSLPLSP
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
A5FPS8
B2VDG6
HSPQ_ERWT9
Heat shock protein HspQ
Erwinia
MIASKFGLGQQVRHQLYGFLGVIVDVDPEYSLADTEIDDAATSETLRGAPWYHVVMEDDDGQTVQTYLAEAQLSWEIPGEHPEQPSLDELAASIRQQLQAPRLRN
Involved in the degradation of certain denaturated proteins, including DnaA, during heat shock stress.
B2VDG6
O50291
PSBU_CROS5
PSII-U
Crocosphaera subtropica
MKTIVRLFAILMVLISSVGFVGSAVAAELNPVDAKLTTEYGQKIDLNNEDVRGFRQLRGFYPNLAAKIIKYSPYDSVEEVLDIPGLSERQRQRLEANLDKFVVTPPSSELNEGGDRINPGLY
Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
O50291
C5J049
TPM03_PERAM
Tropomyosin Per a 7
Periplaneta
MDAIKKKMQAMKLEKDNAMDRALLCEQQARDANLRAEKAEEEARSLQKKTQQIENDLDQTMEQLMQVNAKLDEKDKALQNAESEVAALNRRIQLLEEDLERSEERLATATAKLAEASQADDESERARKILESKGLADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAESGESKIVELEEELRVVGNNLKSLEVSEEKANLREEEYKQQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVHEKEKYKFICDDLDMTFTELVGY
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
C5J049
Q7VGP1
RSMH_HELHP
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Helicobacter
MKHYSVLKNEMIQALDCLKEDSILIDCTLGFGGHTIGALQAYPNIEVYAFDKDIYALNLAKERLKPYLQNIHFCHNAFSQFLDIVPNVVLPRVRGIIADIGVSSMQLDETQRGFSFVSSTLDMRMDTRADLNATKVINTYSPIRLEEIFRIYGEVRQSKKLAEIIAYERKKKPFSSCLELSTLIEQHFPRVGGIHPATLAFQALRIEVNDELGELKRLLHNIELAFDEGKIASCRVGIISFHSLEDRIIKQCFKQWSKSCICAEESLRCECGNNHAKGQILTKKPIIPTPQEIAQNKRSRSAKLRIFELKSSKDKGV
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Q7VGP1
A1S3Z6
HCP_SHEAM
Prismane protein
Shewanella
MFCIQCEQTIRTPAGNGCSYAQGMCGKLAATSDLQDLLIYMLKGVSAWAVKARELGLPPTEADTFVPKAFFATLTNVNFDDERIIEYARKAESLRNVLKTQCTEAAQKAGIRLESLPDSASVLLGTSKPELLEQAKAALPNLGKDDIHEDVMALRLLCLYGLKGAAAYMEHARVLEQQSADIAAEFHRIMAFLGTDSVDADALFTVAMDIGQLNFKVMAMLDEGETAAFGHPEPTQVNTKPVKGKAILVSGHDMKDLELILKQTQGKGINVYTHGEMLPALAYPEFKQYPHLVGNYGSAWQNQQKEFANFPGAVVMTSNCIIDPNVGQYADRIFTRSIVGWPGVVHLEGDDFSAVIEKALSLEGFLYDEISHQITIGFARNALMAAAPAVVENVKNGSIRHFFLVGGCDGDKAERSYFTDFAKATPNDSLILTLGCGKYKFNKLEFGDINGIPRLLDIGQCNDAYSAIQLAIALSEVFECDINELPLSLVLSWFEQKAIVILLTLLSLGVKNIRTGPTPPAFLTPNLLKVLEDKFGLKNTTTVEADLNAILNVA
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
A1S3Z6
A3QHQ1
PANB_SHELP
Ketopantoate hydroxymethyltransferase
Shewanella
MSKITSSTLLKFKQEGKKFTALTAYDASFAGAFDSEGIDVLLVGDSLGMVLQGHDDTLPVTVEDIVYHTRCVRRGIKRSLLIADMPFMSYATPEQAMTNATALMQAGANMVKLEGGHWLLETVTKLTERGIPVCAHLGLTPQSVHVFGGFKVQGRDADNAQRIIDEAKAIEAAGAQLLVLECIPAALAKSITEALTIPVIGIGAGADTDGQILVMHDVLGISSGYIPRFSKNYLAQTGEIRSAIRAYIEEVDTGVFPAAEHTFS
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
A3QHQ1
P45689
CSOSA_HALNC
Major carboxysome shell protein CsoS1A
null
MADVTGIALGMIETRGLVPAIEAADAMTKAAEVRLVGRQFVGGGYVTVLVRGETGAVNAAVRAGADACERVGDGLVAAHIIARVHSEVENILPKAPQA
Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell.
P45689
Q9M4C3
RR4_PLARP
30S ribosomal protein S4, chloroplastic
Plagiochasma
MSRYRGPRVKIIRRLGALPGLTNKTFKSKSGYINQSTSNKKVSQYRIRLEEKQKLRFHYGLTERQLLKYVRIARKAKGSTGQVLLQLLEMRLDNIIFRLGMAPTIPGARQLVNHQHILINNNTVDIPSYNCKPKDIITIKDRQKSQSIITKNLNFFQKQKIPNHLTFDLIQFKGLINQIVDRECIYLKINELLVVEYYSRQV
With S5 and S12 plays an important role in translational accuracy.
Q9M4C3
Q7VET8
GCSP_MYCBO
Glycine dehydrogenase (aminomethyl-transferring)
Mycobacterium tuberculosis complex
MSDHSTFADRHIGLDSQAVATMLAVIGVDSLDDLAVKAVPAGILDTLTDTGAAPGLDSLPPAASEAEALAELRALADANTVAVSMIGQGYYDTHTPPVLLRNIIENPAWYTAYTPYQPEISQGRLEALLNFQTLVTDLTGLEIANASMLDEGTAAAEAMTLMHRAARGPVKRVVVDADVFTQTAAVLATRAKPLGIEIVTADLRAGLPDGEFFGAIAQLPGASGRITDWSALVQQAHDRGALVAVGADLLALTLIAPPGEIGADVAFGTTQRFGVPMGFGGPHAGYLAVHAKHARQLPGRLVGVSVDSDGTPAYRLALQTREQHIRRDKATSNICTAQVLLAVLAAMYASYHGAGGLTAIARRVHAHAEAIAGALGDALVHDKYFDTVLARVPGRADEVLARAKANGINLWRVDADHVSVACDEATTDTHVAVVLDAFGVAAAAPAHADIATRTSEFLTHPAFTQYRTETSMMRYLRALADKDIALDRSMIPLGSCTMKLNAAAEMESITWPEFGRQHPFAPASDTAGLRQLVADLQSWLVLITGYDAVSLQPNAGSQGEYAGLLAIHEYHASRGEPHRDICLIPSSAHGTNAASAALAGMRVVVVDCHDNGDVDLDDLRAKVGEHAERLSALMITYPSTHGVYEHDIAEICAAVHDAGGQVYVDGANLNALVGLARPGKFGGDVSHLNLHKTFCIPHGGGGPGVGPVAVRAHLAPFLPGHPFAPELPKGYPVSSAPYGSASILPITWAYIRMMGAEGLRAASLTAITSANYIARRLDEYYPVLYTGENGMVAHECILDLRGITKLTGITVDDVAKRLADYGFHAPTMSFPVAGTLMVEPTESESLAEVDAFCEAMIGIRAEIDKVGAGEWPVDDNPLRGAPHTAQCLLASDWDHPYTREQAAYPLGTAFRPKVWPAVRRIDGAYGDRNLVCSCPPVEAFA
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Q7VET8
B9L1H7
PYRG_THERP
UTP--ammonia ligase
Thermomicrobium
MPKYVFVTGGVVSSVGKGITTAAIGRLLKSRGLRVALMKLDPYLNVDPGTMSPYQHGEVFVTEDGAETDLDLGHYERFTDENLSRASNVTTGQVYSAVIAKERRGDYLGGTVQVIPHITNEIKARIRQVAELHRPDVIVVEVGGTVGDIEGQPFLEAIRQMRREEGRRNVLYIHVTFLPYIASTGEVKTKPTQHSVKELRAIGIQPDVIICRTDHPVGDDVRAKVALFGDVDEDAVILLPTAETIYEVPLMLERAGLGRYVMEHLGWDDRDPDLADWERMVERLKSPRRRLRIALVGKYVELHDAYLSVVEALRHAGLAHDVAVEIVWVNSTAERSEIEAALRHVNGIVVPGGFGPRGVEGKMLAARYARERGIPYLGLCYGLHMAVIEFARNVLGLCGANSTEIDPETPHPVIDLMPDQRGVEMGGTMRLGRYPCQLVPGTKAALAYGESLVYERHRHRWEVNNAYREAFEAAGFVVSGQSPDGRYVEIMELHDHPWFVGVQFHPEFKSRPNRPHPLFVAFIGVAKHVLREGEQRPLPLAEPVAMPAADD
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
B9L1H7
A5CXR3
TRPD_VESOH
Anthranilate phosphoribosyltransferase
Candidatus Vesicomyosocius
MNIQQAIKQIVKKQDLSQNEMQKVMNDIMTGKTTDTQTSGFLVGLAIKGESIDEITAVVKIIRSFTKSVTIKNTKHLVDTCGTGGDGLGLFNISTACAFVVAAAGGSVAKHGNRGISSKSGSADVLKAAGVNLNMSVERISKCIEKIGIGFMFAPFHHHSIKYTTNVRKDLAIKTIFNIVGPLTNPAKVPNQIIGVYTQNLVEPIAHVLKKLGSKHIIVVHSKDGLDEISIADDTFVAELKNGKIKTYTINPTNFGLPLGNLDDIKVNNADDSLILIQQALDGKDSVAKNIVALNSGAAIYVCELANSLQEGVSKALKILNSGVAHQKLDDFVRESTGC
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
A5CXR3
Q9FMY1
C86B1_ARATH
Cytochrome P450 86B1
Arabidopsis
MNFNSSYNLTFNDVFFSSSSSSDPLVSRRLFLLRDVQILELLIAIFVFVAIHALRQKKYQGLPVWPFLGMLPSLAFGLRGNIYEWLSDVLCLQNGTFQFRGPWFSSLNSTITCDPRNVEHLLKNRFSVFPKGSYFRDNLRDLLGDGIFNADDETWQRQRKTASIEFHSAKFRQLTTQSLFELVHKRLLPVLETSVKSSSPIDLQDVLLRLTFDNVCMIAFGVDPGCLGPDQPVIPFAKAFEDATEAAVVRFVMPTCVWKFMRYLDIGTEKKLKESIKGVDDFADEVIRTRKKELSLEGETTKRSDLLTVFMGLRDEKGESFSDKFLRDICVNFILAGRDTSSVALSWFFWLLEKNPEVEEKIMVEMCKILRQRDDHGNAEKSDYEPVFGPEEIKKMDYLQAALSEALRLYPSVPVDHKEVQEDDVFPDGTMLKKGDKVIYAIYAMGRMEAIWGKDCLEFRPERWLRDGRFMSESAYKFTAFNGGPRLCLGKDFAYYQMKSTAAAIVYRYKVKVVNGHKVEPKLALTMYMKHGLMVNLINRSVSEIDQYYAKSFDEGYIN
Involved in very long chain fatty acids (VLCFA) omega-hydroxylation. Required for the synthesis of saturated VLCFA alpha, omega-bifunctional suberin monomers.
Q9FMY1
B0U0B6
RUVB_FRAP2
Holliday junction ATP-dependent DNA helicase RuvB
Francisella
MIETDRIISANTVQTKDENSIDRAIRPKTLAEYEGQPAVREQMEIFIQAAKSRKDALDHTLIFGPPGLGKTTLSNIIANEMEVELKQTSGPVLEKAGDLAALLTNLEENDVLFIDEIHRLSPVIEEILYPAMEDYQLDIMIGEGPAARSIKIDLPPFTLVGATTRAGLLTSPLRDRFGIIQRLEFYSVDDLAKIVYRSAKLLDLDITDDGANEIAKRSRGTPRIANRLLRRVRDYAQVKASGVISYDIADKALTMLKVDPVGFDHMDHKYLLTLMEKFGGGPVGLDTMAAALSEEKGTIEDVIEPYLIQQGYLMRTARGRIATLLAYNHFKLKIPDSLSSDQQQNLSL
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
B0U0B6
Q9A1K1
RADA_STRP1
Branch migration protein RadA
Streptococcus
MAKKKATFICQECGYQSPKYLGRCPNCSAWSSFVEEVEVKEVKNARVSLAGEKSRPVKLKDVDNISYHRTQTDMSEFNRVLGGGVVPGSLILIGGDPGIGKSTLLLQVSTQLANKGTVLYVSGEESAEQIKLRSERLGDIDNEFYLYAETNMQAIRTEIENIKPDFLIIDSIQTIMSPDITGVQGSVSQVREVTAELMQLAKTNNIATFIVGHVTKEGTLAGPRMLEHMVDTVLYFEGERHHTFRILRAVKNRFGSTNEIGIFEMQSGGLVEVLNPSQVFLEERLDGATGSAVVVTMEGSRPILAEVQSLVTPTVFGNARRTTTGLDFNRVSLIMAVLEKRCGLLLQNQDAYLKSAGGVKLDEPAIDLAVAVAIASSYKEKPTSPQEAFLGEIGLTGEIRRVTRIEQRINEAAKLGFTKVYAPKNALQGIDIPQGIEVVGVTTVGQVLNAVFS
DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Q9A1K1
Q0ZJ15
NU3C_VITVI
NADH-plastoquinone oxidoreductase subunit 3
Vitis
MFLLYEYDIFWAFLIISSVIPILAFFISGVLAPISKGPEKLSSYESGIEPMGDAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGVSVFIEALIFVLILIVGSVYAWRKGALEWS
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Q0ZJ15
Q8LFP1
PRA1H_ARATH
PRA1 family protein H
Arabidopsis
MAFSPNPLSLSVPDPAFESWLRDSGYLELLDHRTSAAAAAASSSASVSSSAAATSAASDDVVSSITGGFFASLLSRLVTVSSLLTINPFSKLSADDFSGDTTPWTTGFIGNCDSYSFPSSSQQARMRVHENIKRFARNYATLFIVFFACALYQMPLALVGLLGSLALWELFKYCSDKWKFDRHPSMRKLSIGIGQCATAVLLTFLNVQMALFSALAISYSVMILHAGFRKLTPSKKPTRGR
May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Q8LFP1
P11955
CHI1_HORVU
26 kDa endochitinase 1
Hordeum
MRAFVLFAVVAMAATMAVAEQCGSQAGGATCPNCLCCSRFGWCGSTPYCGDGCQSQCSGCGGGSTPVTPTPSGGGGVSSIVSRALFDRMLLHRNDGACQAKGFYTYDAFVAAASAFRGFGTTGGTDTRKREVAAFLAQTSHETTGGWATAPDGAFAWGYCFKQERGATSNYCTPSAQWPCAPGKSYYGRGPIQLSHNYNYGPAGRAIGVDLLRNPDLVATDPTVSFKTAMWFWMTAQAPKPSSHAVITGQWSPSGTDRAAGRVPGFGVITNIVNGGIECGHGQDSRVADRIGFYKRYCDILGVGYGNNLDCYSQRPFA
Defense against chitin-containing fungal pathogens.
P11955
P47673
RRF_MYCGE
Ribosome-releasing factor
Mycoplasma
MTKAHYIDFFKQAADKKIQWLKEELTKIRTGRPNPKIFDNLLIESYGQKMPLISLAQVTINPPREIIIKPFDPKSNTNAIYSEIQRANIGVQPVIDGEKIRVNFPQITQETRLENIKHVKKIIEQIYQELRVVRRDALQMIKKDNHNEDLENSLKAEIEKINKNYSNQLEEIQKDKEKELLTI
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
P47673
A8F909
RSMA_BACP2
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Bacillus
MNKDIATPIRTKEILKKYGFSFKKSLGQNFLIDTNILDRIVDHAEVTDETGVIEIGPGIGALTEQLAKRAKKVTAFEIDQRLLPILNDTLSPYDNVTIIHQDVLKADVGKVIEENFADCKEVMVVANLPYYVTTPIIMKLLEENLPLKGIVVMLQKEVADRMAAIPSSKEYNSLSIAVQYYTEAKTVMVVPKTVFVPQPNVDSAVIKLTVRETPAVSVENDEFFFQLIRASFGQRRKTLMNNLMNNLPDGKQHKAIIEEALQTADIDGKRRGESLSIEEFARLSNVLQKALF
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
A8F909
A1R0M4
RIMP_BORT9
Ribosome maturation factor RimP
Borrelia
MVKIIDNSEVYNLIKNVTDQLGIEIIEINTFKKRDEGRIQIVLYKGNDFGVDTLCDLHKMILLSLEVVLKYNFSLEISTPGINRKIKSDREFKIFEGRKIKLMLDNDFEEGLILKAEADGFIFKTDTKEIRILYSDVKKAKLS
Required for maturation of 30S ribosomal subunits.
A1R0M4
Q74L61
ECFA2_LACJO
Energy-coupling factor transporter ATP-binding protein EcfA2
Lactobacillus
MSIEFKNVDYVYAPGTPFQTQGLIDISFKIEKGSFVAIAGHTGSGKSTLMQHFDGLLLPSKGEITVAGEQINANTSSKALKAIRKKVGLVFQFPENQLFEETVLKDVMFGPLNFGFSEQKAKEQAVEWIKKVGLSEDMMDKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGQKQMFEIFKEYQRAGHTVILISHNMDDISEYADDMLVLDHGHLIKHASPQEIFSDQEWVKKHYLDEPATSRLTRELQKGGFQFSEMPLTIESLVSKVANELKKKGDMDE
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Q74L61
Q1WTA0
MURG_LIGS1
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
Ligilactobacillus
MRLLISGGGTGGHIYPALALIEAIKQKEPDSEILYVGTHKGLESRIVPSAGVPLKTIKIQGFKRSLSLENFKTVYLFLKSVHDCKKIIRDFKPDVVVGTGGYVCGAVVYAAARMKIPTFVHEQNSVAGVTNKFLSRFVDKVGICFEDARKDFPASKVVFTGNPRAQQVAGMKDTGRLEKEYKLRKDLPTVMIFGGSRGAEGINAAALKAIPQFAKKEYQVLFVTGKVHYDKIMAKDEAKNLPDNVRIEPYIADMPAILPEVASIVGRAGATSLAEITALGIPTILIPSPYVTNDHQTKNAMSLVNKDAALMIKEKDLTADILVKNVDKIMNDSDKRLQMGKNAKEAGIPDAANQVIKVLEDIMHK
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Q1WTA0
Q8ESU4
TRPB_OCEIH
Tryptophan synthase beta chain
Oceanobacillus
MTTYSFPNTKGKYGEFGGRFVPELLMPAVLELEKAYEDALKDESFNEELQTYLTEYIGRETPLYHAKKLTEHAGGAQIYLKREDLNHTGAHKINNTIGQALLTLRMGKKKVVAETGAGQHGVATATVCSLLGLECIVFMGEEDIKRQKLNVFRMELLGAEVVSVSQGSGTLKDAVNEALRYWVNNVNDTHYIIGSVVGPHPFPKIVRDFQSVIGKETKEQSMKKIGSLPDAVVACVGGGSNAMGMFYPFIDDKEVTLFGVEAAGAGLDTKQHAATLTGGSPGMLHGTFTYLLQDDCGQIEEAFSISAGLDYPGIGPEHSHLHQTKRVTYSSITDEEALEAFQLLSKTEGIIPALESAHAVSYATKLAKEMNPEQSIVICLSGRGDKDVEQVKERLEGEQ
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q8ESU4
Q9BA86
ATPB_PHODC
F-ATPase subunit beta
Phoenix
MRTNPTTSSPVVSTLEEKNLGRIAQIIGPVLDVVFPPGKMPNIYNALVVKSRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEKNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRVLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTSQRYKELQDIIAILGLDELSEEDRLTVARARKMERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEVESKLKK
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Q9BA86
Q3J6V9
ARGB_NITOC
NAG kinase
Nitrosococcus
MTLTVDHAMNIAQVLTESLPYIQRFAGKTVVIKYGGNAMVDDDLKNSFSRDVVLMKLVGINPVVIHGGGPQIGRLLERVGKQSEFIQGMRVTDKETMDIVEMVLSGQVNKEIVNLINRHGGHAVGLTGKDGTLIHAEKLHLTQDRDDPTINIPEIIDMGHVGKVKQINTRIVDLLVQSDFIPVIAPIGVGENGQSYNINADLVAGKLAEALGAEKLILLTNTPGLLDKEGKLLTGLNAEQVQSLIADGTISDGMLPKIQCALEAVHAGVRSAHILDGRVEHAVILELFTDEGIGTLIRNRH
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Q3J6V9
Q88L02
FADB_PSEPK
3-hydroxyacyl-CoA dehydrogenase
Pseudomonas
MIYEGKAITVKALESGIVELKFDLKGESVNKFNRLTLNELRQAVDAIRADASVKGVIVRSGKDVFIVGADITEFVDNFKLPEAELVAGNLEANRIFNAFEDLEVPTVAAINGIALGGGLEMCLAADYRVMSTSARIGLPEVKLGIYPGFGGTVRLPRLIGSDNAIEWIAAGKENRAEDALKVGAVDAVVAPELLLAGALDLIKRAISGELDYKAKRQPKLEKLKLNAIEQMMAFETAKGFVAGQAGPNYPAPVEAIKSIQKAANFGRDKALEVEAAGFAKLAKTSVAESLIGLFLNDQELKRKAKAHDEIAHDVKQAAVLGAGIMGGGIAYQSAVKGTPILMKDIREEAIQLGLNEASKLLGNRVEKGRLTPAKMAEALNAIRPTLSYGDFANVDIVVEAVVENPKVKQAVLAEVEGQVKDDAILASNTSTISINLLAKALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSDVAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFAKLVSAGVDFVRIDKVMEKFGWPMGPAYLMDVVGIDTGHHGRDVMAEGFPDRMKDERRSAVDALYEANRLGQKNGKGFYAYETDKRGKPKKVFDATVLDVLKPIVFEQREVTDEDIINWMMVPLCLETVRCLEDGIVETAAEADMGLVYGIGFPPFRGGALRYIDSIGVAEFVALADQYADLGPLYHPTAKLREMAKNGQRFFN
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
Q88L02
Q7VE08
YBEY_PROMA
Endoribonuclease YbeY
Prochlorococcus
MQNLNDSSISVDLTIDLSLSGFTFDLMKDSIDSKMIDLIMDCDTWRNSIVSWFDCILMQPNLTCPQIVRKNRFFSMGLLFTNDLSIRQMNKEWRKKDESTDVLSFPAIDEHIVLPPNQFLELGDIIVSVETAFKQAKIHNHSLMHELRWLVSHGFLHLLGWDHPSSASLNEMLSFQELLLKTPNGSPLRNSMRDY
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Q7VE08
B4N278
TRMB_DROWI
tRNA(m7G46)-methyltransferase
Sophophora
MVTTSQEQGHDALTATSAVTGLPQKRFYRQRAHSNPIADHSFDYPARPEDVDWSALYPNIQPDQQVEFADIGCGYGGFLVTLGEMFPQKLSIGMEIRVKVSDYVVDRIAALRLKSGKLNGDAYKNIACIRTNAMKYLPNYFRKGQLEKMFFLYPDPHFKRAKHKWRIINQALLSEYAYVLRQGGLVYTMTDVEDLHQWIVSHMNQHPLYERISPEDESQDPITPKLYQSSEEGAKVVRNKGDHFLAIFRRI
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
B4N278
B5FA98
DEOC_ALIFM
Phosphodeoxyriboaldolase
Aliivibrio
MSDLKAAALRALKLMDLTTLNDNDTDEAVIALCKNAKTAVGNTAAVCIYPRFIPIAKKTLREQGTPEVRIATVTNFPHGNDDIEIAVAETKAAVAYGADEVDVVFPYRALIAGDETTGFELVKQCKEACGDVLLKVIIETGELKEEALIKKASQICIEAGANFIKTSTGKVPVNATPEYARMMLEVIRDMDVAKTVGFKPAGGVRTAEDAQAYLAMADEILGDDWADNMHYRFGASSLLTNLLNTLEVTEETADPSAY
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
B5FA98
B8GDE3
COBQ_METPE
Probable cobyric acid synthase
Methanosphaerula
MSLMILGTSSHVGKSVTVAAICRIMIRQGISVAPFKSQNMSLNSYVTRDGAEIGIAQAMQAFAARVLPSALMNPVLLKPKGDSTSQVVLLGHPYKDVQIRDYYQETDHLLEIAVDAYHQLVEEYGAVIVEGAGGAAEVNLYDRDIANIRLAEHLRLPIVLVADIERGGVFAQVYGTIALLPEQIRPLVKGIIINKFRGDPTLFESGVKTLEDLTGVPVLGVIPYTRLDLPSEDSLSLQDKERQTGLVRIAVIRLPQIANFTDFELLERHAAVDYLLPGESLDGYDCIIIPGTKNTVNDLLALQASGTAAAIRDARGQGVPVIGICGGYQMLGKTVIDDGSEARKGTYEGLGLLDLVTTFEGYDKTTVQVQRTAAPVPPILDAMGTVSGYEIHMGTTVLKSGRTAFAGEGAVSDDGLVFGTYLHGLFMVPAAAEALLSYLYSQRGLTFTGIEEQNEDPYDLLADHFEAHLQMERLLTLCSDHTPETPV
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
B8GDE3
B1IFW6
UVRC_CLOBK
Excinuclease ABC subunit C
Clostridium
MFDLEYQLKNLPDKPGVYLMKNNLGEIIYVGKAKILKNRVRQYFQKSQKHSEKVKAMVKNIEEFEYIITDSEIEALILECNLIKKYRPKYNILLKDDKHYPFIKVTLAEDFPRVVSTRKVTKDGSKYFGPYVDGSSVKDIIELIKKTFPIRTCKKNIVEGAKAIRPCLNYQIGLCKAPCAQYIKKSEYREIIDDVIKLLSGKHLDIVENFKLNMEKAAENLEFEKAAMLRDKINIIEKIGEKQKIILNNFDNEDYISLYSDGKDTCFQVFFLRNGKIVGREHFIIEDTFDTNSSTLISNFLKEFYGGTAYIPKTIYVPSIEDEALLEQWLTLKKESKSTIKIPIKGEKKNILVLVEKNAKTTLENFKLKYLQEKALYDNVLKDLKNILRLQEEPIRIEAFDISNIQGFDSVGSMVVFEKGRAKPSDYRRFKINTVKGADDYKSMKEILTRRFQHGLSEIKSIQDRKLEFSSGKFSVFPDLILMDGGKGQINIALEVLNTFNIDIPVCGMVKDNKHRTRGLIYNGEEIIINKYGSVMKFITRVQDEVHRFAISYHRSLRGKNSFHSLLDDIPNIGEKRKKDLLFNFKSIDNIKKATYEELLSIPSMDKKSAECVLEFFK
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
B1IFW6
C0ZUT0
MSHA_RHOE4
N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase
Rhodococcus erythropolis group
MHISRPRRVAVLSVHTSPLAQPGTGDAGGMNVYVLQSAIQLAKRGVEVEIFTRATSSADAPVVDAAPGVRVRNIAAGPFEGLDKADLPTQLCAFVAGVLREEARHEPGYYSLIHSHYWLSGQVGWLARDRWGVPLVHTAHTLAAVKNLSLAEGDTPEPAARQIGEQQVVAESDRLVANTTDEAKALHELYGADPTRIDVVAPGADLTRYRPGDRDSARASLGLDPGEIVVTFVGRIQPLKAPDVLLRAAAEVISRSPGLPLRILVVGGPSGTGLARPDVLIELARSLGITAQVTFLPPQAPERLADVYRASDLVAVPSYSESFGLVAIEAQACGTPVIAADVGGLGVAVRNGETGLLVQGHRTEDWAGALESLVTAPTRLAELAAQAPRHAENFSWEHTADGLLESYRKAAVNYNNGTGPSDFSPRRARGLWRLRRTGGVRT
Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
C0ZUT0
A0A1L9WQM9
ACRA_ASPA1
Acurin A biosynthesis cluster protein A
Aspergillus subgen. Circumdati
TGTPEPIAIVGMGCRFPGGANTPSKLWDLLCAKRDVQRRIPTDRFHVDAFYDRDGERAGCLNVREAYTLDEDIRQFDAAFFKTNALEAEAMDPQQRLLLETVYEALESAGGVMEDLHGSDTAVYVGVMTGDYHELLLRDPEDMPKYMATGTARSILSNRISYFFDWTGPSMTIDTACSSSLVAVHEAVQALRQGRSTLACAAGANLILGPEMMISESKLHMLSPTGRSRMWDAGADGYARGEGFAAVMLKTLSQAVADGDYVYGVIRETGVNSDGRTNGITLPGADSQTALIRQTYARAGLDIDSQRCQYFEAHGTGTAAGDPIEARAIYNAFFASSSEQAETPLYVGSVKTAVGHLEGTAGLAGLVKAVEAVRRGVIPPNMLFESLNPEIQPFYHRLAVPTDTIPWPEVREGEPRRASVNSFGFGGTNAHAIIESYDNPHRRPSSATSSLYTPLVLSANSESSLRGQVEALHAFLSTTDTPVQHILHTLQTRRSQHPVRATFSAPDRDTLSTALSKAVASDSTLGTRVDKRPAKPRILAVFTGQGAQWPTMGREILRASPLAQRTLSTLQSALDTLPDGPDWLLSTEILADKDTSRLASASVAQPLCTAVQILVVDLLRLAGITPSVVVGHSSGEIAAAYAAGMISAAEAIRIAYYRGVHASLARGQNGQRGGMMAVGMSYDEATEFCEENFAERIEVAASNAPSSVTLSGDEDAIAEAKAILDERGVFARPLRVDTAYHSAHMIPCSEPYLDSLAACEIAPQEAREGCVWVSSVHGARMEGYRVDTLTGEYWNDNMVSPVMFSTAVEMALSEEAACDVAIEIGAHPALKGPFTQTAKQVAAAASSATPLPYSGTLSRGQHDIEALSETLGYLWLHLGAKAVAFPAYTSAFTDALPQWVPDLPRYSWDHRQSFWRESTKSANFRSRLPRHPLLGVRSTEDLDQEMRWAITLRTQELPWLEGHKVEGQVIYPAAAYLVMAMEAAHNLVGEGLSVQMLELFDVEIANAIPLPEDGKGVEVQFTLVPSPGNAKSETKTAQWACYARTAGTGKSSWRSNARGTVRVVLGPAADEDLPPRNPPTGVFHEVKTERFYEALTAIGLHYTGPFRGLDSVHRRSGTAMATATQIPAAELGVPIHPAVLDAAFQTLFAAYCWPEDGSLRAPFVPTGLQSLRIVNRDLVQASAQLTVDAAITHSSGTTIIADLDLYSPAAAGLIQLQGLRCSSLTPPGPRDYKELYTQTAWEVDLSSGLAALSSVSDSDSPSNLALVDLSERLAYYYLRHLNTTIPRSAVPQMEWHHQRIFEWIDHLFPLVTSGKHPTIRPEWSTDTKPHLLALASQYPDSVDLQLIRAVGEHLPAVVRGEAWMLEHMVANDTLDRFYKFGLGFARANGYMGRVAGQIAHRYPRSRILEIGAGTGGATKGILEALDGRFERYTFTDISTGFFEAAATQFERWAGKMSYRALDVEKELSSQGWDGEEAGFDVIVASNVLHATKSLRKTMENVRRLLKPGGFLLLLEVTSEIVRVKLMMAGLPGWWLGGEDGRRYGPTITVEQWDTLLKETGFAGVDHVVNDFVDESKYMTSVMVTQAVDADVRLLREPLSAGWTLPPVTVVGGQKGLAGRVVEALGSAGSVQLVENLEGLFVQPDISVTSLVILEDFDHPVLEDFTPCKLEALQRALPECRQLLWVSGQCREKNPYGNMAIGLCRAIAAEQPHIQFQHLDIEDAVDAGAAKAVTEALVRLVFASQTRLATKNVLWTCEPELVRENGQWLVPRIVPDKRLNDQLNARKMVVQGMATSEEKLELVKQAERYVLSPALPSVVEKDGAVEVKVTHALVNAVQLDQGSVCVVSGNLLSKPDVQVIACTNSVRSVVTVSEEMVFPAENASPPLLQTVAFGLVADEWLHGLSSSDVLVLHQADEQLGRVLRSKAAEAGVKVVDVRTHAYASERSIRAQIPPSTKLLVDFAQSSVQWERILPAQCKIRSYGDAIAPGTSIADTANLNTSQLQRAISWAQQQQPADTALETIPAAELATTPTPSYHAILSFSPSTTIPTITRPVNPALLFRPDRTYLLVGCTGGLGQSLCRWMVLNGARHLALTTRNRTRISTTWLADLAQLGANVQLFEADVADMASLTAIHQTITTGMPPIAGIANAAMVLSDRSFGELKHTDFTTVFGPKVLGTKNLDTLFHSQKLDFFIMFSSLASIVGNRGQSNYVAANLFMSTVAAQRRARGLAASVFHIGMVLGVGYVSTTGVYETTLRQYKYMPIAEPEFWDMFAQAIVIGHPTLAGGHAPEMITGLHRHSLREEVAKAFWAENPRFSLHTLVEESQTVVVDAASAKQVPLAEAVAEAETLEEVDGVIQEAFVVKMERMLQAAKGSIERGQPLINLGVDSLIAVEIRSWFLKELEVDMPVLKLVGGMSVGELCREAASEVL
Highly reducing polyketide synthase; part of the cluster that mediates the biosynthesis of acurin A, a highly reduced polyketide coupled to a serine via a peptide bond . The activities of the highly reducing polyketide synthase acrA and the nonribosomal peptide synthetase acrB are collectively responsible for the synthesis of the acurin A core structure with a heptaketide backbone produced by acrA covalently fused to a L-serine by acrB . After the formation of the PK-NRP hybrid product, it is detached from acrB by reductive release to set up the formation of the lactam ring by aldol condensation (Probable). The hydrolyase acrC then catalyzes water loss to generate a double bond in the ring (Probable). This double bond is probably reduced, which is followed by three oxidations at C-22 to generate the carboxylic acid moiety, involving probably the FAD-binding monooxygenase acrE and the cytochrome P450 monooxygenases acrD and acrF (Probable). Finally, a last methylation step performed by the O-methyltransferase acrG leads to the production of acurin A (Probable).
A0A1L9WQM9
Q93G07
CH60_LACAC
Chaperonin-60
Lactobacillus
MAKDIKFAENARRSLLKGVDKLADTVKTTIGPKGRNVVLEQSYGNPDITNDGVTIAKSIELKDHYENMGAKLVAEAAQKTNDIAGDGTTTATVLTQAIAREGMKNVTAGANPVGIRRGIEKATKAAVDELHKISHKVESKEQIANVAAVSSASKEVGELIADAMEKVGHDGVITIEDSRGINTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQEIVQQGKSLLIIADDVTGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLEDIAALTGGTVITDDLGFELKDTKIDQLGQARRVTVTKDSTTIVDGAGSKDAIKEREDSIRKQIEESTSDFDKKKLQERLAKLTGGVAVIHVGAATETELKERRYRIEDALNSTRAAVDEGYVAGGGTALVDVEKAIKDLKGETSDEQTGINIVLRALSAPVRQIAENAGKDGAVVLNKLESQENEIGYNAATDKWENMVEAGIIDPTKVTRTALQNAASIAALLLTTEAVVADIPEDKPEAPQAGAAGAPGMGM
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Q93G07
B8GRC1
ATPD_THISH
F-type ATPase subunit delta
Thioalkalivibrio
MSELTTLARPYAKAVFEVAQGAGDLARWSDQLGFMAAVVHDPTMKAFLDSPKLTREAAADTVIGVCEGRIDDQGKNFVRLLAENGRLTLLPEIAAIYEVMRAEAEGKVEALVVSAQPVSDAQKSAIAQSLAKRLGREVELVCEVDESLIGGAVIRAGDLVIDGSVRGRLERMAANLSR
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
B8GRC1
Q43931
CATB_ACIAD
Muconate cycloisomerase I
Acinetobacter
MYKSVETILVDIPTIRPHKLSVTTMQTQTLVLIKIITEDGIVGWGEATTIGGLNYGEESPESVKANIDTYFKPLLLSIKAPLNVAQTLKLIRKSINGNRFAKCAIQTALLEIQAKRLNVPVSELLGGRIRDRLPVLWTLASGDTDKDIAEAKKMIELKRHNTFKLKIGSNPLQHDVDHVIAIKKALGPEISVRVDVNRAWSELECVKGIQQLQDGGIDLIEQPCAIENTDALARLTARFDVAIMADEVLTGPDSAYRIAKKSGADVFAVKVEQSGGLIEACEVAKIARLAGISLYGGTMLEGPVGSIASAHAFSTFETLEFGTELFGPLLLTQSILKTPLQYENFELVVPNTPGLGIEVDEDKLEQLRRH
Catalyzes a syn cycloisomerization.
Q43931
P50649
RIR2_PLAFG
Ribonucleotide reductase small subunit
Plasmodium (Laverania)
MRRILNKESDRFTLYPILYPDVFPFYKKAEACFWTAEEIDYSSDLKDFEKLNENEKHFIKHVLAFFAASDGIVLENLAVSFLREVQITEAKKFYSFQIAVENIHSETYSLLIDNYIKDEKERLNLFHAIENIPAVKNKALWAAKWINDTNSFAERIVANACVEGILFSGSFCAIFWFKKQNKLHGLTFSNELISRDEGLHTDFNCLIYSLLDNKLPEQMVQNIVKEAGGVEVEKSFICESLPCDLIGMNSRLMSQYIEFVADRLLECLGCSKIFHSKNPFNWMDLISLQGKTNFFEKRVADYQKSGVMAQRKDHVFCLNTEF
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
P50649
Q7VHV4
SYA_HELHP
Alanyl-tRNA synthetase
Helicobacter
MAQYDIRKQYLDFFASKSHKVYDSMPLVPDDASLLFTNAGMVQFKDIFTGKIPIPAPPRATSSQLCIRAGGKHNDLENVGYTARHHTLFEMLGNFSFGDYFKKEAIAYAWEFVTQVLGFSKDVLYVTIHESDDEAYELWCEHIEPSRIKRMGDKDNFWQMGDSGPCGPCSEIYVDQGEKYFQSDEDYFGGEGDRFLEIWNLVFMQFEQKGGVRTLLPKPSIDTGMGLERVIALKEGKINNFDTSLFAPLMQCLQKLTNKTYFGDDEIFDRLDLQEAEMIKIKNIQASFRVIADHARSVAFLLAQGVNFDKEGRGYVLRRILRRAVRHGYLLGLKKPFLWQVVEVVCESMGVHYSYLQERKRAIKEQCKNEEERFFETIESGMTLFSTELEKLQSAVQTQKQEILFSGEVAFKLYDTYGFPLDLTQDMLRERHIQVDMQAFEQCMNEQKSRSKASWKGSGDALKEGDFNALLSKFGENKFVGYESNKETCKIKALLDSQFKMVDTLSPSSQGWVMLDKTPFYPESGGPVGDKGALYSTNRILQSAQAQKFAQVLDTQKFFGLNLSQIEALSALKVGQEVFAEVDSIRFEIAKHHSATHLLHLALRTILGSHIAQAGSLVQPHRLRFDFSHPKALTNEEITHIENLVNEQILQSNAQLCENMDMQQAKAKGAMALFGEKYGERVRVVSFGDSIELCGGIHVNNTAEIGSFYIVKESGVSSGVRRIEAVCGNAAYHYGKNALLELSRARESLKAQDVLQGIEKIKMQLNEAKEKANKAKQSVKSLDYEEINGVRLIVLKLDSVSANEAKEIIDRSKNENESVAILLLSESNNKISIVAGVKNAPLKAGAWVKQVAQELGGNGGGRDDFATAGGKDIDKISQALNLAKDIATKALQ
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Q7VHV4
Q9NX74
DUS2L_HUMAN
tRNA-dihydrouridine synthase 2-like
Homo
MILNSLSLCYHNKLILAPMVRVGTLPMRLLALDYGADIVYCEELIDLKMIQCKRVVNEVLSTVDFVAPDDRVVFRTCEREQNRVVFQMGTSDAERALAVARLVENDVAGIDVNMGCPKQYSTKGGMGAALLSDPDKIEKILSTLVKGTRRPVTCKIRILPSLEDTLSLVKRIERTGIAAIAVHGRKREERPQHPVSCEVIKAIADTLSIPVIANGGSHDHIQQYSDIEDFRQATAASSVMVARAAMWNPSIFLKEGLRPLEEVMQKYIRYAVQYDNHYTNTKYCLCQMLREQLESPQGRLLHAAQSSREICEAFGLGAFYEETTQELDAQQARLSAKTSEQTGEPAEDTSGVIKMAVKFDRRAYPAQITPKMCLLEWCRREKLAQPVYETVQRPLDRLFSSIVTVAEQKYQSTLWDKSKKLAEQAAAIVCLRSQGLPEGRLGEESPSLHKRKREAPDQDPGGPRAQELAQPGDLCKKPFVALGSGEESPLEGW
Dihydrouridine synthase. Catalyzes the NADPH-dependent synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs . Negatively regulates the activation of EIF2AK2/PKR .
Q9NX74
O28002
RPO3_ARCFU
DNA-directed RNA polymerase subunit D
Archaeoglobus
MMPEIEILEEKDFKIKFILKNASPALANSFRRAMKAEVPAMAVDYVDIYLNSSYFYDEVIAHRLAMLPIKTYLDRFNMQSECSCGGEGCPNCQISFRLNVEGPKVVYSGDFISDDPDVVFAIDNIPVLELFEGQQLMLEAVARLGTGREHAKFQPVSVCVYKIIPEIVVNENCNGCGDCIEACPRNVFEKDGDKVRVKNVMACSMCGECVEVCEMNAISVNETNNFLFTVEGTGALPVREVMKKALEILRSKAEEMNKIIEEIQ
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
O28002
B8ZU80
PURA_MYCLB
IMP--aspartate ligase
Mycobacterium
MPAVVLIGAQWGDEGKGKVTDLLGGRAQWVVRYQGGNNAGHTVVLPTGENFTLHLIPSGVLTPGVTNVIGNGVVVDPGVLLSELQGLEDRGVDTSQLLISADAHLLMPYHVAIDKVTERYMGNKKIGTTGRGIGPCYQDKIARMGIRVADVLEPGELTHKIEAALEFKNQVLVKIYNRKALDLAQVVETLLEQAQQFRHRITDTRLLLNDALEAGETVLLEGAQGTLLDVDHGTYPYVTSSNPTAGGAALGSGIGPTRIHTVLGILKAYTTRVGSGPFPTELFDENGEYLAKTGSEIGVTTGRRRRCGWFDAVIARYATRVNGITDYFLTKLDVLSSLETVPVCVGYQIAGVRTHDMPITQSDLARAEPIYEELPGWWEDISGAREFEDLPAKARDYVLRLEELAGAQVACIGVGPGRDQTIVRCDVLRSRR
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
B8ZU80
Q9KPA1
YGFZ_VIBCH
tRNA-modifying protein YgfZ
Vibrio
MDWQNRFSVLNLSSHDPLPELMLTHLTGWGAITLVGADKKAYLQGQVTCNVVSLQEQQVTFGAHCDAKGKVWSVFRLFHHHDGYAMFQPQSAMEVELRELKKYAIFSKVTIAESSDIALGVMGSQADAWIDTVSETTGDVRRIAGGTAVRMSPQRWLLLVNAEQAEQYVNAWQGLHVEQSLWTRMDIEEAVPVVTQTAQNEHIPQALNVQAVDGISFTKGCYTGQETVARAKYRGINKRAMYIVKGNLSAPLSQDEPVVLERAVGENWRSAGALLTHYRFTDSIAIGLIVLPNDLEHDVKLRLAAQPDTRWHIQPLPYSLSDE
Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication.
Q9KPA1
A8JGF7
LIAS_CHLRE
Lipoic acid synthase
Chlamydomonas
MKRNKLPGGDKYTEIKAKLRELKLSTVCEEARCPNLGECWGGGDGHTATATIMLMGDTCTRGCKFCAVKTSKAPPPLDPHEPENVSKAIAAWGLDYVVLTSVDRDDLPDGGAAHIASTIRLLKQKTEGRLLVEALVPDFQGDMGGVQTIVEAGLDVYAHNIETVERLQGQVRDRRAGWAQSLATLSAAKRVSGGRLLTKSSIMLGCGESREEVVDTLKALRANGVDVVTLGQYMRPTKKHMAVAEFVTPEAFAAYEQIAKDLGFLYVASGPMVRSSYRAGELYITNVLKGRRGGEGEGGEGQQQQQGQQQQQARAATA
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
A8JGF7
C4LC44
UNG_TOLAT
Uracil-DNA glycosylase
Tolumonas
MQTWSDVLGQEKKQAYFQETMDFVRREREAGKIVYPPAADVFNAFKYTEFADVKVVILGQDPYHGPNQAHGLCFSVLPGVAVPPSLVNIYKELHRDIPGFEIPSHGYLLSWAQQGVLLLNTVLTVEAGKAHSHASSGWEHFTDRVIAALNEHREGLVFLLWGNHAQKKGQYIDRQRHHVLMAPHPSPLSAHRGFLGCGHFSQTNQFLTDADKQPINWQIAPIA
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
C4LC44
Q0ATU5
MNME_SYNWW
tRNA modification GTPase MnmE
Syntrophomonas
MIGDDIAAISTAPGEGGIAIVRLSGNDVIEKVERIFKPYRAGIKLSDKEGYSLSLGWLCDEKMEIIDEVLLGLMRAPRSYTGEDVVEINCHGGTLPARRCLEAVMWQGVRLAQPGEFTRRAFLNGRLDVSQAEAVIEVIRAKTERGMNLALKQLAGRNSQEINLLEDQMIEVNAMLEASLDFPDEVGDLDYSAAQGKLQEVKNRIDKLLLAGERAEIYREGINVAICGKPNVGKSSLLNALLRKEKAIVTSIPGTTRDIIEDYINIRGIPVKLKDTAGIRSTEDLVERIGIERSQEVISEADLVLFILDVGTGIDQEDRKIYEKIEKKNKIVLVNKEDLEEKNISEAELEQLFPGVKIVRGSIIEETGLEELEESIEKAVLSGQLQSDDMEVMINLRQKNALLTAKRHIEESLAAMGKVSLDCLGVDIWGALEALGEISGKNLKEEVIERIFHDFCIGK
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Q0ATU5
P22551
SLSG0_BRAOA
S-locus-specific glycoprotein
Brassica
MRGVIPNYHHSYTLFFFVILVLFPHVFSTNTLSPNEALTISSNKTLVSPGDVFELGFFKTTTRNSPDGTDRWYLGIWYKTTSGHRTYVWVANRDNALHNSMGTLKISHASLVLLDHSNTPVWSTNFTGVAHLPVTAELLANGNFVLRDSKTNDLDRFMWQSFDYPVDTLLPEMKLGRNLIGSENEKILTSWKSPTDPSSGDFSFILETEGFLHEFYLLKNEFKVYRTGPWNGVRFNGIPKMQNWSYIDNSFIDNNEEVAYSFQVNNNHNIHTRFRMSSTGYLQVITWTKTVPQRNMFWSFPEDTCDLYKVCGPYAYCDMHTSPTCNCIKGFVPKNAGRWDLRDMSGGCVRSSKLSCGEGDGFLRMSQMKLPETSEAVVDKRIGLKECREKCVRDCNCTGYANMDIMNGGSGCVMWTGELDDMRKYNAGGQDLYVKVAAASLVPS
Involved in sporophytic self-incompatibility system (the inability of flowering plants to achieve self-fertilization).
P22551
Q6F1W7
RPOA_MESFL
Transcriptase subunit alpha
Mesoplasma
MKQFNKPEFGIVKESPNKFYGKFEAAPLERGFAVTLGNALRRTLLSSTPGASVFAIKIAGAQHEFTSISGIEENVTRIVLNVKKLILRIDSAIYNDDETVELKVGTSTIGPVTAGSLVLPAGVEVLNKDLVIANVAEGGNLDLVLYAKNSRGYKTFKENKELKDVVPGMITIDSNYSPIIKVAYGSTPINLGKAQDFEKLILEVETDGSILASDAVSLASKILISHFDVFTTLAEEVEEVAIMGVETVEEKELDKPVEELEFTQRSLNCLKRAGISTLRELVSKTEDEIQDIRNLGRKSLKEIKDKVAALELTFKQN
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q6F1W7
O74366
TFB4_SCHPO
RNA polymerase II transcription factor B subunit 4
Schizosaccharomyces
MDEFQTLKQNASWDISEDANDTPSLLVVILDANPASWYSLSKKVPVSKVLADITVFLNAHLAFHHDNRVAVLASHSDKVEYLYPSIAPEQKVAEVDPTKEANTYRKFREVDDLVLSGMKRLMSSTDKVSRKTMISGALSRALAYINQVQNKNTLRSRILIFSLTGDVALQYIPTMNCIFCAQKKNIPINVCNIEGGTLFLEQAADATGGIYLKVDNPKGLLQYLMMSLFPDQNLRKHLNTPNQANVDFRATCFCHKKVLDIGFVCSVCLSIFCEPRVHCSTCHTKFTVEPMSKKLHT
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
O74366
B7J5S3
LEUD_ACIF2
Isopropylmalate isomerase
Acidithiobacillus
MEAFTVVEAVVAPLDRPNVDTDAIIPKQFLKTIERKGLGKHLFDAWRYLERDGKQVNNPDFVLNQPAYAGAQILLARENFGCGSSREHAPWALADYGFRAVIAPSFADIFANNCVQNGILLVRLPMDVVDHLFHEVAANPGYRLRIDLPAQEVQTMGDSRYAFPMDAGHKHKLMHGLDDIQLTLQRDNAIRVYEARRRQTAPWLFRD
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
B7J5S3
Q21YC4
NUOD_ALBFT
NDH-1 subunit D
Rhodoferax
MAEIKNYTLNFGPQHPAAHGVLRLVLELDGEVIQRADPHIGLLHRATEKLAETKTYIQALPYMDRLDYMSMMCNESAYCLAVEKMLGLEVPIRAKYIRVMFAEITRLLNHLLCVGAGALDCGAMTVMLYAFREREDLLDMYEAVSGARMHAAYFRPGGVYRDLPDTMARHQPNKIRSAKSTEKLNRNRDGSLLDFIDDFTQRFPTYLGEYHTLLTDNRIWKQRTVGIGVVTAERALNLGFSGPMLRGSGVAWDLRKKQPYEIYDRLDFDIPVGKTGDCYDRYLVRMEEMKQSNRIIKQCVDWLRVNPGPVITDNHKIAPPNRESMKSNMEELIHHFKLFSEGFSVPEGEAYATIEHPKGEFGIYMVSDGANKPYRMKIRPPAFVHLAALGEMGRGHMIGDAVAIIGSLDIVFGEVDR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Q21YC4
Q00237
CHLL_LEPBY
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Leptolyngbya
MKLAVYGKGGIGKSTTSCNISVALAKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQEKDYHYEDVWAEDVIYKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFDEYDVILFDVLGDVVCGGFAAPLNYADYCMIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTAKRDLIEKYVDAVPMPILEVLPLIEDIRVSRVKGKTLFEMAESDPSLNYVCDYYLNIADQILANPEGVVPKDAADRDLFSLLSDFYLNPQQPKTAEEELDLMMV
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
Q00237
Q6G001
PLSX_BARQU
Phosphate-acyl-ACP acyltransferase
Bartonella
MIRISVDVMGGDYGPEATIAGAAIVQKHLPNVYFLFYGVDEAVKPVLKKYPCLASLSRFCSTESYTRMDEKPSQALRNGRGRSSMWYAIEAVKNGEADACISAGNTGALMAMSYFCLKMMAEAERPGIAGIWPTLRSESVVLDIGATIGASASQLVDLAVMGAGMFRTLYHTEKPSVGLLNVGVEEVKGLYAIKKAGMILREVQLEGLEYKGFVEGNDIGKGIVDVVVTEGFSGNIALKTAEGTARQIGEILNAAMRSSFFSSLGYFLSRGAFRTLRHKMDPDRVNGGVLLGLNGVVIKSHGSANASGFASAIRVAYEMVSNGLLKKITADLRRFHENKEKLFDKESEPTINNGETI
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Q6G001
A6VB75
SECA_PSEA7
Protein translocase subunit SecA
Pseudomonas
MFAPLLKKLFGSKNERDVKRMAKAVQAINALEPQMVALSDEQLKAKTAEFQQRYAKGETLDQLLPEAFAVVREAGKRVMGMRHFDVQLIGGMTLHDGKIAEMRTGEGKTLVGTLPVYLNALSGKGVHVVTVNDYLARRDANWMRPLYEFLGLSVGVVTPFQPPEDKRAAYAADITYGTNNEFGFDYLRDNMAFSLDDKFQRELNFAVVDEVDSILIDEARTPLIISGQAEDSSELYIKINKLIPRLKRQVEEVEGKPSEEGHYSIDEKTRQVELNEQGHQFIEDLLSQNGLLGEGESLYSAHNLSLLTHVYAALRAHTLFHRNVEYIVQGDQILLIDEHTGRTMPGRRLSEGLHQAIEAKEGLPIQAESQTLASTTFQNYFRLYNKLAGMTGTADTEAFEFRQIYGLDVVVIPTHRPIARKDFNDLVYLTQEEKYAAIITDIKQCQALGRPILVGTASIESSEYVSKLLQQAGIEHKVLNAKYHEKEAEIIAQAGAPGSVTIATNMAGRGTDILLGGNWEVEVAALENPTEEQIAQIKAEWQKRHQQVIEAGGLHVIASERHESRRIDNQLRGRAGRQGDPGSSRFYLSLEDNLMRIFASDRVKNFMKALGMQSGEAIEHRMVTNAIEKAQRKVEGRNFDIRKQLLEFDDVANEQRKVIYHMRNTLLSAEDVGETIKEFREETLNATINQHIPPQSLPEQWDVEGLEAALYSDFAVRLPIQQWLDEDDKLYEETLRSKILEQIVAAYYEKEELAGAEALRAFEKQMLLRVLDDLWKDHLSTMDHLRHGIHLRGYAQKNPKQEYKRESFTLFQELLDSIKRDTIRVLSHVQVRREDPAEEEARLRREAEELAKRMQFQHAEAPSMEQAVAGEDEELPEGPAPVVPLEPVRNEQKIGRNEPCPCGSGKKYKHCHGQLD
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
A6VB75
C1C862
PDXT_STRP7
Pyridoxal 5'-phosphate synthase glutaminase subunit
Streptococcus
MKIGILALQGAFAEHAKVLDQLGVESVELRNLDDFQQDQSDLSGLILPGGESTTMGKLLRDQNMLLPIREAILSGLPVFGTCAGLILLAKEITSQKESHLGTMDMVVERNAYGRQLGSFYTEAECKGVGKIPMTFIRGPIISSVGEGVEILATVNNQIVAAQEKNMLVSSFHPELTDDVRLHQYFINMCKEKS
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
C1C862
A6UR49
COFH_METVS
FO synthase subunit 2
Methanococcus
MDLISFKEKDISKKECLELFLDTENFFDILKVADDIRKESVGDTVTYVLNANINFTNVCSGTCKFCAFKTEKEDPNSFFLNPDKVAEKALLARKTGATEVCIQGGLLPEIDTYFQAEILQKVKKITEKYGGIDIHAFSPMEVKSAAENCGLNVKEALKILKDSGLKTMPGTAAEILNDEIRNEICPTKLTTSEWIDVVKTAHKNGIKTTCTMMYGHIEENVHLVEHLSILKEIQKETSGFTEFVPLTFLHENAPLHHIGKVKSGASGILDLKVYAISRIFFKNYLKNIQTSWVKLGIKLSQISLNCGANDVGGTLMEESISKAAGGSFGTCMSEEKLKNMILNVNKIPKKRNTLYELIN
Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
A6UR49
Q0ADD6
MNMG_NITEC
Glucose-inhibited division protein A
Nitrosomonas
MHFSRDFDIIVVGGGHAGTEAALAAARMGQKTLLLTQNLDTLGQMSCNPSIGGIGKGHLVKEIDALGGAMAAAIDEAGIQFRTLNSSKGPAVRATRAQADRVLYRQAIRKRLEAQPNLLILQSTVDDLLLLDDKITGVATHLGITFSARAVVLTVGTFLGGLAHVGDRNFQAGRAGDPASIRLAHRLREMNLSVGRLKTGTPPRIDARTIDFQFLREQPGDEPIPTFSFLGNTAQHPRQVSCWMTRTNEKTHEIIRAGLDHSPLYTGKIEGIGPRYCPSIEDKVVRFSDRDSHTVFLEPEGLETSEIYPNGISTSLSFEVQVELVRSIAGLENAHITRPGYAIEYDYFDPRALKRSLETKAIDGLFFAGQINGTTGYEEAAAQGLLAGLNASLKIKEQESWCPSRDEAYLGVLVDDLVTRGVTEPYRMFTSRAEFRLQLREDNADMRLTEAGHQFGLVDEKRWQIFAAKREAIETEKARLRRTWVPAGVLHKLQTLQTSDQSDDRSYSLYELLRRPGISYTELVSLSEVESSMIDGRIAQQLEIDVKYEGYVERQRQEVVRHTQHETMVLPKNLDYSTVRGLSNEVTQKLNQHQPETIGQAARISGITPAAISLLLVHLKRGMARQAAKQEETHESGKTVA
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Q0ADD6
Q4ZL75
PDXY_PSEU2
Pyridoxal kinase PdxY
Pseudomonas syringae
MKRTPHLLAIQSHVVFGHAGNSAAVFPMQRIGVNVWPLNTVQFSNHTQYKQWTGEVLAPQQIPALIDGIAAIGELGNCDAVLSGYLGSAAQGRAILTGVARIKAANPKALYLCDPVMGHPEKGCIVAPEVSDFLLQEAAAMADFMCPNQLELDSFSGRKPESLHDCLAMARALLARGPRAIVVKHLDYPGKAADGFEMLLVTAEASWHLRRPLLAFPRQPVGVGDLTSGLFLSRVLLGDDLVAAFEFAAAAVHEVLLETQACGSYELELVRAQDRIAHPRVKFEAVRL
Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
Q4ZL75
Q6KZH9
THIE_PICTO
Thiamine-phosphate pyrophosphorylase
Picrophilus
MKLSGLYLVTKDYYNGNFFNIVEESLSAGVNILQYRDKTNPYNIKIEAGRRLKNLAYKYNVPFIVDDSPVLLDILDADGIHIGKDDPPFEYIKERFPGKIIGVSTYGDINLGIKYERLGADYIAFGSFFKTSTKDDAEMCDINILNNASKFNIPVFAIGGINTRNVDELLKYKISGIAVVSAIFDAANPGEATRTFLEKLRKIL
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Q6KZH9
A0QLV3
Y4764_MYCA1
Putative S-adenosyl-L-methionine-dependent methyltransferase MAV_4764
Mycobacterium avium complex (MAC)
MAATAEVGVTATLGAAARAVATRQGLLNDPYAEPLLGAVGIDYLTRAIADHTFAADESPVGDDPAVTSLLDALAAHTRFVDEFLAEAGRAGIRQVVILASGLDTRPYRLWWPRGTTVYEIDRPRVLDFKAGVLRGLDARLATNRCAVGIDLRDDWPAALRRVGFDAAQPTAWVAEQLLVGYLKPAEQNRLLRRLTAASAAGSRLAADHLPTWDPLQLEAERAFVEGWRRRGLDIDLASLTHPGEYHYVPEYLATHGWEPAARSIADLLGALGLGPRRRAGSGGAQFIPEYVTATRV
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
A0QLV3
B7H316
GRPE_ACIB3
HSP-70 cofactor
Acinetobacter calcoaceticus/baumannii complex
MANEQNEQAQDIQNEQVEQSNEQTQAEGVEQANDVTVESLQAQITKLEENLKLEKARTANAVYEAQKSVERIQRESEKHKETVLEKFAKELLDSVDNLERAIQAAGDEETPVLEGVKLTLKSLLTTLEKFGVVEADTQNGFNADLHQAVGIDPNAKANEIGTVLQKGYTLNGRLLRPAMVMVGQ
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
B7H316
Q48UX8
RL1_STRPM
50S ribosomal protein L1
Streptococcus
MAKKSKQMRAALEKVDSTKAYSVEEAVALVKETNFAKFDASVEVAYNLNIDVRKADQQIRGAMVLPNGTGKTQRVLVFARGAKAEEAKAAGADFVGEDDLVAKINGGWLDFDVVIATPDMMAIVSRLGRVLGPRNLMPNPKTGTVTMDVAKAVEESKGGKITYRADKAGNVQALIGKVSFDADKLVENFKAFHDVMAKAKPATAKGTYMANVSITSTQGVGIKVDPNSL
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
Q48UX8
Q9URV2
APC1_SCHPO
Cell untimely torn protein 4
Schizosaccharomyces
MLELKTNVIQDPELKDSLDLQENDRVEIIGDAVHYIVNDHLNRVFNYTVDQQKIHAALITTFASGKKAIVVILDDIGYVYYVGDNNNDSYIINVPFSTESAWSSPSGLYLQRHRSSDENLNTDLPHIFCLNDPLDELTLIKFDGKKILSLFDSIVYVVGEIVVTHNKKEKKLSFWRSRFIDPESDQSIKSSRNRRRESSFSREKNPDLTRSDSIHYTANTRLSEKFEEQGLAYSTIFSHIESFPITGSTSFDSILGNGVLVITTLVKELEKGYMMLFRLVRDRSPYFLDSLQLHAINLSAIKSKHLQKIVVLSSKGKVSLESPMSPSLPIEGTFRSFRVHGATLYLEDTDGVQRYISLDNRASNSLVKWCLSVIRYVLPLREYEIFYTGHLYALFAFKLSHDEAFISSILACFTFFSRDKVHVEPIEDCNEAYSLSSKFHFKKEILIASQLSSHLDYSTFKNYLMPLAITLHFISEELRLDSVVKPRKDQLVALLLQITTWLKWPRYCEYYNFDIAETFLSIPLSIQVDVEEPVGPTSILQWIIECLRSQSTVPFYGLESYGLPHSCSTMFPQTLSLMQLLDCLLNPNMTLQNLVEEMVRLGISRKRCERYPFGILCIIFTVLEIAAEEYSPNWESEELRLVNRLDVDSFLHPKTPKWVFNKQDQEVKEIKALTSTVTDSTLVDTQSFHPYKVVTDMIFREDRRLAEVNKLLNYSSQITIMTEHFDVDLSSVPMQQKVAQCICVRTLSVPIGAGMLTYGSKNPLPTEKVTPRLFNFTLHLHPGTLIIQPNKEFVTQELTEWPEFNVGVALGLSISKFSKEINTSWIMFNRPETLTAYHAGFLFGLGLNGHLKALATWHSFIYLTSKHDTTSIGLLLGLASSYLGSMDAKVTKLLSVHISALLPVGSNELNISPLTQTAGILGIGLLFHDSCHRRMSEVTMEEILASNESELKNEGYKLAAGFSLGLINLGRGSNLPGMSDLKLVSRLQVGISSQATFQSLEAGSPGAIMALTMIYMKTNDLEVAKKIDIPKSRYLLDFYRPDLILLRVAGKNLIMWDEVKADYEWVKYQIPDIMLSQFDLQEKKVLSSDDLLLYNVLAGICFSLGLRFAGTGNPKAKEILINFLDSFIRLCHLPAKTHDERVTAVTVIRCTQIVALSSSCVMAGYCDLDVLRRLRVLHGRMEPVNYGAQMATHMALGILSLGGGRYSLSRSNLAIAALLISFYPQFPRTTQDNRAHLQAARNLWALAVEERCIIPRNQDTKQPCIVPLNVVQKSGAVQKLEAPILLPPYDSISSVSTLGDKYWNLKIDLDNNSDYRELLRESQTLTLMPYDRTSSKEEPLNLFPKLKDTSSPLWNLVKTSRLFQSSNSPLNVASLQESNNKTSLGVKLLLSMDFDNLTRDRLLSLQILLQFFESCWTGVLLNKFHSRQYLFLSRDLVEDLSLRVWEYVYSHNHNEESV
Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Mutations to this protein prevent the exit from mitosis.
Q9URV2
Q96N28
PLD3A_HUMAN
Protein slowmo homolog 1
Homo
MKIWSSEHVFGHPWDTVIQAAMRKYPNPMNPSVLGVDVLQRRVDGRGRLHSLRLLSTEWGLPSLVRAILGTSRTLTYIREHSVVDPVEKKMELCSTNITLTNLVSVNERLVYTPHPENPEMTVLTQEAIITVKGISLGSYLESLMANTISSNAKKGWAAIEWIIEHSESAVS
In vitro, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space. Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane.
Q96N28
B5FPG7
NUOCD_SALDC
NDH-1 subunit C/D
Salmonella
MTDLTAQDAAWSTRDHLDDPVIGELRNRFGPDAFTVQATRTGIPVVWVKREQLLEVGDFLKKLPKPYVMLFDLHGMDERLRTHRDGLPAADFSVFYHLISIERNRDIMLKVALSENDLRVPTFTKLFPNANWYERETWEMFGIDIEGHPHLTRIMMPQTWEGHPLRKDYPARATEFDPFELTKAKQDLEMEALTFKPEDWGMKRGTDNEDFMFLNLGPNHPSAHGAFRIILQLDGEEIVDCVPDIGYHHRGAEKMGERQSWHSYIPYTDRIEYLGGCVNEMPYVLAVEKLAGITVPDRVNVIRVMLSELFRINSHLLYISTFIQDVGAMTPVFFAFTDRQKIYDLVEAITGFRMHPAWFRIGGVAHDLPRGWDRLLREFLEWMPKRLDSYEKAALRNTILKGRSQGVAAYGAKEALEWGTTGAGLRATGIDFDVRKWRPYSGYENFDFEVPVGGGVSDCYTRVMLKVEELRQSLRILQQCLDNMPEGPFKADHPLTTPPPKERTLQHIETLITHFLQVSWGPVMPAQESFQMVEATKGINSYYLTSDGSTMSYRTRVRTPSFAHLQQIPSAIRGSLVSDLIVYLGSIDFVMSDVDR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
B5FPG7
Q4R2Z8
ZN541_MACFA
Zinc finger protein 541
Macaca
QMQVFQMITKSQRIFSHAQVSKASSQLPAPEGKPAALRPLQGPWPQQLPPLAPAVDSLNAGPGNPEAEGSPARRRKTTPGVAREASPGNTRRDAKGGLKVAAVPTPLAAPSLDPSRNPDISSLAKQLRSSKGTLDLGDIFPSTGQRQTQLGGEELPGASLPGKQAPAENGAVSGTTKGEKGPPCSRGGGYRLLGNPRAPRFSGFRKEKAKMDMCCAASPSQVAMASFSSAGPPADPSKSKLTIFSRIQGGNIYRLPHPVKEENVAGGGNQQNGGSTDWTEPRSTFICKNCSQMFYTEKGLSSHMCFHSDQWPSPRGKQEPQVFGTEFCKPLRQVLRPEGDRHSPPGAKKPLDSTAAAPLVVPHSIPVVPVTRHVGSMAMEQEKDGEERDSKESSQQRKRKKRPPPKRLFIPPPPSTAGEPGPAGCHQSRLRSPMFLVDRLLKGLFQCSPYTPPPMLSPIREGSGVYFNTLCSTSTQASPDQLISSMLDQVDGSFGICVVKDDTKISIEPHINIGSRFQAEIPELQERSLAGIDEHVASLVWKPWGDMMINPETQDRVTELCNVACSSVMPGGGTNLELALHCLHEAQGNVQVALETLLLRGPHKPPTHLLADYRYTGSDVWTPIEKRLFKKAFYAHKKDFYLIHKTIQTKTVAQCVEYYYIWKKMIKFDCGRAPGLEKRVKREPEEVERTEEKVPCSPRERPSHHPIPELKIKTKSYRRESILSSSPNAGPKRTPEPSGSVESQGIFPCRECERVFDKIKSRNAHMKRHRLQDHVEPIVRVKWPVKPFQLKEEELGADIGPLQW
Component of some chromatin remodeling multiprotein complex that plays a role during spermatogenesis.
Q4R2Z8
D4ASE6
SCPF_ARTBC
Serine carboxypeptidase ARB_07161
Trichophyton
MKGLLSLLLVGAANALAASYEPRSLTEDMLQGKEKEVWDAIKGEIPGAQLDDYFNPPTAHQREPDEKWDGKLEGKSVNTLWVEEGKDKPSGIEEYGMRFKTVDPSSLGVDNVTQYSGYLDNKKNGQHLFFWFFESRRDPQYDPVILWLNGGPGCSSMTSLFMELGPARVGQDLKLTRNPNSWNNRASIIFLDQPVNVGFSYGKSGAFNTPSASKDVFAFLTLFFKKFPQYALQDFHIAGESYAGHYIPFASYPPMACGKGGYSAVLDQPTCKAMEAAVPQCQKEIKRCYDKPTDVATCVKGAKFCKDALVRPYSRTGQSIYDIRGRCEDPKDLCYPILGWIAKYLNQRHVQKAIGAEVSHFKGCSNHISSQFFAHGDYNQPFHRKIPGILKDVNVLVYAGDADYICNWLGVKEWTEALQWPGRHIFRRKNLSVVYHSVNKWPLGRVKYHNGLAFLQVFKAGHRVPYDQPENALDFFNRWLAGEWTP
Involved in degradation of small peptides.
D4ASE6
Q0I738
PSBU_SYNS3
PSII-U
unclassified Synechococcus
MKRLLSWLTGLVVIAGLLIGLLVPPSVSAAEIRNVADDKLAERGDKVDLNNSSVRRFQQFPGMYPTFAGKIVLGGPYENVDDVLKLDLSERQKELFEKYRDNFVVTAPSIALNEGFDRINDGQFR
Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
Q0I738
Q5F8Z2
ENO_NEIG1
2-phosphoglycerate dehydratase
Neisseria
MSAIVDIFAREILDSRGNPTVECDVLLESGVMGRAAVPSGASTGQKEALELRDGDKSRYSGKGVLKAVEHVNNQIAQALIGIDANEQSYIDQIMIELDGTENKGNLGANATLAVSMAVARAAAEDSGLPLYRYLGGAGPMSLPVPMMNVINGGEHANNSLNIQEFMIMPVGAKSFREALRCGAEIFHALKKLCDSKGFPTTVGDEGGFAPNLNSHKEALQLMVEAAEAAGYKAGEDVLFALDCASSEFYKDGKYHLEAEGRSYTNAEFAEYLEGLVNEFPIISIEDGMDENDWEGWKLLTEKLGKKVQLVGDDLFVTNPKILAEGIEKGVANALLVKVNQIGTLSETLKAVDLAKCNRYASVMSHRSGETEDSTIADLAVATNCMQIKTGSLSRSDRMAKYNQLLRIEEELAEAAYYPGKAAFYQLGK
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q5F8Z2
Q93W66
TM16A_ARATH
Protein MUTANT SNC1-ENHANCING 5 LIKE
Arabidopsis
MAARVLASVIVMGSGIIARACTQAYRQALANASKTGVAHEATQTIKRGLTIGEAEARQILGVTEKSSWDEILKKYDTLFERNAQNGSFYLQSKVHRAKECLETAYQKSTTTSA
Regulates ATP-dependent protein translocation into the mitochondrial matrix.
Q93W66
Q9LWU9
DLT_ORYSJ
Protein SMALL ORGAN SIZE 2
Oryza sativa
MLAGCSFSSSRHQMSTAQRFDILPCGFSKRGSRGDGAAPRVAGDARSGATTCSFRTHPAPPVTQSVSWGAKPEPGGNGNGAHRAVKRAHDEDAVEEYGPIVRAKRTRMGGDGDEVWFHQSIAGTMQATAAGEGEEAEEEKVFLVPSAAAFPHGMAAAGPSLAAAKKEEYSKSPSDSSSSSGTDGGSSAMMPPPQPPEFDARNGVPAPGQAEREALELVRALTACADSLSAGNHEAANYYLARLGEMASPAGPTPMHRVAAYFTEALALRVVRMWPHMFDIGPPRELTDDAFGGGDDDAMALRILNAITPIPRFLHFTLNERLLREFEGHERVHVIDFDIKQGLQWPGLLQSLAARAVPPAHVRITGVGESRQELQETGARLARVAAALGLAFEFHAVVDRLEDVRLWMLHVKRGECVAVNCVLAMHRLLRDDAALTDFLGLARSTGATILLLGEHEGGGLNSGRWEARFARALRYYAAAFDAVDAAGLPEASPARAKAEEMFAREIRNAVAFEGPERFERHESFAGWRRRMEDGGGFKNAGIGEREAMQGRMIARMFGPDKYTVQAHGGGGSGGGEALTLRWLDQPLYTVTAWTPAGDGAGGSTVSASTTASHSQQS
Probable transcription factor that acts as positivie regulator of brassinosteroid (BR) signaling . Functions downstream of BRI1 and GSK2 to modulate BR responses. Acts as a direct target of GSK2 kinase to mediate BR responses . Involved in feedback inhibition of BR biosynthetic genes. Repressed by BZR1 . Cooperatively functions in a transactivating complex with SMOS1 to enhance the transcription of the SMOS1 target PHI-1, and regulate plant organ size . Interaction between SMOS1 and DLT is a crosstalk point for auxin and brassinosteroid signaling .
Q9LWU9
Q4WCX4
NACB_ASPFU
Beta-NAC
Aspergillus subgen. Fumigati
MDQAKLARMQASVRIGTFCSFLWIFEVLESESVFSADGFQAHHLGNVIGKGTPRRKVKKVHKSSGADDKKLQTTLKKMNVQPIQAIEEVNMFKEDGNVIHFAAPKVHASVPSNTFALYGNGEEKELTELVPGILNQLGPDSLASLRKLAESYQNMQKQAGAEGKKDEDEDDIPDLVEGENFESNVE
Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II.
Q4WCX4
Q9XXM8
NHR68_CAEEL
Nuclear hormone receptor family member nhr-68
Caenorhabditis
MENKEVCLVCQDFSSGYHYGIPSCNGCKTFFRRTVMKKQKFVCQFDQNCPVDKSIRCACRFCRFEKCLKVGMDKTSLQASRDPIGYTKRNKKTLRHPMNELSGDESNSCTPDRQLSPLRSFENSLNFLAVRERSANELRMSSYLPKRSLKQALCSKPLINDPIFMSKHATVSPRHTFEKLRFITQDDYHYWHERDWFVLTEYAKTFKVFKNMPYHDKTELVCHAAIVIPVLNQVYNSPDYGLDTVVFPDGTYYDRTHEPTRPAGLNRKKYQVLDLVLKPFREMEINFNEFAAFKAITFLNPDADISLESKHAINEERVLITKQLYAYMVQKDGLEKAIYRFGRLILMGTSMSKMACESKEAVWIADFFENIGFTSFAKELIFGDH
Probable transcription factor that acts in a feed-forward loop with nhr-10 to activate genes, including itself, involved in the vitamin B12-independent breakdown of the short-chain fatty acid propionate . This pathway is triggered in response to a diet low in vitamin B12, when canonical vitamin B12-dependent propionate breakdown cannot function; the resulting accumulation of propionate is probably sensed by nhr-68 and/or nhr-10 .
Q9XXM8
Q8IYT1
GAR4_HUMAN
Golgi-associated Rab2B interactor-like 4
Homo
MNADFLLPYYTAQSGSSMSMFNTTMGKLQRQLYKGEYDIFKYAPIFESDFIQITKRGEVIDVHNRVRMVTMGIARTSPILPLPDVMLLARPATGCEEYAGHGQATKRKKRKAAKNLELTRLLPLRFVRISVQDHEKQQLRLKFATGRSCYLQLCPALDTRDDLFAYWEKLIYLLRPPMESNSSTCGIPAEDMMWMPVFQEDRRSLGAVNLQGKGDQDQVSIQSLHMVSEVCGATSAAYAGGEGLQNDFNKPTNVLNASIPKTSTELAEEPATGGIKEAAAAGAAAGAATGTVAGALSVAAANSAPGQVSAAIAGAATIGAGGNKGNMALAGTASMAPNSTKVAVAGAAGKSSEHVSSASMSLSREGSVSLAIAGVVLTSRTAAEADMDAAAGPPVSTRQSKSSLSGQHGRERTQASAEGCKEGRERREKDRALGRSSHRRRTGESRHKTRGDKIAQKSSSRSSFSHRANRDDKKEKGCGNPGSSRHRDSHKGVSHTPISKESRTSHKSGRSLWTTSSGSSKGLGRVSSFLRNVRANLTTKVVGTPHGRDVNVMAKMAERSTNVAIAETAEGGQGLETVGSMTPDIMETVTFEAH
RAB2B effector protein required for the compacted Golgi morphology, probably through interaction with small GTPase RAB2B.
Q8IYT1
Q97VS5
PCKG_SACS2
Phosphoenolpyruvate carboxykinase [GTP]
Saccharolobus
MKSSLDFLNNFIQRDAVKKLESINNYPLIEFLNSVVKLCEPDSVYLITGSDEEKEYIRKKALESKEEIRLQTSGHTIHFDHPLDQARAREDTFILSDTKIPYVNTKPRNEGLSEMLTLLKGSMRGREMYVGFYSLGPRNSPFQILAVQVTDSPYVIHSENILYRIAFEDFSNNTKFLRFVHSKGEPDIKKRRIMIDLANNTVYSVNTTYAGNSVGLKKLALRLTIMKAVEEGWLSEHMAIVGFNGDKGIHYFTASFPSGSGKTSTSMIGNLISDDLAFIREFEGLPKAVNPEIGVFGIIQGINARDDPIIWEVLHKPGEVIFSNVLMTEDGDVYWEGSELPKPERGYNHEGRWDRESGKPASHPNARFTVPLTSFSNLDKNWDNPNGVIIDGIIFGVRDYSTLVPVVEAFSWSHGVITIGASMESARTSAVIGKSDELEFNPMAILDFMPISLSRYLRNYLNFGKRLRKSPKIFGFNYFLKDDNKFLNSKEDKKVWVSWAVKRVEETANAIYTPIGLIPFYEDLKALFKRVLGKEYGKEEYEKQFTIKLRKYLEKTERIIEIYLKFEDIPSEVINELKMQKERIVDYINKYGDSVSPFRLEKD
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Q97VS5
Q5LCA7
THIE_BACFN
Thiamine-phosphate pyrophosphorylase
Bacteroides
MLSLQFITHQTENYSYLESARMALEGGCKWIQLRMKEASPEEVEAVALQLKPLCKAKEAILILDDHVELAKKLEVDGVHLGKKDMPIGEARQMLGEAFIIGGTANTFEDVKLHHAAGADYLGIGPFRFTTTKKNLSPVLGLEGYTSILAQMNEAGIRIPVVAIGGIVAEDIPAIMETGVNGIALSGAILQAPDPVEETKRILNI
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Q5LCA7
A9AA46
GATD_METM6
Glutamyl-tRNA(Gln) amidotransferase subunit D
Methanococcus
MDIGDFVKLELENTTYSGTLMPSLNENTIVIKMKSGYNVGLDKKKIKNIEILESGDKPKYGLPPLNLEKNPKLKNISILSTGGTVASRVDYKTGAVHPAFTADDLIRAVPELMDVANIKGKVILNILSENMLPKYWAMTAEAIKEEIENGAEGIVIAHGTDTMHYTASALSFMVTSEVPIILVGAQRSSDRPSSDAALNIIAAVKAATEPIKGVYVLMHGETGDTVCHLHEGTKVRKLHSSRRDAFKSVNKTPIAEVNPVTKEVKYLRDVKSRDKSKIKEVVLNTNLEEKVALIKVYPGIDSEILKFYVDNGYKGIILEGTGLGHTPETFFEGIDYANENNVLVAMTTQTINGRVNMNVYSNGRELQAKGVIPCEDMLSEVAFVKLMHLLGNYEFEEAKELMPKNIAGEINESINLEC
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate.
A9AA46
A4VZL7
RSMG_STRS2
16S rRNA 7-methylguanosine methyltransferase
Streptococcus
MKPEVFYKTLADQGIQLTDQQKHQFHRYFQLLVEWNEKINLTAITEESEVYLKHFYDSIAPLLQGHIQNEPLRLLDIGAGAGFPSLPMKIIFPQLDVTIIDSLNKRINFLHLLAEELELEGVHFYHGRAEDFAQDKNFRAQFDLVTARAVARMQILSELTIPYLKLHGKLIALKASSAEDELTQAKNALNLLFAKVIENHDYTLPNGDPRTLTIVEKKKETPNKFPRKAGMPNKRPL
Specifically methylates the N7 position of a guanine in 16S rRNA.
A4VZL7
B5DF27
LOXL2_RAT
Lysyl oxidase-like protein 2
Rattus
MEIPFGSCLYSCLALLVLLPSLSLAQYESWPYQLQYPEYFQQPPPEHHQHQVPSDVVKIQVRLAGQKRKHNEGRVEVYYEGQWGTVCDDDFSIHAAHVVCREVGYVEAKSWTASSSYGPGEGPIWLDNIYCTGKESTLAACSSNGWGVTDCKHPEDVGVVCSEKRIPGFKFDNSLINQIESLNIQVEDIRIRPILSAFRHRKPVTEGYVEVKEGKAWKQICDKHWTAKNSHVVCGMFGFPAEKTYNPKAYKTFASRRKLRYWKFSMNCTGTEAHISSCKLGPPMFRDPVKNATCENGQPAVVSCVPSQIFSPDGPSRFRKAYKPEQPLVRLRGGAQVGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGTAKEAVTGSRLGQGIGPIHLNEVQCTGTEKSIIDCKLNTESQGCNHEEDAGVRCNIPIMGFQKKVRLNGGRNPYEGRVEVLTERNGSLVWGNVCGQNWGIVEAMVVCRQLGLGFASNAFQETWYWHGNIFANKVIMSGVKCSGTELSLAHCRHDEEVVCPEGGVQYGAGVACSETAPDLVLNAEIVQQTAYLEDRPMALLQCAMEENCLSASAVHTDPTRGHRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTYYDLLSLNGTKVAEGHKASFCLEDTECEGDIQKSYECANFGEQGITMGCWDMYRHDIDCQWIDITDVPPGDYLFQVVINPNYEVPESDFSNNIMKCRSRYDGYRIWMYNCHVGGAFSEETEQKFEHFSGLLNNQLSVQ
Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3. During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction. When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.
B5DF27
Q21MI1
ERPA_SACD2
Iron-sulfur cluster insertion protein ErpA
Saccharophagus
MSAPQTFVPEPVQVTENALAKVKALIEEEGNPDLKLRVFVTGGGCSGFQYGFAFDEACAEDDAKIERDGVTVVVDAMSYPYLVGAQVDYEEGLKGSKFVVANPNASTTCGCGSSFSI
Required for insertion of 4Fe-4S clusters for at least IspG.
Q21MI1
F8WKW0
UGT1_GARJA
UDP-glycosyltransferase 75L6
Gardenia
MVQQRHVLLITYPAQGHINPALQFAQRLLRMGIQVTLATSVYALSRMKKSSGSTPKGLTFATFSDGYDDGFRPKGVDHTEYMSSLAKQGSNTLRNVINTSADQGCPVTCLVYTLLLPWAATVARECHIPSALLWIQPVAVMDIYYYYFRGYEDDVKNNSNDPTWSIQFPGLPSMKAKDLPSFILPSSDNIYSFALPTFKKQLETLDEEERPKVLVNTFDALEPQALKAIESYNLIAIGPLTPSAFLDGKDPSETSFSGDLFQKSKDYKEWLNSRPAGSVVYVSFGSLLTLPKQQMEEIARGLLKSGRPFLWVIRAKENGEEEKEEDRLICMEELEEQGMIVPWCSQIEVLTHPSLGCFVTHCGWNSTLETLVCGVPVVAFPHWTDQGTNAKLIEDVWETGVRVVPNEDGTVESDEIKRCIETVMDDGEKGVELKRNAKKWKELAREAMQEDGSSDKNLKAFVEDAGKGYQAESN
Glucosyltransferase acting on a broad range of substrates, including crocetin, 4-coumaric acid, caffeic acid and ferulic acid. No activity with indol-3-acetic acid, bixin and norbixin, and no formation of O-glucosides. Involved with UGT94E5 in sequential glycosylation of crocetin to crocin (bis(beta-D-gentiobiosyl) crocetin).
F8WKW0
P38544
RAN_ONCVO
Ras-related nuclear protein
Onchocerca
MATGDDIPTFKLVLVGDGGTGKTTFVKRHLTGDPEKKYVATLGVEVHPLIFHTNRGQIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTARVTYKNVPNWHRDLARVCENIPIVLCGNFVDVKDRKVKAKTITFHRKKNLQYYDISAKSNYNFEKPSLWLVRKLLGDPNLEFVAMPALAPPEVQMDPTMVAQYEQEIAAAANAELPDDDEDL
GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis.
P38544
A8GXR7
DER_RICB8
GTP-binding protein EngA
belli group
MTKKIIAKKIIALVGRPNVGKSTLFNRLSMRKKAIVHDLPGVTRDRKYTDGRIGSFEFSLIDTPGFEENPDSFGKRLMEQTTKAINEADLICFMVDSRSGILPDDKLLSDFVRKYNKPAVLVINKCEKAFDFDKEYYKLGFDSMVAISAEHGTGMIDLYDEIIAKLPEEDSAEAEIHDPIKGDCLQIVVSGRPNAGKSTFINALINDERLLTGPEAGITRESIEIDWQYKGNHIKLIDTAGLRKKATITESLEKLSASDAINSIKFANTVILMIDALSPLKQQDLNIASHVANEGRSIVIVVNKWDLIKESEKEAFKEEFYYQINTTLPQVKGVPALFISAKNKQNIADVLDSCIKIYKTWNKKITTSKLNEWLNFTTEAHPLPLQKGGKRVRVKYMTQTKTRPPTFKLFSNNPEKITDSYTRYLVNNMREAFDMPGVPIRFNYIKTKNPYV
GTPase that plays an essential role in the late steps of ribosome biogenesis.
A8GXR7
Q1GPJ7
TRMD_SPHAL
tRNA [GM37] methyltransferase
Sphingopyxis
MSFTAVPLTLYPDMFPGPLGHSMAGRALESGTWNCAPVQIRDFATDRHRTVDDTPAGGGAGMVLKADVLAGAIDHAMKAHPGLPVLAMTPRGTPITQARVRELAAGPGAIILCGRFEGFDERIFDARPIEQVSMGDIILSGGEMAALLLLDACIRLLPGVMGAASSGDDESFENGLLEYPHYTRPVTWEGRTIPEVLRSGDHAKIAAWRKQQAEEATRLRRPDLWERHIDARARPASGARRKEED
Specifically methylates guanosine-37 in various tRNAs.
Q1GPJ7
O67342
NUON1_AQUAE
NDH-1 subunit N 1
Aquifex
MNWNAILPEAILAIGILTVFILELFLERKHYKFLSVLAFIFVVLSGYSIFFVNYPAKLFFDGFSVDALNLIGKLFILAVTGFVLLSSYDYFSKKNSQYGELPYLYLIATLGLMVMISSDNLAIIFTGLELASITMYILVGLFRREYLSKEGAFKYLVIGTTGTSMYALGSALVYASSGSMVLSPVKEENTLFALGVILIISALALKVSAVPFHFWTPDAYEGAPTPTTAYLSTVPKIGMYFLFVKLTMYLFSAFPDWKYVVMLLAVLSMFYGNIVAYAQKSVKRLLAYSSIAHAGYFLTALTAVDKHLFSALLFYVFVYALATVGAFTVLAILEKKEGWTHHFLDFKGLKEENPVLASMLALFLFALIGIPPAAVFLGKLGIFFGLVKTDMFALGILFAIASLISAGYYLKVIVYMFLYSGEVRHGQTTVSAGEAFTVLGTAFLVIFFGLFPHVVLDFILRALS
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
O67342