accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q8DAR1
|
GLGC1_VIBVU
|
ADP-glucose synthase 1
|
Vibrio
|
MAGVLGMILAGGEGSRLRPLTESRSKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLFHHMKKGWNINGITDRFIDPIPAQMRTGKRWYEGTADAIYQNLRFMELSEPEQVCIFGSDHIYKMDIKQMLSFHKEKLAALTVSALRMPLAEASQFGVIEVDAEGRMVGFEEKPSAPKSIPGDPDFALVSMGNYIFEADVLFAELIEDADNENSSHDFGKDIIPKMFPRGDVFVYDFSQNRISGEKAEVYWRDVGTIDAYWQAHMDLLKTDAPFSLYNRKWPLHTYQPPLPPATFTDSDNGRVQIIDSLVCNGSYVRGSRIEKSVLGFRSNIASACDISESILLGDVKVGEGCVLRRVIVDKDVDIAPGTQIGVNLQEDKKIFHVSDDGIVVIPKGARVGY
|
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
|
Q8DAR1
|
P83243
|
KA131_TITOB
|
Toxin To1
|
Tityus
|
ACGSCRKKCKGSGKCINGRCKCY
|
Blocks reversibly Shaker B potassium channels. Also displaces binding of noxiustoxin to mouse brain synaptosome membranes.
|
P83243
|
B0Y0Y6
|
CLP1_ASPFC
|
mRNA cleavage and polyadenylation factor clp1
|
Aspergillus subgen. Fumigati
|
MSLPGLELSQTSSEREFVPAPPTQITLSKGSEWRFEVAFGTAIRVKLLAGTAELFGTELAASQTYTFSGTKAAIYTWHGCTLEVSAGDTISTIDGLGSGGLNGEGARGYGAGGCQSEYTAEETPMVEYANVHFALEAMRQEAKATGKDGPRVLILGPENAGKTSVAKILTAYATKVGRQPIVVNLDPAEGMLSVPGTLTATAFRTMMNVEEGWGSSPMSGPSAVPVKLPLVYFYPLQNPLEAEGAVYRPIVSRLALSVTGRMAEDEDTRETGIIVDTPGILSAGKPGSLEIINHIVTEFASSERLYSTMMKNYDNKPTSSASAAASDERITVVKLSKSGGCVDRDAAFMKSVRESQIRTYFFGNPIPSTASAALSMSASSTTNITLSPHAQQLDFDSLAVYNYTIASSDEDEDEYDPSQFGASDTFLPGGRNDAEGPETKHAEETSFTSSVPGLGGPSGDDAASGSSAVPLKKVLPPAPNTLANSLLAVTHTAPNASPAEIRDASIMGFLYVADVDSEKGKIRVLAPIGGRVPPRAIVWGKKWPGEVVGLVG
|
Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
|
B0Y0Y6
|
P32568
|
SNQ2_YEAST
|
Protein SNQ2
|
Saccharomyces
|
MSNIKSTQDSSHNAVARSSSASFAASEESFTGITHDKDEQSDTPADKLTKMLTGPARDTASQISATVSEMAPDVVSKVESFADALSRHTTRSGAFNMDSDSDDGFDAHAIFESFVRDADEQGIHIRKAGVTIEDVSAKGVDASALEGATFGNILCLPLTIFKGIKAKRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVSGEVAYDGIPQEEMMKRYKADVIYNGELDVHFPYLTVKQTLDFAIACKTPALRVNNVSKKEYIASRRDLYATIFGLRHTYNTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAFVTIYQASENIYETFDKVTVLYSGKQIYFGLIHEAKPYFAKMGYLCPPRQATAEFLTALTDPNGFHLIKPGYENKVPRTAEEFETYWLNSPEFAQMKKDIAAYKEKVNTEKTKEVYDESMAQEKSKYTRKKSYYTVSYWEQVKLCTQRGFQRIYGNKSYTVINVCSAIIQSFITGSLFYNTPSSTSGAFSRGGVLYFALLYYSLMGLANISFEHRPILQKHKGYSLYHPSAEAIGSTLASFPFRMIGLTCFFIILFFLSGLHRTAGSFFTIYLFLTMCSEAINGLFEMVSSVCDTLSQANSISGILMMSISMYSTYMIQLPSMHPWFKWISYVLPIRYAFESMLNAEFHGRHMDCANTLVPSGGDYDNLSDDYKVCAFVGSKPGQSYVLGDDYLKNQFQYVYKHTWRNFGILWCFLLGYVVLKVIFTEYKRPVKGGGDALIFKKGSKRFIAHADEESPDNVNDIDAKEQFSSESSGANDEVFDDLEAKGVFIWKDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGIITGDMLVNGRPIDASFERRTGYVQQQDIHIAELTVRESLQFSARMRRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLLRKGGQTVYFGDIGKNSATILNYFERNGARKCDSSENPAEYILEAIGAGATASVKEDWHEKWLNSVEFEQTKEKVQDLINDLSKQETKSEVGDKPSKYATSYAYQFRYVLIRTSTSFWRSLNYIMSKMMLMLVGGLYIGFTFFNVGKSYVGLQNAMFAAFISIILSAPAMNQIQGRAIASRELFEVRESQSNMFHWSLVLITQYLSELPYHLFFSTIFFVSSYFPLRIFFEASRSAVYFLNYCIMFQLYYVGLGLMILYMSPNLPSANVILGLCLSFMLSFCGVTQPVSLMPGFWTFMWKASPYTYFVQNLVGIMLHKKPVVCKKKELNYFNPPNGSTCGEYMKPFLEKATGYIENPDATSDCAYCIYEVGDNYLTHISSKYSYLWRNFGIFWIYIFFNIIAMVCVYYLFHVRQSSFLSPVSILNKIKNIRKKKQ
|
Could be an ATP-dependent permease. Confers hyper-resistance to the mutagens 4-nitroquinoline-N-oxide (4-NQO) and triaziquone, as well as to the chemicals sulphomethuron methyl phenanthroline when present in multiple copies. Exhibits nucleoside triphosphatase activity.
|
P32568
|
B2A5T8
|
SYP_NATTJ
|
Prolyl-tRNA synthetase
|
Natranaerobius
|
MSKNNEEFVKEITPQSEDYSQWYLDVIKKTKLVDYAPVKGCMVIRPYGYAIWEKMKEGLDRRIKETGHENAYFPLFIPESLLQKEADHVEGFAPEVAWITKGGDEELSESLAVRPTSEAMFGEMYSDWIQSWRDLPVLINQWANVVRWEKSTKPFLRTSEFLWQEGHTAHRTEEDAEEEALQMLDVYKDFVENDMAIPVLNGLKSEKEKFAGALRTFCIEALMSDGRALQAGTSHNLGQHFAKVFDITFLDQDDERKYVWQTSWGVSTRLIGALIMVHGDNRGLKIPPKVAPHQLVMVPITPKKQREQVLEESDKLYQELKDKFRVKLDNREEHTPGWKFNEWEMKGVPIRLEIGPKDIEKDQVVLVRRDTDEKMFVKRDELIDKLEELIEDIQNKMLQTAKNFLEENTHTASSLDELGQILEQKRGMIKAYWCGNQACEEKVKDDTKATIRVIPFEAETGGSCIACGYHNDDNKEVFFARAY
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
|
B2A5T8
|
A7Z1T2
|
CFR_BACVZ
|
23S rRNA m8A2503 methyltransferase
|
Bacillus amyloliquefaciens group
|
MQQKNKYIRIQEFLKQNKFPDFRMNQIKNAVFQGRINHFNEITVLPKSLRKLLIEEFGESILNIAPLKVQHSEQVTKVLFEISGDEKIETVNMKYKAGWESFCISSQCGCHFGCKFCATGDIGLKRNLTSDEMTDQILYFHLKGHSIDSISFMGMGEALANVQVFDALHVLTNPELFALSPRRLSISTIGIIPGIKKITQDYPQVNLTFSLHSPFNEQRSKLMPINERYPLLEVMDTLDEHIRVTSRKVYIAYIMLPGVNDSIDHANEVVNLLRSRYKRGNLFHVNIIRYNPTVSSPMRFEEVNEKQVVNFYKKLKSAGINVTVRSQFGIDIDAACGQLYGNYQKNKNQ
|
Specifically methylates position 8 of adenine 2503 in 23S rRNA. Confers resistance to some classes of antibiotics.
|
A7Z1T2
|
A5GLI2
|
PDXJ_SYNPW
|
Pyridoxine 5'-phosphate synthase
|
unclassified Synechococcus
|
MASLGVNIDHIANVRQARRTVEPDPVPMALLAELGGADGITVHLREDRRHIQDRDVDLLRQTVRSRLNLEMAATEDMVLIALRVQPDMVTLVPERREEVTTEGGLDVSSQRVDLTSKISRLQDAGIPVSLFVDPERGQLEACRDCRARWVELHTGTYAEAKWTDQPSELARLTEATALARAMGLRVNAGHGLTYQNVEPVAAIEGMEELNIGHTIVARAVAVGLQQAVREMKALVQNPRRDPLFGSY
|
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
|
A5GLI2
|
Q82IV0
|
DEF1_STRAW
|
Polypeptide deformylase 1
|
Streptomyces
|
MAQQDTDQQHTGVLPVDDDGFVIDAEDCEEREAAYRERGTSRPITVVGNPVLHKECKDVTDFGAELEQLVADMFASQRTAEGVGLAANQIGVDLKVFVYDCQDDEGTRHVGVVCNPKLVDLPADRRRLDDSNEGCLSVPTAYAPLARPDYAEVTGQDEKGNPIKVRGTGYFARCLQHETDHLYGYLYIDRLSKRERKDALRQMAENEPRYPVVAND
|
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
|
Q82IV0
|
B7IDI7
|
MURA_THEAB
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Thermosipho
|
MGYFKVKNSILNGNVRISGAKNSALPILAATILSSEKLEIENVPDLLDVQTMIEILRKIGKKVIFENNKVTLNGTVENHVVPYDLVRKMRASFNVAGPLAVILGESKVSLPGGCAIGVRPVDYHIMGLKKLGFEVEIEHGEVYIKKGKKEKEVIINLPFPSVGATEHLMTTAALMEGTTVIENAAMEPEIVDLQNFLNSLGAKIQGAGSRKIVIEGVNSLNGGSYKVIPDRIEAGTYAIAIAATGGKGYIEEIIPEHLEILWEILKETGTNVIIEKNRVFVDGEGKKRGININIQPYPGFPTDLQPQILVYLSLADGVSMVVENVFKNRFHHIDELVRMGADIRVVDGTAIVNGVKKLSGTKVEGTDLRATAALIIAGLVAEGTTEVHNDFHVLRGYENIVEKIRHLNGEIEHIV
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
B7IDI7
|
B1XLK6
|
HEM1_SYNP2
|
Glutamyl-tRNA reductase
|
unclassified Synechococcus
|
MNIVVVGLSHKTAPVEIREKLSIQEAKMDEAIAHLKSYPHVEEVAVISTCNRLEIYAVVQETEQGVREICQFLAETGQLQLNRLRRYLFTLLHQDAIRHLLRVAAGLESLVLGEGQILAQVKAAHKLGQQHKGLGRLLDRMFKRAITAGKRVRSETNIGTGAVSISSAAVELAQMKVKDLSNQKIAIIGAGKMSRLLVQHLVSKGAEDITIVNRSERGARDLAKKFPDVDLQLELLPEMLNVVEQADIVFTSTGATEPILDRAKLENLDLHTLILIDISVPLNVAADVEEIAGVRLYNVDALKEVVAQNQASRRKMAEEAEALLEEEVENYIQWWQSLETVPTISSLRSKVESIREQELEKALSRLGAEFEEKHQEVIETLTRGIVNKILHDPMVQLRAQQDIEARRVCLQSLQMLFNLETEEAI
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
B1XLK6
|
P0DP67
|
YAFV_YEREN
|
Omega-amidase YafV
|
Yersinia
|
MSTLKLTLLQQPLVWLDAQANLRHFDMLLESIQQRDVIVLPEMFTTGFAMNAAENALPETEVIDWLRHWSVRTDALIGGSVALNTPDGAVNRFLLVQPDGTILRYDKRHLFRMAGEHHHYLAGKERKVVEWRGWRILPQVCYDLRFPVWSRNQQDYDLALYVANWPAARAKHWQTLLAARAIENQAYVAGCNRVGDDDNGHHYQGNSVILDALGEIQAQAEPGQAAQLDAELSLETLQAYRERFPAFHDTDKFLLL
|
Hydrolyzes alpha-ketoglutaramate (a-KGM) to alpha-ketoglutarate (alpha-KG) and ammonia (specific activity 21 umol/min/mg), has very weak activity on L-glutamine, and no activity on deaminated glutathione (dGSH) or glutathione. May function as a metabolite repair enzyme.
|
P0DP67
|
Q99547
|
MPH6_HUMAN
|
M-phase phosphoprotein 6
|
Homo
|
MAAERKTRLSKNLLRMKFMQRGLDSETKKQLEEEEKKIISEEHWYLDLPELKEKESFIIEEQSFLLCEDLLYGRMSFRGFNPEVEKLMLQMNAKHKAEEVEDETVELDVSDEEMARRYETLVGTIGKKFARKRDHANYEEDENGDITPIKAKKMFLKPQD
|
RNA-binding protein that associates with the RNA exosome complex. Involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA and play a role in recruiting the RNA exosome complex to pre-rRNA; this function may include C1D.
|
Q99547
|
C1DST4
|
LPXA_AZOVD
|
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
|
Azotobacter
|
MSLIDPRAIIDPSATLAPDVRVGPWTLIGPHVHIGEGTEIGPHVIVRGPTWIGRHNRIFQFSTIGEDTPDLKYKGEPTRLVIGDHNVIREGVTIHRGTVQDRSETTIGDHNLIMAYVHIGHDSVMGSHCILVNNASLAGHVHVGDWAILSGYTLIHQHCQIGAHSFVGMGSGVSKDVPAFVTVLGSPAQARSMNFEGMRRRGFSPEAMNALRRAYKVVYRQGLTVEQALVELEESAKQFPEVAIFRDSVRASTRGITR
|
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
C1DST4
|
B2JP67
|
GCH4_PARP8
|
GTP cyclohydrolase FolE2
|
Paraburkholderia
|
MNQMNPAFVMPDVQSTVDTRQIPIQRVGVKAVRHPLTVRTPDGSAQPTVGTWNLDVHLPAEVKGTHMSRFVALLEENKAPLDSSAFRALLTSMLEKLEAPAGRIEVSFPYFVNKTAPVSGVQSLLDYEVSLMGDSRDGATRLFLKVLVPVTSLCPCSKKISQYGAHNQRSHVTINAELIDDVPVEDLIRIAEEEASCELWGLLKRPDEKFVTERAYENPKFVEDLVRDVAQRLNDDHRIVAYVLEAENFESIHNHSAYAVIESDKRLR
|
Converts GTP to 7,8-dihydroneopterin triphosphate.
|
B2JP67
|
Q1BFX4
|
Y088_MYCSS
|
Putative S-adenosyl-L-methionine-dependent methyltransferase Mmcs_0088
|
unclassified Mycobacterium
|
MSSLRTADDTWDIATSVGSTAVMVAASRAAETERDEALIRDPYARLLVTGAGTGIWESVLDAKFVETVAAADAEAAAIFEHMISYQAVRTHFFDAFFTAAAEAGIRQIVILASGLDSRAYRLDWPSGTTVYEIDQPKVLEYKSATLAEHGVEPAATRREVGIDLRHDWPAALRGAGFDPSRPTAWLAEGLLMYLPADAQDRLFEQITELSAPGSRVAAETAGVQAEDRRQQMRERFERIAEKFDMTASLDIQQLIYEDPDRADVADWLDAHGWTATAVSSQQEMRRLDRWALPADLTDDDAFSNFVTAEKQS
|
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
|
Q1BFX4
|
C5BZB0
|
CH60_BEUC1
|
Chaperonin-60
|
Beutenbergia
|
MAKIIAFEEEARRGMERGLNHLADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEEPFEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPIALKKGIDKAVEAVTAALLEQAKEVETKEEIAATAGISAGDPAIGELIAEALDKVGKEGVITVEESNALGLELELTEGMRFDKGYLSAYFVTDQERQEAVLEDAYILLVESKISSVKDLLPLLEKVIQGGKSLVIIAEDIEGEALATLVVNKLKGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISETVGLSLENADLDALGQARKIVVTKDETTIVEGAGDPDQLAGRVAQIRAEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALIQAGKVAFETLELVGDESTGGNIVKVAIDAPLKQIAINAGLEGGVVAEKVRSLPAGHGLNAATGDYEDLLAAGINDPVKVTRSALQNAASIAGLFLTTEAIVADKPEKASAPAGGGDGDMGGMGF
|
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.
|
C5BZB0
|
B6JCP2
|
TRPB_AFIC5
|
Tryptophan synthase beta chain
|
Afipia
|
MSLPKPNSFRAGPDERGHFGTFGGRFVAETLMPLILDLEKAYAAAKADPSFQKEMNGYLKDYVGRPSPLYFAERLTEHLGGAKIYLKREELNHTGSHKVNNVLGQIMVARRMGKKRIIAETGAGQHGVATATLCARFGLECIVYMGAVDVARQEPNVIRMEMLGAKVVPVQSGTRTLKDAMNDALRDWVTNVATTFYCIGTVAGPHPYPAMVRDFQSVIGHETREQMMAAEGRLPDSLVACIGGGSNAMGLFHPFLDEPAVEIFGVEAAGHGLTNLHAASLAGGRPGVLHGNRTYLLMNEDGQIQDAHSISAGLDYPGIGPEHAWLHETGRVTYLSATDEEALAAFQLLSRLEGIIPALESAHAIAKLSQLAPKRPRDHLMVVNLSGRGDKDVPQVGDILRGRKS
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
B6JCP2
|
A8MDY8
|
LEUC_CALMQ
|
Isopropylmalate isomerase
|
Caldivirga
|
MGLTLTEKILSKAAGRQVSPGDVTEITVDLAAFHDLTGHHVVEVMENIGAVKVWDLDRFVIAFDHLAPPPNDRAAEIQVKLRKFAKSINVRNFHDVGDGILHQLLLEKYALPGQVVMAADSHTTTVGAVGAFAQGMGASDMAAILMTGKTWLMIPEPFLIRLINEPAPGVYGKDVALHILSVFKAEGLNGKSVELQVEKPKAFPMDYRATVSNMGVEFGADAAIFIPDEETVSYLSRSRGINVKPITPDPDAKYVDEYTIELNKLEPLVAAPHSVDNVKPVSEVEGIEVDYVFIGSCTNGRLSDLEAAARILKNGKVKARCIVIPASRDLFTKALDAGYVETLTKAGCVVTYGTCGPCLGGHFGVIGPGETAVSTGSRNFKGRMGSPEGKVYLANAATAAATALEGRLTDPRKYL
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
A8MDY8
|
Q5HNR9
|
DTD_STAEQ
|
Gly-tRNA(Ala) deacylase
|
Staphylococcus
|
MKIIVQRVKNARVTNDTIDNQINKGYCLLVGVGQNSTEEDVKVIARKIAHARLFEDENDKLNLNIQQVEGEILSVSQFTIYADVKKGNRPGFSNSKAPEQAKDLYQKFNKELEGYGLIVKTGEFGTHMNVEINNDGPVTLIYESQDGKII
|
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
|
Q5HNR9
|
Q5XDY5
|
NANE_STRP6
|
ManNAc-6-P epimerase
|
Streptococcus
|
MPDKPTKEKLMEQLKGGIIVSCQALPGEPLYSETGGIMPLMAKAAQEAGAVGIRANSVRDIKEIQAITDLPIIGIIKKDYPPQEPFITATMTEVDQLAALNIAVIAMDCTKRDRHDGLDIASFIRQVKEKYPNQLLMADISTFDEGLVAHQAGIDFVGTTLSGYTPYSRQEAGPDVALIEALCKAGIAVIAEGKIHSPEEAKKINDLGVAGIVVGGAITRPKEIAGRFIEALKS
|
Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
|
Q5XDY5
|
Q2RNK3
|
COQ7_RHORT
|
2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase
|
Rhodospirillum
|
MTSPSSRTPRGSTPPFEPSADELVLHASGRKTAEDRLPGDPSPAALIDRFLRVDQAGEHGAVRIYQGQLAVLGRRSANVGVLRHMLAQEEVHLATFDKLVADRRARPTLLGPLWHVAGFALGAGTALLGEKAAMACTTAIEEAIDGHYKDQYDRLGDDELPLKATIDTFRREELEHRDIGYANGARQAPAFPVLSGAIKAGAKLAIWVSERV
|
Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
|
Q2RNK3
|
Q49434
|
T1SX_MYCGE
|
Putative type-1 restriction enzyme specificity subunit MG438
|
Mycoplasma
|
MTPKLKLNNNINWTKRTIDSLFDLKKGEMLEKELITPEGKYEYFNGGVKNSGRTDKFNTFKNTISVIVGGSCGYVRLADKNFFCGQSNCTLNLLDPLELDLKFAYYALKSQQERIEALAFGTTIQNIRISDLKELEIPFTSNKNEQHAIANTLSVFDERLENLASLIEINRKLRDEYAHKLFSLDEAFLSHWKLEALQSQMHEITLGEIFNFKSGKYLKSEERLEEGKFPYYGAGIDNTGFVAEPNTEKDTISIISNGYSLGNIRYHEIPWFNGTGSIALEPMNNEIYVPFFYCALKYLQKDIKERMKSDDSPFLSLKLAGEIKVPYVKSFQLQRKAGKIVFLLDQKLDQYKKELSSLTVIRDTLLKKLFPDMTERTKSIKDY
|
The specificity (S) subunit of a type I restriction enzyme; this subunit dictates DNA sequence specificity. This bacterium does not encode the associated endonuclease or methylase subunits.
|
Q49434
|
Q9W415
|
WUHO_DROME
|
tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit wuho
|
Sophophora
|
MCTTISFAEPEIVLGHGRRVLFVNPDDLQIFKEIELPPDLGLKGHTSQSQESCTAAAAASTATAASGQAPGGKEQQLANQPEEGGTSASASGLGCATSTSVQNVAYSPDGQLLAVTTSGKQKALLLYRSRPENARLLSARPLARASSALRFCSDSSSILVTDKTGDCYQYDCVEVEAPPRLLLGHLSVVYDILWSEDQQHIITCDRDDKIRVTNYPATFDIHSYCLGHREFVSGLALLTEQHIASASGDKTLRVWNYIQGKELLQHELPAPAVRLLVRQLEPEKVFQAAVLFYEHVDALGLYRLERSSDDTWSVTATQLVCAEAGSWSISNFTLTSDRIYITGAENERLSLRVYDIATGQPASSGVPEGWLKMVLDGLGANEEGAPPFIPEDLSVWFKKRFDNVSDYLERKKRRIEEQQQQKCG
|
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. Required during gametogenesis.
|
Q9W415
|
C0ZG86
|
SYI_BREBN
|
Isoleucyl-tRNA synthetase
|
Brevibacillus
|
MDYSKTLALPKTEFPMRGNLPSREPQMQAVWEEQNIYQQVLDRTKDRPSFVLHDGPPYANGDIHIGHALNKILKDFIVRYKSMAGFYAPYIPGWDTHGLPIEQAIINAQGLDRRSIEVNDFRQRCEEYAWSYIDKQRDQFKRLGVRGDWENPYVTLLPEYEANQIRVFGEMAKKGYIYKGLRCVYWSPSSETALADAEIEYKDKRSPSIYVSFQVADGKGKLDIETGVVIWTTTPWTLPANLAISLHPELEYNVVKVDGRKFLVANGLIEAASKEIGWEGVEILATFKGQELEGVETQHPFYDRKSPLILGEHVTLDAGTGCVHTAPGHGEDDFNVGQKYNLGVLCPVDHEGKMTNEAPGFEGLFYEDANKVITEKLKENGALLKLSFFTHSYPHDWRTKKPVIYRATEQWFASIDGFRTQMLEAIKNVKWIPHWGETRLANMIADRGDWCISRQRVWGVPIPIFYCKACNEPIINDTTINHVADLFRKEGSKVWFSREANELVPEGLSCTKCDCNDFRKETDIMDVWFDSGSSHQAVLRERGIAWPADMYLEGSDQYRGWFNSSLSTGVAVYGTAPYKSVLSHGFALDGEGRKMSKSLGNVIVPQQVIDKMGADILRLWVASVDYQADVRISDAILNQIAEVYRKIRNTFRFLLGNLDGFNPATDRVAYEELGELDRYVLAKAAKVAKRTRKAYDEYQFHTVFHAVHNFCVIDLSAFYLDICKDRLYVEAPDSLKRRAAQTVMYDCLLSLVKLVAPLLPHTADEVWAFIPGVEEKSVQLTDMPEGDEQHLSFAAEAESKWDAFLAIRDEVLKAMEEARRNKVFGNSVDAKLALYPQTEEVAKTLAAMDDLADLFIVAHVDVHSGSAPAEAVQLEGIAAVVSAADGGKCERCRVVKPDVGTRESHASLCVRCADVVEQHYAHVTE
|
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
|
C0ZG86
|
P40841
|
BR2EE_PELLE
|
Brevinin-2Ee
|
Pelophylax
|
GIFDKLKNFAKGVAQSLLNKASCKLSGQC
|
Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity.
|
P40841
|
A6VI43
|
COFH_METM7
|
FO synthase subunit 2
|
Methanococcus
|
MDFISFKEKEISKKECLELFENTENFFDVIKLADSLRKDIVGDAVTYVVNANINFTNICTGTCGFCAYKAEHGDPHAFFLNPDEVAKKALEARKIGATEVCIQGGLLKEIDTYFQAEILKKVKEITAPYGKIDVHAFSPMEVKSAAENAGLNVKEALKILKESGLNSMPGTAAEILNDEIRSEICPTKLKTSEWIDVVSNAHKTGIKTTCTMMYGHVEENDHLAEHLSILRNIQKETGGFTEFVPLTFLHENAPLYHTERVKSGASGMLDLKVYAISRIFFKDSIKNIQTSWVKLGTKLSQVSLNCGANDIGGTLMEENISKSAGGSYGTYMSEEQLKDMVLAVGRIPKQRNTAYEIIE
|
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.
|
A6VI43
|
A9VRF1
|
PURL_BACMK
|
Phosphoribosylformylglycinamidine synthase subunit II
|
Bacillus cereus group
|
MSLMLEPNPTQIKEERIYAEMGLTDEEFAMVEKILGRLPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTTGERVLQGPGEGAGIVDIGDNQAVVFKMESHNHPSAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSPRVKYLFEEVVAGIAGYGNCIGIPTVGGEVQFDPCYEGNPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEELSESSEAKRPAVQVGDPFMEKLLIEACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQERMLIVVKKGREQEIVDLFEKYGLAAVTMGKVTEDKMLRLFHKDEMVAEVPADALAEEAPIYHKPSKEAAYFAEFQQMKMETPKVEDYKETLLALLQQPTIASKEWVYDQYDYQVRTSTIVTPGSDAAVIRVRGTEKGLAMTTDCNSRYIYLDPEVGGKIAVAEAARNIVCSGGEPLAITDCLNFGNPEKPEIFWQIEKSVDGMSEACRKLQTPVIGGNVSMYNERSGEAVYPTPTVGMVGLVHDLKHVTTQEFKQAGDLVYVIGETKAEFGGSELQKMIYGKIFGQSPSIDLDVELKRQKQVLAAIQAGLVQSAHDVAEGGLAVAITESAIGAKGLGATVKLDGEATAVLFAESQSRFVITVKRENKEAFEKAVEAIQVGEVTNTNEVTIHNEENEVLLTANVDEMRKAWKGAIPCLLK
|
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
|
A9VRF1
|
Q9ZRW8
|
GSTUJ_ARATH
|
Glutathione S-transferase 8
|
Arabidopsis
|
MANEVILLDFWPSMFGMRTRIALREKGVEFEYREEDLRNKSPLLLQMNPIHKKIPVLIHNGKPVNESIIQVQYIDEVWSHKNPILPSDPYLRAQARFWADFIDKKLYDAQRKVWATKGEEQEAGKKDFIEILKTLESELGDKPYFSGDDFGYVDIALIGFYTWFPAYEKFANFSIESEVPKLIAWVKKCLQRESVAKSLPDPEKVTEFVSELRKKFVPE
|
Catalyzes the glutathionylation of 12-oxophytodienoate (OPDA). In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC), and glutathione peroxidase activity toward cumene hydroperoxide.
|
Q9ZRW8
|
B2K5J4
|
SUFS_YERPB
|
Selenocysteine reductase
|
Yersinia
|
MNFPIERVRADFPLLSRQVNGQPLVYLDSAASAQKPQAVIDKELHFYRDGYAAVHRGIHSLSAEATQQMEAVRTQVADFIHAASAEEIIFVRGTTEAINLVANSYGRHFLAAGDSIIITEMEHHANIVPWQMLAQDLGVEIRVWPLTATGELKITALAALIDDTTRLLAVTQVSNVLGTVNPIKDIVAQAKAAGLVVLVDGAQAVMHQPVDVQALGCDFYVFSGHKLYGPSGIGILYGKSALLQQMPPWEGGGAMIKTVSLTQGTTFADAPWRFEAGSPNTAGIMGLGAAIDYVTELGLLPIQQYEQSLMHYALAQLSQIKSLTLYGPTERAGVIAFNLGQHHAYDVGSFLDQYGIAIRTGHHCAMPLMAFYQVPSMCRASLALYNTREDVDRLVAGLQRIEKLLG
|
Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
|
B2K5J4
|
B8IH88
|
NDK_METNO
|
Nucleoside-2-P kinase
|
Methylobacterium
|
MAIERTFSILKPDATARNLTGAINAVIEEAGLRIVAQRRIRMSEAQAKTFYEVHAERPFYGELVSFMTSGPVVVQVLEGENAVAKYREVMGATNPAQAAEGTIRKKFALSVGENSVHGSDSAENAKVEIAQFFDEKDIVG
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
B8IH88
|
C5B9W5
|
DADA_EDWI9
|
D-amino acid dehydrogenase
|
Edwardsiella
|
MRVVILGSGVIGVTSAWYLAQAGHQVTVVDRQEGPGLETSAANAGQISPGYAAPWAAPGIPLKALKWLFQRHAPLAMSLDGSLFQLRWLWQMLRNCDSTHYAQNKARMVRLAEYSRDCLAQLRRTTTIDYEGRQLGTLQLFRTPQQYENAARDIAVLREAGVPYRLLPTAQLSTVEPALAVAGVRLSGGLHLPHDETGDCQLFTRHLAQQAAQSGVHFIFSTQVLRLLRSGARIQGVQCGHDTLVADAYVVALGAYSTGLLQDIVAIPVYPLKGYSLTLPIDDPDAAPRSTVLDESYKVAITRFDRRIRVGGMAEVVGFDMSLPLARRRTLERVVRDLYPRGGLLPQASFWSGLRPATPDGTPLVGATPLENLYLNTGHGTLGWTMACGSGQLLADIISGVTPTIRVDDLSVSRYTA
|
Oxidative deamination of D-amino acids.
|
C5B9W5
|
Q54C16
|
SGMB_DICDI
|
Acid sphingomyelinase B
|
Dictyostelium
|
MKVKAPILLLFVFLINFCFSIKQTQQQNFDITIDNNNYNNNNNNNKNEIINNNNKNNNNLNDEYFEKLGYDTNGTKCDICKFGINQVQKMIASKQGIEDISKYAIDLCTYLHIEKAEVCNGLIPLFANMTYNVLSYPTVTGEYVCGFVGFCPYVPRNSSNIINFPKPKPPHVPPVAPSPNSPTMKILHISDIHVDPVYESGMNADCGEPLCCRAPNGPGVGEKAAGEWGHYLCDINMKMVESMFEFIDQEFGEDIDIVFWTGDNPPHDIWEQTYDSQINASQLVTNLVKKYFGSTAKVFPAIGNHESLPVNSFPLPPGSSWIFNALSYDWSDWVNVDEQVANLQYGGYYTLPVQSGLRVISLNMNWCNNGNLYLAENSTDPANMLQWIVDTLQASEDIGEKVYLVGHIPPGIPDCIDSWSEQLLQIVNRYEDTILASFYGHTHRDEFSVYYTQSDENDPSSPMRASNVIYTTPSVTTYQHQNPSFRIFTVDSNTGYLMESSTYHTDLSQANLNGKPTWLLEYNTTNTYNIPNLTPISMDLAIQNINSSNSMLEDYHVHYYSASPYPESKPCTSISCKLDYICKMKSAAYLKYYECIHHEVNNYLLNESDDDSIKSHKKLNILLDLNNYLNNEVLKSC
|
Converts sphingomyelin to ceramide.
|
Q54C16
|
Q64NW2
|
CLPP_BACFR
|
Endopeptidase Clp
|
Bacteroides
|
MDDFRKYATKHLGMNAMVLDDVIKSQAGYLNPYILEERQLNVTQLDVFSRLMMDRIIFLGTQIDDYTANTLQAQLLYLDSVDPGKDISIYINSPGGSVYAGLGIYDTMQFISSDVATICTGMAASMASVLLVAGAKGKRSALPHSRVMIHQPMGGAQGQASDIEITAREIQKLKKELYTIIADHSGTSFDKVWADSDRDYWMTAQEAKEYGMIDEVLIKK
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
Q64NW2
|
Q67P86
|
IF2_SYMTH
|
Translation initiation factor IF-2
|
Symbiobacterium
|
MEPRLRVFELARELGVDSKRVLEVLQSLNVDVKNHMSTIDQKTAEKVTDAVRRTEAQEGQGAGKSAAKSAKPAAQPKPTREANPAKTSLLEDFFGSGTRPQRPLSEKRERRPLTERRPLAERRPLAERPLVDRPVTERPLAERPAAELRPGAAKAAAPARPAAEAQPVAERRAPAEAAQAAQAERRPAEKAQPAAAAKAAPPEKAGAAPVPGAVAEQKQAATPAAAEQKPAGKAEQTAGAAQAKPARAEAGTGASSRPASAAPAAQGEKRPAAAAERREEPQAEAPQTSGPSRPVPAGPGQPARPAGSGIGVPVKPAAGGKSGLGLPTRPGEKAADGARGGGSGIGLPVKPAAGQGTAARAGGLGLPQKPKAGAPRPGGGLGAPQRPGRRGAPLAIPKLDPKVAEQAKAGEGKPRYGQSGDKRRADLYDRREHPSSQPSEEKLFGQRPKRKASAQERRVLKPITVTGPMSVKDLAHEMGVTAAEVIKTLLTGFGIMATINQELDVDTCVLVASEFGVEATVEQKEDIIEVYDRVEDPDEPAELKKPRHPVVTIMGHVDHGKTSLLDAIRQAKVAAGEAGGITQHIGAYEVELNGRKITFLDTPGHEAFTAMRARGANVTDIAVLVVAADDSVMPQTVESINHAKAANVPILVAINKIDKPEANPQRVMQDLTQYGLVPEEWGGDTIMVPVSAKQKTNLDLLLENILVLAEVSDLKANPDKPAAGTILEAALDKARGPVATVLVQAGTLNTGDVFVAGTSWGRVRAMFDHRGRKLKSAGPSTPVRVLGFDSVPQAGDVFRVTPDEKTARAIAEKRIAKAQAERLAQKAISLDDFMNQVAQGEIKDLNVIVKADVQGSVEAIRGQLEKLRNEEVKVKVIHAGVGAISESDVMLAVASKAIIIGFNVRPDDRASRAADEHGIDVRTYSVIYDIVDDIEAAMKGMLKPKIEEVILGKAEVRETFKVPKVGMAAGCMVIQGKVTRNARYRLIRDGVVVWDGEINALRRFKDEVREVSEGYECGITLQNFHDFKRGDILEAYELQEIKAG
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
Q67P86
|
Q11UP4
|
MNMA_CYTH3
|
tRNA-specific 2-thiouridylase MnmA
|
Cytophaga
|
MSKKGRVLVAMSGGIDSSVAAVMLHEQGYEVIGMTMKTWDYANLGGSKKETGCCSLDSINDARNIAVSLGFPHYIVDIREEFGDYVINHFNKEYLDGRTPNPCVLCNTHIKWDSLLRRADKMDCDFIATGHYAQVRSENNRFVISKGLDENKDQSYALWGISQQSLSRTMFPLGHLHKTDIRAMAAERGFMDLVNKSESYEICFVPDNDYRGFLKRRNPGLEEEVRGGEFVMEDGTVVGKHEGYPFYTIGQRKGLGITLGYPVFVTEIQKENNRVVLGREEGLNRNGMWVDQLIMSKYENLKGIQKQSITKVRYNDDGTSSTIEQVGDEMRVLFHEHVKAIAPGQAAVFYEGNDVIGGGWIKSSFKQD
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
Q11UP4
|
Q3E7X8
|
YE077_YEAST
|
Y' element ATP-dependent helicase YEL077C
|
Saccharomyces
|
MTLGNSYDAFNHDPWMDVVGFEDPNQVTNRDISRIVLYSYMFLNTAKGCLVEYATFRQYMRELPKNAPQKLNFREMRQGLIALGRHCVGSRFETDLYESATSELMANHSVQTGRNIYGVDSFSLTSVSGTTATLLQERASERWIQWLGLESDYHCSFSSTRNAEDVVAGEAASSDHHQKISRVTRKRPREPKSTNDILVAGQKLFGSSFEFRDLHQLRLCYEIYMADTPSVAVQAPPGYGKTELFHLPLIALASKGDVKYVSFLFVPYTVLLANCMIRLGRCGCLNVAPVRNFIEEGYDGVTDLYVGIYDDLASTNFTDRIAAWENIVECTFRTNNVKLGYLIVDEFHNFETEVYRQSQFGGITNLDFDAFEKAIFLSGTAPEAVADAALQRIGLTGLAKKSMDINELKRSEDLSRGLSSYPTRMFNLIKEKSEVPLGHVHKIRKKVESQPEEALKLLLALFESEPESKAIVVASTTNEVEELACSWRKYFRVVWIHGKLDAAEKVSRTKEFVTDGNMRVLIGTKLVTEGIDIKQLMMVIMLDNRLNIIELIQGVGRLRDGGLCYLLSRKNSWAARNRKGELPPIKEGCITEQVREFYGLESKKGKKGQHVGCCGSRTDLSADTVELIERMDRLAEKQATASMSIVALPSNFQESNSSDRYRKYCSSDEDSNTCIHGSANASTNASTNAITTASTNVRTNATTNASTNATTNASTNATTNSSTNATTTASTNVRTSATTTASINVRTSATTTESTNSSTNATTTASINVRTSATTTKSINSSTNATITESTNSNTNATTTESTNSKTSATTTASTNSNTSATTTESTNSKTSATTTASTNSNTSATTTESTNSNTSATTTASTNSSTNATTTESTNASAKEDANKDGNAEDNRFHPVTDINKESYKRKGSQMVLLERKKLKAQFPNTSENMNVLQFLGFRSDEIKHLFLYGIDIYFCPEGVFTQYGLCKGCQKMFELCVCWAGQKVSYRRMAWEALAVERMLRNDEEYKEYLEDIEPYHGDPVGYLKYFSVKRREIYSQIQRNYAWYLAITRRRETISVLDSTRGKQGSQVFRMSGRQIKELYYKVWSNLRESKTEVLQYFLNWDEKKCQEEWEAKDDTVFVEALEKVGVFQRLRSMTSAGLQGPQYVKLQFSRHHRQLRSRYELSLGMHLRDQIALGVTPSKVPHWTAFLSMLIGLFYNKTFRQKLEYLLEQISEVWLLPHWLDLANVEVLAADNTKVPLYMLMVAVHKELDSDDVPDGRFDIILLCRDSSREVGE
|
Catalyzes DNA unwinding and is involved in telomerase-independent telomere maintenance.
|
Q3E7X8
|
O05073
|
VPI_HAEIN
|
Mu-like prophage FluMu I protein
|
Haemophilus
|
MKAEKTSLAVLTAQLTSPDGWQQLLPKGEFRSRDGSPTDVAHWFIDGTIAQNLIHKARQLNQDLLVDYDHETILKAKKGIDAGNVVAAGWFNADEIQWFDDETRQGLYIKPRWTPKAYQQIKDGEFAFLSAVFPYDENGTPLELRMAALTNDPGITGMQRLAVLSATLNPQENVKMPESLRKLLAKLGVEIAEGVELTEEQANTALNALETLQTDKTKADEQVATLSAKNTEVDLSQYVPKATYDAVMSQVAVLSAKTDDVEIDNHISKARNEGRAVEAEVEYLKQFGKQQGVAALSAMLEKRPQIAVLSAQQTQTTKVEKPVEKGTAVLSAADKEAAKLLGISEQDYAKELEAK
|
Potential protease involved in virion morphogenesis.
|
O05073
|
Q6KIL4
|
KTHY_MYCMO
|
dTMP kinase
|
Mesomycoplasma
|
MFISFEGIDGAGKSTIIKKLKRKLPKLYPDKKFVFTREPGGKKLKEAEKIRKILLDKKTNIDPMTETLLYAASRRVHLDSLIWPALKKGHIVISDRYVDSSYVYQGIARGLGVKVVKEINDIATSNFMPDYTFFLSISEEESIIRRHKRGKPDRLEMSSKDFFSRAYEGYFKIINSPTMADRFILVNAEENVGTILKNILNEFDKILKK
|
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
|
Q6KIL4
|
B4F0S0
|
SELA_PROMH
|
Selenocysteinyl-tRNA(Sec) synthase
|
Proteus
|
MTHDTRSLYSQLSSIDSLLHQADIQTLVDGYGQTFIVEHLRKLQEEARIIIRQNNQLPQWHDNWAEELKNRIALQRKAAIKPVFNLTGTVLHTNLGRALMAESAIEAVSQVMRSPATLEYSLDGASRGHRDRAIADLLCELTGAEDACIVNNNAAAVLLMLATVAPDKEVVVSRGELVEIGGAFRIPDVMCQAGCRLKEVGTTNRTHLKDYRNAINENTGLLMKVHTSNYSIQGFTAEVEGTQLAALGKEMNLPTAIDLGSGSMTNLAALGLPSEPMPQDYLQQGIDLVTFSGDKLLGGPQAGIILGKKAWIEAIQHHPLKRALRVDKMTLAALDATLRLYQQPEKMIKDIPTLRLLTRTQTEIHDMAQRLLPHFQAYYGDNYHITISSCASQIGSGSLPIESLPSAALTFAAKDGKGSQLDALAAHWRNLEKPIIGRITDGRLWLDLRCLEDENALIQALSL
|
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
|
B4F0S0
|
P68573
|
DBH2_BACSU
|
SPbeta prophage-derived DNA-binding protein HU 2
|
Bacillus
|
MNKTELIAKVAEKQGVSKKEGAPSVEKVFDTISEALKSGEKVSIPGFGTFEVRERAARKGRNPQTGEEIDIPATKAPAFKPAKALKDAVKAK
|
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
|
P68573
|
Q54EV7
|
XPO1_DICDI
|
Exportin-1
|
Dictyostelium
|
MENILNFNEPLDINLLDQIVSVLYNPLSNKNDIKAAQMVLGKFQEHPDAWSKVDTILETSKIVQTKFIALVIMDSLIKYRWKSLPREQCEGIKNYIVSLIIRLSSDPQTSSREKLLVNKLNLVFVQILKQEWTTNWSTFIPEIISSSKTNESLCENNMVILRLLSEEIFNFSEEQMTQTKIQTLKITFEKEFSLINDLCFYILENATRASLIKATLETLQRFLNWVPLHYIIEVNGGIAEPSKLVKLLLHKYFPEPLFRNSTLKCLTEIGNLNLGNQQYDAVFIAIIDKFMNQIKFIKPDPSKIPQDYEDGDQGERSFIHTVSLFLTGFFKSHLKIMENSLNIPYLTLAHEILVNISNIDELELFKICLEYWNFLSSNLYSDIATFTTTLLSTPPRLQLYKSVLSKVRVVLIDHMAKPEEVIVVEDENGNIVRETTKDTDSLTLYESMRETLIFLTHLDSENTQHIMLEKLQTLISGREFTFQRLNTLCWAIGSISGAQNKEQEKRFLVTVIKDLLELCQNKKGKDNKAVIASDIMYIVGQYPRFLKDHWKFLKTVVNKLFEFMHESHPGVQDMACDTFLKISKQCKRKFVVLQVEESQPFINELLNQLSTTIAHLEQSQIHTFYEAVGYMIASSSDAAFREKLVNKFMELPNHSWLQIMGAASVKVESLLTVEVARDILNLIKTNNRAAMSLENCYITQISKIYLDLLNVYRTYSDHISRNPNIYRETLGQAMRSVKKETLKLLETFIEKSSDKQVIYSNFLQPLLEAVLGDYRTNIPETRDPEVLSLMTAIITSLKQLVHPEVPKILEAVFETTLSMITKNFEDYPYHRINFFNLIRAINSNAFTVFHNLHPQQFKLLIDCVVWAFKHTERNISETGLHILKELIENVSKNSDVANVFFKTYLVSLLNDILYILTDSFHKSGFALECDILRMMFQVVENGVVKIPLFDPQQANFPSNSEYVKEIVVTFLSASPNVSRPQIQAFVTRLFNLANINNNDFKSATRDFLITLKEWKSHENADLYSDEKNIEKALALKKQSMIPGMVRPNDVNLEMNDL
|
Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES).
|
Q54EV7
|
A3QFJ6
|
ZIPA_SHELP
|
Cell division protein ZipA
|
Shewanella
|
MENLQLVLFVLGAVAIIAVLVHGFWSIRRQQPKSLKESPMTGLYTDKTRDSDGFDADGVGPVRVVKNNAEQGIPKATSTSRATPFGARAQESEPADVSPSFSLSDEPKQKAPRSRQEPVMSATPNEEVSDAHLEQMELGLGQAPAQPSLFEDPVTERKQEAVRPAPRVEAPQSVAPASVEPVSVEPEPAPKVAEETPLGDPQDVLVLHVVAKEGEALNGAELLPSLLTLNFKFGDMDIFHRHEDNAGTGKVLFSLANMVKPGVFNPDEMEQFTTQGIVLFMTLPCYGDPLMNFSIMLNSAHQLADDLGGEVLDGGRGAWSEQTKQSYLQRIRAQM
|
Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
|
A3QFJ6
|
Q88UX0
|
RS4_LACPL
|
30S ribosomal protein S4
|
Lactiplantibacillus
|
MSRYTGPSWKISRRLGMSLSGTGKELARRPYAPGDHGQGRRGKLSEYGTQLREKQKLRMMYGLTERQFANLFIKAGKIREGKHGVNFMILLERRLDNMVYRLGLATTRRQARQLVNHGHITVDGKRVDIPSYEVSVGQVVSVREKSKKLAVITGAVEAVVARPNFVQFDADKLEGSLTRLPEREELEADIDESLIVEYYNKL
|
With S5 and S12 plays an important role in translational accuracy.
|
Q88UX0
|
A7IFX6
|
RS12_XANP2
|
30S ribosomal protein S12
|
Xanthobacter
|
MPTINQLIRKPREAQKARDKAPALQASPQKRGVCTRVYTTTPKKPNSALRKVAKVRLTNSYEVIGYIPGEGHNLQEHSVVMIRGGRVKDLPGVRYHILRGVLDTQGVKNRKQRRSKYGAKRPK
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
A7IFX6
|
Q753F5
|
ENOPH_ASHGO
|
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
|
Eremothecium
|
MEEDYGVFILDVEGTVCPIAFVREQLFPYFLDKVEELINNADETERDLLADMQSRHGGAAAASLLRQLVAEDVKDPALKALQGRVWERGYASGEITAPVYADAVRFIQRNAGRVYIYSSGSVQAQRLLFGHVSNPSGDGVLDLTGHLAGFFDIPAAGRKTEAKSYERILAAIGLERQPGAAIFVSDSVAELDAASASGLSVRLAVRPGNERVSGARYTTLTDFEGL
|
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
|
Q753F5
|
Q6PCG6
|
VEZA_XENLA
|
Vezatin
|
Xenopus
|
MTAEFDEEVVFENSPLFQYLQDLGHTDFEICPLSKEEERLAENGQGKQDVHTTEKKSIISRTVEFLKSWSPFLSKKKKDEKIHLLEIGFRLESLRTILQQEVLIQEDVELIELLDPGILSAGQTQNQQNDHLPTLWSIATPNIWETSILFVFLSAVAAFQSWSISSSLIWGPSLILFAAFTVLKTLHTWRSARLRIILRKYCTQVEGTVSNSRAFTNLVRKALRLIQETEVISRGFTLVSAACPYGKAGQHASQHLLGLRKAVYRTVRTNFRISRLATLYMLKHYPLNSEIDNVTNYICVVPLKDLGLGLCEEHVSEEDAHNLTDAFSLPALKVLFQLWIGQSSEFFRRLALLLSPENASQGPSTSPEQLPHFIWSDVVQDLPHTQAACMAELKRSYEFYRYFETQHQSGLERTAKRKEVGELNNLHGAVRSLQLHLKALLNEVIVLEDELDKLSSCKEMQAVTPEASLMLEEKLRIIQPHVQASNTCWEEALCQVERMVRKPTTKKDTGKYSCENLNYPVVSNVPPAMRIEDRDPVPEEQILEAYVEEAVTDQEFNSEEIYLFSPEERERQKREREESRRVLQELKAVLGLKASEAERQKWKQLLFSEHAVITPLLPEEPVGHFEPLLSIYPEEPHKNLGFYGEIPSEINGTEHVKDAPIQVDHGNMNHEDEAKICPVSEEVEPASCKEEEDETPCPAPRTVLPPAIKERLARIHQSSDLNFTSGLATQVAARSLTFTFLQEQTFGDEWDDDDDNEDHDHDKERNNDSSQLEG
|
Plays a pivotal role in the establishment of adherens junctions and their maintenance in adult life.
|
Q6PCG6
|
Q87WQ5
|
IF2_PSESM
|
Translation initiation factor IF-2
|
Pseudomonas
|
MTQVTVKELAKVVDTPVERLLQQMREAGLPHTAAEQVVTDNEKQALLTHLKSGHKAKVEEPRKITLQRKTTSTLRVAGSKSISVEVRKKKVFVQRSPEEIEAERKREMDERRAVENAARQKAEEEAKRRAEEDARNQPAAGQPASAPAQPVAAAEPVREAPAAAAPAPASAAPSADARKRDEQRRPDKPRADDRNARGGDGDRKNAPHRASVKEKAPAPRVAPRTTDEESDSFRRGGRGKGKLKKRNAHGFQSPTGPVIRDVAIGETITVGELSAQMSVKAAEVIKFMFKMGTPVTINQVLDQETAQLIAEELGHKVTLVSDNALEDSLAESLKFEGESFSRAPVVTVMGHVDHGKTSLLDYIRRAKVAAGEAGGITQHIGAYHVETERGMVTFLDTPGHAAFTAMRARGAKATDIVILVVAADDGVMPQTIEAVQHAVAAGVPLVVAVNKIDKPGADLDRIRSELSVHGVTSEEWGGDTPFVSVSAKMGTGVDELLEAVLLQAEVLELKATPSAPGRGVVVESRLDKGRGPVATVLVQDGTLRQGDMVLVGSNFGRIRAMLDENGKPVKEAGPSIPVEILGLDGTPDAGDEMSVLSDEKKAREVALFRQGKFREVKLARAHAGKLENIFENMGQAEKKTLNIVLKSDVRGSLEALNGALNGLGNDEVQVRVVGGGVGGITESDANLALASNAVLFGFNVRADAGARKIVEQEGLDMRYYNVIYDIIEDVKKALTGMLGSDVRENILGIAEVRDVFRSPKFGAIAGCMVLEGTVYRNRPIRVLREDIVIFEGELESLRRFKDDAADVRAGMECGIGVKSYNDVKVGDKIEVFEKVQVARSL
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
Q87WQ5
|
Q5SJ65
|
UDGB_THET8
|
Uracil/hypoxanthine/xanthine DNA glycosylase
|
Thermus
|
MDREAFVQTLTACRLCPRLVAWREEVVGRKRAFRGEPYWARPVPGFGDPEARILLFGLAPGAHGSNRTGRPFTGDASGAFLYPLLHEAGLSSKPESLPGDDLRLYGVYLTAAVRCAPPKNKPTPEELRACARWTEVELGLLPEVRVYVALGRIALEALLAHFGLRKSAHPFRHGAHYPLPGGRHLLASYHVSRQNTQTGRLTREMFLEVLMEAKRLAGL
|
DNA glycosylase with broad substrate specificity. Can remove uracil from double-stranded DNA containing either a U/G, U/A, U/C or U/T base pair . Can also excise hypoxanthine from double-stranded DNA containing G/I, T/I, and A/I base pairs, xanthine from both double-stranded and single stranded DNA, thymine from G/T mismatched DNA, 5'-hydroxymethyluracil and 5'-fluorouracil .
|
Q5SJ65
|
Q1CV79
|
GLMM_HELPH
|
Phosphoglucosamine mutase
|
Helicobacter
|
MKIFGTDGVRGKAGVKLTPMFVMRLGIAAGLYFKKHSQTNKILIGKDTRKSGYMVENALVSALTSIGYNVIQIGPMPTPAIAFLTEDMRCDAGIMISASHNPFEDNGIKFFNSYGYKLKEEEEKAIEEIFHDEGLLHSSYKVGESVGSAKRIDDVIGRYIVHLKHSFPKHLNLQSLRIVLDTANGAAYKVAPVVFSELGADVLVINDEPNGCNINEQCGALHPNQLSQEVKKYRADLGFAFDGDADRLVVVDNLGNIVHGDKLLGVLGVYQKSKNALSSQAIVATNMSNLALKEYLKSQDLELKHCAIGDKFVSECMRLNKANFGGEQSGHIIFSDYAKTGDGLVCALQVSALVLESKQVSSVALNPFELYPQNLVNLNVQKKPPLESLKGYSALLKELDQLEIRHLIRYSGTENKLRILLEAKDEKLLESKMQELKEFFEGHLC
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
Q1CV79
|
A9WNI9
|
NB_RENSM
|
Ferric nitrobindin
|
Renibacterium
|
MPVEIPRDLTPELVPLSWLLGQWEGQGRLGTGEAESEHFFQRVTFSSNGLPYLEYVAESWLTDEEGMKLRPLSVEMGFWALDRKLGEADGGPGLIPADIVPALTTADDVEKLRNDTSGFDITATIVHPGGISELYYGTIKGPQIELSTDAVMRGAGAKDYSAATRIFGLVNGDLFWRWDVAAEGNSLEAHASAILKKTAAPESAEQRPSE
|
Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo.
|
A9WNI9
|
B9JTR0
|
LDH_AGRVS
|
L-lactate dehydrogenase
|
Agrobacterium
|
MKVGIVGAGMVGSASAYALTMLGIASEIVLVDYNTDLAQAQAEDISHAVPFVSATLVRAGDYGDFAGAGVVIISAGVSQKRGETRLELLGRNAEVFRQVVDQVLAAAPNAILLIASNPVDIMTDIATRLSGLAPQRVIGSGTILDTARFRSLLGRYLEISPQSVHAYVLGEHGDSEVLAWSNAMVGAVPLMSFAKQAGKPVTDTVRSEIDAGVRHAADKIIKGKGATYYGIGAGLARIVKAIASDQRDVLSVSSVTAELAGVTNVAASVPRVIGSSGILMDLVPDLDETERIALAKSARMLKDLALSVPC
|
Catalyzes the conversion of lactate to pyruvate.
|
B9JTR0
|
Q703W7
|
GLCDH_THETK
|
Glucose 1-dehydrogenase
|
Thermoproteus
|
MRAVTVTPGVPESLRLREVPEPKPGPGQVLLKPLLVGVCGTDKEIIEGRYGKAPEGSDYLILGHEALAEVAALGKGVDNVSEGDLVVPTVRRPLDCQLPVDYCPPGKYLEHGIWGLHGHAAELSITDAAYLVKVPKELRDIAVLTEPLSVVEKGVELGVESYKARLGSPPKTALVLGAGPVGLLASMVLRLMGVSITAVATRPHDSLKARLVEELGGRYIDAVHERLEGEFDLVIEATGAPSLAVQGLERLAPGGVEVLLGVYPPTGELKGLGSLLTDAVLKNKLVVGSVNAGLRHFERALAHLKEANDSLNGFPKRLITKVVPLERYQEAYVWTHDDIKVVLQVQT
|
Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. To a lesser extent, is also active with xylose as substrate, but mannose, arabinose, galactose, fructose 6-phosphate, glucose 6-phosphate, glycerinaldehyde 3-phosphate, ribose, sorbitol, ethanol, erythritol, or lactose are not oxidized by the enzyme. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NADP(+). Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway.
|
Q703W7
|
Q3SWX9
|
RAD21_BOVIN
|
64-kDa carboxy-terminal product
|
Bos
|
MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLASTGASNLLLEPEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPREDQQQQHQQRDVIDEPILEEPSRLQESMETSRTNLDESAMPPPPPQGVKRKAGQIDPEPMIPPQQAEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEDDEEEEDEDASGGDQDQEERRWNKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEPYSDIIATPGPRFHII
|
May promote apoptosis.
|
Q3SWX9
|
Q39I40
|
PDXY_BURL3
|
Pyridoxal kinase PdxY
|
Burkholderia cepacia complex
|
MKNVLSIQSHVIYGHAGNSAAVFPMQRLGINVWPLNTVQLSNHMQYGHWAGSAIDAAKMEQLVDGIAAIGALKRCDAVLSGFLGSPPQARAAVEIVRSVKAMNPNAWYFCDPAMGQTGGIRPEPGVEEFMVQEMPALADGMSPNHTELQKLAGRRIETVAEAVEACRALIRRGPQIILVKHLHDRNSPADRFNMLAVTETEAWIGQRPLYAFPRHPVGVGDLTSAIFVACRLRGDSVRAAFEHTLAAVHAVVKATYDARRYELELVAAQDEIARPSEWFGAWVTDA
|
Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
|
Q39I40
|
A0AFA6
|
RLMH_LISW6
|
rRNA (pseudouridine-N3-)-methyltransferase RlmH
|
Listeria
|
MNIQIITVGKLKEKYLVQGIAEYLKRLTAYAKVTIVEVPDEKAPEVLSDAEMKQVKDKEGVRILAKIPDDTHVIALAIDGKMKSSEEFAADLDKLATYGKSKVAFVIGGSLGLSESVLKRSDEQISFGRLTLPHQLMRLVLVEQVYRAFRIVRGEPYHK
|
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
|
A0AFA6
|
B1XYE7
|
GLYA_LEPCP
|
Serine hydroxymethyltransferase
|
Leptothrix
|
MFDRATQTLAAIDPEITAAIDAEVRRQEEHIELIASENYTSPAVMAAQGSQLTNKYAEGYPGKRYYGGCEHVDVVEQLAIDRAKQLFGAQNANVQPNSGSQANQAVFFGLLQPGDTIMGLSLAEGGHLTHGMPLNMSGKWFKVVSYGLDAQEDIDYDAMERLAHEHKPKLIIAGASAFALRIDFERFAKVAKAVGAYFMVDMAHYAGLIAAGVYPNPVPFADVVTTTTHKTLRGPRGGLILMTDAVAKQINSAIFPGIQGGPLMHVIAGKAVAFQEALQPEFKAYQEQVVKNATAMAETLTARGLRIVSGRTESHVMLVDLRPKGITGKEAEALLGRAHITCNKNGIPNDPQKPMVTSGIRLGSPAMTTRGFKEEQAVLTANLIADVLEAPNDEAVLERVRAQVAQLTRDFPVYR
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
B1XYE7
|
Q6CUQ5
|
CWC25_KLULA
|
Pre-mRNA-splicing factor CWC25
|
Kluyveromyces
|
MSDLNLLKSWNPKLVKNRKKVWEAQQQLVEENKKIKERQKEIEKERELDRYSSLIRDEDQKNVKRKTGLEWMYDNTSTALTENVDYLLGKKEITDTLLDLSGNNNKSEKSENQKQTIRKHYQGIEDVICSKTNHKNVDLSSDDPMAKFKAAKQAHLKTLKQNIQPTSHEYPVHKPLRGANSKRYDSGNGSRSNYKNSRYNNKYYRS
|
Involved in pre-mRNA splicing.
|
Q6CUQ5
|
Q6F9J2
|
PQQB_ACIAD
|
Pyrroloquinoline quinone biosynthesis protein B
|
Acinetobacter
|
MLIKILGSAAGGGFPQWNCNCENCLGLKQGTIQAKARTQSSIAISDNGKDWILCNASPDIAQQIAHNPELQAPSSIRRGTSIGSIILTDSQIDHTTGLLNLREGCPHQVWATPEVHEDLSTGFPIFNMLKHWNGGLVHHPIDIQTSFQVAVCEAIRFTPVPILSNAPPYSPYRHRPLPGHNIALWIEDTRTGHSLFYAPGLGQMDDSILSYMQRADCLLVDGTLWKDQELALLGVGKNTGQDMGHLALQEERGLIHLLSQFPKQRKVLIHINNTNPILNEDSVERATLKQLEIEVSYDGMLIEV
|
May be involved in the transport of PQQ or its precursor to the periplasm, in association with PQQ biosynthesis, but is not absolutely required for this synthesis.
|
Q6F9J2
|
A7FMW4
|
PRIB_YERP3
|
Primosomal replication protein N
|
Yersinia
|
MTTNRLVLSGTVCKTPVRKVSPSGIPHCQFVLEHRSTQQEAGFSRQTWCRMPIVVSGQQSQALTHSITVGSQLTVEGFISCHQGRNGLNKLVLHAEQIEFIDSGD
|
Binds single-stranded DNA at the primosome assembly site (PAS).
|
A7FMW4
|
Q04LD5
|
RLMN_STRP2
|
tRNA m2A37 methyltransferase
|
Streptococcus
|
MKPSIHSLAHQTMQEWVLEQGEKKFRADQIWEWLYRKRVQSFEEMTNLSKDLIAKLNDQFVVNPLKQRIVQESADGTVKYLFELPDGMLIETVLMRQHYGLSVCVTTQVDCNIGCTFCASDLIKKQRDLNNGEIVAQIMLVQKYFAERGQDERVSHIVVMGIGEPFDNYNNVLNFVCTINDDKGMAIGARHITVSTSGLAHKIRNFADEGVQVNLAVSLHAPNNELRSSIMKINRAFPIEKLFAAIEYYIETTNRRVTFEYIMLNEVNDSVEQALELAELLKNIKKLSYVNLIPYNPVSEHDQYSRSPKERVLAFYDTLKKKGGNCVVRQEYGTDIDAACGQLRSNTMKRDRQKAVAEVNP
|
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
|
Q04LD5
|
P07124
|
PYS1_NOSS1
|
Rod-capping linker protein
|
Nostoc
|
MFGQTTLGAGSVSSSASRVFRYEVVGLRQSSETDKNKYNIRNSGSVFITVPYSRMNEEYQRITRLGGKIVKIEQLVSAEA
|
Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
|
P07124
|
Q5M583
|
FOLD_STRT2
|
Methenyltetrahydrofolate cyclohydrolase
|
Streptococcus
|
MAIIMDGKALAVNMQEQLQEKVARLKEKEWIVPGLVVIMVGENPASQVYVRNKERAAKKAGFHSKTVNLSESISEEELIEVIEKYNQDPLFHGILVQLPLPNHISEMRILLAIDPKKDVDGFHPMNTGNLWNGRPQMVPCTPAGIMEILREYNVELEGKTAVIIGRSNIVGKPMAQLLLEKNATVTLTHSRTPHLAKVCNKADVLIVAIGRAKFVTEEFVKEGAVVIDVGINRDEEGKLCGDVDFDQVKEKVSMITPVPGGVGPMTITMLMEQTYQAALRSLKG
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
Q5M583
|
P0DUL7
|
HKM9_ASPHA
|
Hancockiamides biosynthesis cluster protein 9
|
Aspergillus
|
MPATTRLITIYGATGNQGGGVARSLLKNPCFQVRALTRNPNSPASQELAGLGAEIRRADGFDSNSLLAAFEGSWGVFVNINSDDKAFRPAGPTEYDLGMKIVDMAAQAGVQHFVFSSGPSSTELTNGKIRMKAMEMKNKIERYARNNTQFQTVSFICAAWYLENFLVKEIAPLFGGFPFVADAEAFLTFRCPRWGGKEDVPFISISDDYGDIVQGLFLDPHRWNGHVVHGCSDILTFDELVTHFQNVTGQKARFQPLESWETFDTFGVPELEDTKLMFGLTQTTGGLYFGPEPSEKNTAAALKRATAAALGLPRDQQTLITVKGWFQKHFPVTPN
|
NmrA-like family domain-containing oxidoreductase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable). Xenocockiamide A is then converted to hancockiamide D via a series of hydroxylations and O-methylations (Probable). The tyrosinase hkm6 may catalyze an aromatic hydroxylation, then the 2-oxoglutarate-dependent Fe(II) dioxygenase hkm4 and the FAD-dependent phenol hydroxylase hkm7 may catalyze consecutive hydroxylations to install 2 more hydroxy groups, and the methyltransferase hkm8 probably catalyzes two methylations using 2 molecules of S-adenosyl-L-methionine (SAM) (Probable). The NRPS hkm11 activates and transfers trans-cinnamate supplied by the PAL hkm12 to hancockiamide D and produces hancockiamide A . NRPS Hkm11 has the flexibility to tolerate the bulky hancockiamide G as a substrate and the absence of the acetyl-transferase hkm3 opens up the opportunity for hkm11 to introduce a second N-cinnamoyl moiety . The cytochrome P450 monooxygenase hkm5 catalyzes the methylenedioxy bridge formation, converting hancockiamide A into hancockiamide G . Hkm5 can also convert hancockiamide B into hancockiamide C, and hancockiamide D into hancockiamide H . The N-acetyltransferase hkm3 finally transfers an acetyl group to 1-N of piperazine, converting hancockiamide A into hancockiamide B and hancockiamide G into hancockiamide C .
|
P0DUL7
|
G5EBD7
|
6PGDH_GLUOX
|
6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating
|
Gluconobacter
|
MRIGIIGLGRMGGNIAVRLTRHGHDVVVHDRTSEVTTSVVGRCEAGRATPADTLADMAKLLEGDEHRVVWVMLPAGAITEDCVQQLGGLLGRGDIIIDGGNTYYKDDVRRSAELAEKGISYVDVGTSGGVWGLERGYCMMFGGTKETAEYIDPILSALAPGIGDVPRTPGRDEAGHDPRAEQGYLHCGPAGSGHFVKMVHNGIEYGMMQAFAEGFDIMKSKNSPILAEKDRFELNMGDIAEVWRRGSVVSSWLLDLTAEALTRSETLNEFSGEVADSGEGRWTIEAAIEEDVPAPVMTAALFTRFRSRSGNNFAEKILSAQRFGFGGHVEKK
|
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NAD to NADH.
|
G5EBD7
|
Q9CBY4
|
CLPP2_MYCLE
|
Endopeptidase Clp 2
|
Mycobacterium
|
MKLQNSQLQPQARYILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLESLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAVLLAAGTPGKRMALPNARVLIHQPSLAGVIQGQFSDLEIQAAEIERMRTLMETTLSRHTGKDAAVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLSAQTV
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
Q9CBY4
|
P37702
|
BGL38_ARATH
|
Thioglucosidase 1
|
Arabidopsis
|
MKLLMLAFVFLLALATCKGDEFVCEENEPFTCNQTKLFNSGNFEKGFIFGVASSAYQVEGGRGRGLNVWDSFTHRFPEKGGADLGNGDTTCDSYTLWQKDIDVMDELNSTGYRFSIAWSRLLPKGKRSRGVNPGAIKYYNGLIDGLVAKNMTPFVTLFHWDLPQTLQDEYNGFLNKTIVDDFKDYADLCFELFGDRVKNWITINQLYTVPTRGYALGTDAPGRCSPKIDVRCPGGNSSTEPYIVAHNQLLAHAAAVDVYRTKYKDDQKGMIGPVMITRWFLPFDHSQESKDATERAKIFFHGWFMGPLTEGKYPDIMREYVGDRLPEFSETEAALVKGSYDFLGLNYYVTQYAQNNQTIVPSDVHTALMDSRTTLTSKNATGHAPGPPFNAASYYYPKGIYYVMDYFKTTYGDPLIYVTENGFSTPGDEDFEKATADYKRIDYLCSHLCFLSKVIKEKNVNVKGYFAWSLGDNYEFCNGFTVRFGLSYVDFANITGDRDLKASGKWFQKFINVTDEDSTNQDLLRSSVSSKNRDRKSLADA
|
Degradation of glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones. These toxic degradation products can deter insect herbivores. Seems to function in abscisic acid (ABA) and methyl jasmonate (MeJA) signaling in guard cells. Functionally redundant with TGG2. Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl beta-D-glucoside.
|
P37702
|
Q2NQZ3
|
STHA_SODGM
|
NAD(P)(+) transhydrogenase [B-specific]
|
Sodalis
|
MQPKYDYDAIIIGSGPGGEGAAMGLTKRGARVAIIERYDNVGGGCTHWGTIPSKALRQAVSRIIEINQSPLHGNTRLPHTGFSDILCHADQVINQQTHMRQGFYERNHCQIFTGEASFVDEHQVQIHYGDNTTETLSAENIVIACGSRPYQPQDVDFDHPRIYDSDSILDLKHDPHHVIIYGAGVIGCEYASIFRGMNVKVDLINTRDRLLAFLDQEMSDALSYHFWENGVVIRHNEEYEEIKGLDDGVEVRFRSGKRMKADCLLYANGRTGNTDTLKLDKVELEADSRGLIKVNSMYQTAARHIYAVGDVIGYPSLASAAYDQGRIAAQVIIKGQANVQLIENIPTGIYTIPEISSVGKTEQELTAMKVPYEVGRAQFKHLARAQIVGMNVGSLKLLFHRETKQILGIHCFGERAAEIIHIGQAIMEQKGEGNTIEYFVNTTFNYPTMAEAYRVAALNGLNRLF
|
Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
|
Q2NQZ3
|
O74547
|
BIT61_SCHPO
|
Target of rapamycin complex 2 subunit bit61
|
Schizosaccharomyces
|
MVGRGSFSSTSSASSINWIPKNTKTSIESVSNTISLSENGQNQDLETVTTKESNVGDSDTTENIKSPFNGQWPFSRRSSQSSSHPVFEETHWSKHSKRPGKLNVLTPTSPSNVNAEVQSISTKTQLSLLNLSPHKHKKPKDGLDLSALQKTLNGSRNFLRGRRDAGGIFGASIPQSLVTNQIINGFGAASLAFAKLGKVRSPLEGRFNLVPISADETWLIVESEVCSLYSGEALHYSLEDLNGILILHLQALIRDTKMNEFVGHLETLFRKATKCLSDSLSPVPEELFLNRIIETWLFFFSSVLPYVQGVFLPIKTKLFDEQEKTQLPYEVNEFCSTNREKLNVHRLALMTFRDYMVLPIANRIQICIGRAESAENALDNAGEVFARLFQILSLLASVRTNDSKEQEITNLATKVRCLLIAS
|
Component of TORC2, which regulates multiple cellular processes to control cell growth in response to environmental signals. TORC2 is required for cell survival under various stress conditions. TORC2 positively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Positively regulates amino acid uptake through the control of expression of amino acid permeases.
|
O74547
|
P11638
|
QA1F_NEUCR
|
Quinic acid utilization activator
|
Neurospora
|
MPPKRKTLNAAAEANAHADGHADGNADGHVANTAASSNNARFADLTNIDTPGLGPTTTTLLVEPARSKRQRVSRACDQCRAAREKCDGIQPACFPCVSQGRSCTYQASPKKRGVQTGYIRTLELALAWMFENVARSEDALHNLLVRDAGQGSALLVGKDSPAAERLHARWATSRVNKSITRLLSGQAAQDPSEDGQSPSEDINVQDAGAKTSDFPHAPHLTFSAPKSSTAETRTLPGPVRPPISANTLENNLQPDGTGIGKLPPNHWRLLDIYFSYTHSWLPILEKKDMYQALYQYSEQGSLLPSANVESGVHAELWSALALASFQAAATAASSATGPASAAHGHDNAINPSPADISDTARKLIPLESGPFQVQHCRALLLLCLVSLGRDDWESAWLLVGFAVRVLLVVRTQLPPDDDRPRPRMRALLVACFIVDTIVSMRHNVPAHLKPDDIADLPLPEDGQDQWEPWTPCEGLGGEHTMLQMLRNPAYPLSTFNHLYGVTKLVALELLPRIRTSSQNAPLEFRSRLQQVIGHNSPFSVFVLSQDTASAFVPTAYLTRTVYLWAAAFSEPLNEHYSHLLIETLDQYQKRFGTYAIPPLIPSLLDSLLALKKQSHSSERHRRHLEELFPAYSSIWPRGGRHSNTGLQPIRQLELPPTATATASIMPHVMEQPLSTSINPVNDRFNGIPNPTPYNSDAALDAITQTNDYGSVNTHGILSTYPPPATHLNEASVALAPGGAPPRPPPPYVDSTTNHPPYHSNLVPMANFGYSTVDYDAMVDDLASIEYTDAVDVDPQFMTNLGFVPGCNFSDISTYEQ
|
Transcription activation of genes for enzymes and proteins of quinate metabolism by binding to a 16 base-pair sequence (consensus 5'-GGRTAARYRYTTAYCC-3') in front of each Qa genes.
|
P11638
|
P0CR07
|
DBP10_CRYNB
|
ATP-dependent RNA helicase DBP10
|
Cryptococcus neoformans species complex
|
MAAITPSWALETTADGEVKEKTSGPGGQWRALNVGPDLIRSLLIRKFKTPTPIQRAAIPPALSTPPRDILGMARTGSGKTLAYLIPLLQRTGSTHHGQGPRALILCPSRELAVQIYTVGKDLARGMNKGKGKGKNKNEDEEDEEGKGKEGLRWALIIGGEGMDAQFEKMSSNPDIVIATPGRFLHLIVEMHMDLRHLQTVIYDEADRLFEMGFDVQLQEILHRLPSTRQNLLFSATLPSSVAEFAKAGLVNPLLVRLDAEQKISPDLALKFFSVKPGEKEASLLVLLREVIGKPNQPEPADPSSAPQAIVFVATKHHVDYVAELLRTTGYRTSLIYSSLDQVARQQQLAGFRSHQSDVLVVTDVAARGLDIPIMDHVINYDFPAGPRIFVHRVGRTARAGRKGTAYSLIVKEDFPYLCDLHTFLGTERMGEPADVLRSLPIEQLSENVEYVFHNLDETAPHITALRNVMRKGQGMFERSRTKANPTSYRQAKSLASALSNNPPRIDDMFEDAMEVEVNEEKARLLAKVAAFTPSETVFEVGKRESESAIIMKKRRKTVDERQKRVSKAEAEKSTASGMEKAPVKELPAPQLPSKNFKDPSFYLDHTQRGAEAEKGYSLKSGVESLSGAITDMTADEGTGPKAQKASQLSWDRKKHKFIKKNGSADGEKMIKSESGALLPASYSSGKYQEWKSKRRHMPDGPVEALALGGGRRGRHGPPGQKRKAEDGDGGEDAGGKGRKDQGKSKGTGKGKDDFKQKSPGKPGKKGIKQSSGLKSAMDIRKQREIAQKRKEKNARKPQKFRK
|
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
|
P0CR07
|
B8ZUB2
|
PXPA_MYCLB
|
5-oxoprolinase (ATP-hydrolyzing) subunit A
|
Mycobacterium
|
MACIDLNADLGEGFGVWRLGDDEAMLRIVTSANVACGFHAGDPAGLLRVCRLAAERGVRIGAQVSYRDLVGFGRRFIDVTADDLLADVVYQIGALQAIAQTAGSAVSYVKPHGALYNTIVTNREQGAAVAAAIQLVDSTLPVLGLAGSTFFDEAARIGLRTVAEAFADRTYRPDGQLISRREPGAVLHDPAVIAQRVVTMVTTGKATAVDGTQLAVTVESICLHGDSPNAIQMATAVRDQLNAAGIDIRAFC
|
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
|
B8ZUB2
|
Q8BX43
|
TR19L_MOUSE
|
Tumor necrosis factor receptor superfamily member 19L
|
Mus
|
MSLQGLMMKRTLLCWPLSCLFVLLPWPLATPTPITPWLCPPGKEPDPDPGQGTLCRTCPPGTFSASWNSYPCQPHYRCSLQKRLEAQAGTATHDTMCGDCQHGWFGPQGVPHVPCQPCSKAPPSTGGCDESGRRGRRGVEVAAGTSSNGEPRQPGNGTRAGGPEETAAQYAVIAIVPVFCLMGLLGILVCNLLKRKGYHCTAQKEVGPSPGGGGSGINPAYRTEDANEDTIGVLVRLITEKKENAAALEELLKEYHSKQLVQTSHRPVPRLLPASPSIPHICPHHHHLHTVQGLASLSGPCCSRCSQKWPEVLLSPEAAAATTPAPTLLPTASRAPKASAKPGRQGEITILSVGRFRVARIPEQRTSSLLSEVKTITEAGPSEGDLPDSPQPGLPPEQRALLGSGGSHTKWLKPPAENKAEENRYVVRLSESNLVI
|
May play a role in apoptosis. Induces activation of MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed. Involved in dental enamel formation .
|
Q8BX43
|
Q89AE7
|
OBG_BUCBP
|
GTP-binding protein Obg
|
Buchnera
|
MKFLDKAIIHVIAGNGGHGRTSFRREKYIPKGGPDGGDGGNGGNVWLQTVTNLNTLIDFKFTKIFKAQDGQQGFNKKKTGKKGSDIVIQIPIGTKIIDHNTNEIIEDMIQDKQLVLVAKGGWHGLGNTRFKSSTNRIPIKHTKGTQGEFRILRLELILIAHVGTLGLPNSGKSTLVRNISNAKTKIANYPFTTLKPVLGTVKINHKEFFVIADIPGLIQGASHGIGLGYQFLKHLERCHLLLHIIDISQINFKNTITNIHVILDELKTYNKILHNKPIWFVFNKIDLIDDIDINTKLKSILEKLGSIQQYFLISAIKKTGLKKIVKKIYDFLKNKNLL
|
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
|
Q89AE7
|
Q1WSN8
|
KUP_LIGS1
|
Probable potassium transport system protein kup
|
Ligilactobacillus
|
MKVKRKIFWGALITLGIVYGDIGTSPLYVMKALIMDAGGLNGLTEDYIIGCLSLVFWTLMLMTTIKYVLIALRADNHGEGGIFALYALVRNKKKWLILPALLGGAALLADGTLTPAVTVTSAIEGLKGISIGSQPWINTQLEVNLVTFVILLVLFLIQRFGTSFIGKAFGPLMLLWFSFLAIFGIVNLIHEPLVLRALSPHYGLMLLFSPANKVGIFILGSVFLATTGAEALYSDMGHVGKRSIYLTWPFVCGALVLNYFGQGAYLIKNLGNFKTTGDIFNPFYEMLPSSVYLFGVLISTIAAIIASQALITGSFTLVEEAVGLKLLPKMKVEHPSLSRGQIYIRTINWSLCICTLLVLVYFRTSERMEAAYGLAITITMLMTTILLSQYLKDKVNVVFNGIFLAVFLSVELIFLISSLTKFTHGGYVTLLITLLILLIMVIWYFGNKLRDYLSDEEEWVSLRDYKDVLQELSNDDRIPLYISNLVMLTKVDKRTYKVKRETLYSILDKSPKKAKVYWFVTVNTTSDPYTNYYTVDMMGTRNIVNLQLYLGFKMDHRVNLYLRQVVEDLIENDIIDEQPQKYTTMPGRKIGDFRFIIIQELLSPNTRVRGWQHLLISARIFIQNHSTNPIQWFGLEFSEVKVEKVPLLLKKRRIPAMEQRMILNPKDVKRSTKE
|
Transport of potassium into the cell.
|
Q1WSN8
|
Q9KSE5
|
BSR_VIBCH
|
Broad spectrum racemase
|
Vibrio
|
MHFKATLLSLSIAATLPSFSLSAAPLHIDTALPDAAQIQQSNSWLEISLGQFQSNIEQFKSHMNANTKICAIMKADAYGNGIRGLMPTIIAQGIPCVGVASNAEARAVRESGFKGELIRVRSASLSEMSSALDLNIEELIGTHQQALDLAELAKQSGKTLKVHIALNDGGMGRNGIDMTTEAGKKEAVSIATQPSLSVVGIMTHFPNYNADEVRAKLAQFKESSTWLMQQANLKREEITLHVANSYTALNVPEAQLDMVRPGGVLFGDLPTNPEYPSIVSFKTRVSSLHHLPKDSTVGYDSTFTTSRDSVLANLPVGYSDGYPRKMGNKAEVLINGQRAKVVGVTSMNTTVVDVTEIKGVLPGQEVVLFGQQQKQSIAVSEMENNAELIFPELYTLWGTSNPRFYVK
|
Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes ten of the 19 natural chiral amino acids known, including both non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino acids (His, Lys and Arg). Among these substrates, is the most efficient with lysine and arginine. Is also able to catalyze the racemization of several amino acids that are not typically incorporated into proteins such as ornithine and norleucine. Is not active on negatively charged (Glu and Asp) or aromatic (Tyr, Trp and Phe) amino acids and displays minimal activity towards beta-branched aliphatic (Ile, Val and Thr) substrates . Enables bacteria to produce and release extracellular non-canonical D-amino acids (NCDAAs) that regulate diverse cellular processes which may function as part of a cooperative strategy in vibrio communities to protect non-producing members from competing bacteria . D-amino acid production by BsrV provides a cue for V.cholerae to decrease peptidoglycan synthesis and to alter its cell wall via incorporation of NCDAAs into the muropeptides, in adaption to stationary phase conditions .
|
Q9KSE5
|
Q43209
|
PIMT_WHEAT
|
Protein-beta-aspartate methyltransferase
|
Triticum
|
MAQFWAEGSLEKNNALVEYLKQYGVVRTDKVAEVMETIDRALFVPEGFTPYTDSPMPIGYNATISAPHMHATCLELLKDYLQPGMHALDVGSGSGYLTACFAMMVGPEGRAVGIEHIPELVVASTENVERSAAAALMKDGSLSFHVSDGRLGWPDAAPYDAIHVGAAAPEIPRPLLEQLKPGGRMVIPVGTYSQDLQVIDKSADGSTSVRNDASVRYVPLTSRSAQLQDS
|
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. This enzyme does not act on D-aspartyl residues.
|
Q43209
|
Q96BM0
|
I27L1_HUMAN
|
Interferon-stimulated gene 12c protein
|
Homo
|
MGKESGWDSGRAAVAAVVGGVVAVGTVLVALSAMGFTSVGIAASSIAAKMMSTAAIANGGGVAAGSLVAILQSVGAAGLSVTSKVIGGFAGTALGAWLGSPPSS
|
Plays a role in the apoptotic process and has a pro-apoptotic activity.
|
Q96BM0
|
B5F287
|
TRMD_SALA4
|
tRNA [GM37] methyltransferase
|
Salmonella
|
MFIGIVSLFPEMFRAITDYGVTGRAVKKGLLNIQSWSPRDFAHDRHRTVDDRPYGGGPGMLMMVQPLRDAIHAAKAAAGEGAKVIYLSPQGRKLDQAGVSELATNQKLILVCGRYEGVDERVIQTEIDEEWSIGDYVLSGGELPAMTLIDSVARFIPGVLGHEASAIEDSFADGLLDCPHYTRPEVLEGMEVPPVLLSGNHAEIRRWRLKQSLGRTWLRRPELLENLALTEEQARLLAEFKTEHAQQQHKHDGMA
|
Specifically methylates guanosine-37 in various tRNAs.
|
B5F287
|
P05507
|
NU4LM_RAT
|
NADH dehydrogenase subunit 4L
|
Rattus
|
MTSAFLNLTMAFTLSLLGTFMFRSHLMSTLLCLEGMMLSLFVMTSTSTLNSNSMISMTIPITILVFAACEAAVGLALLVKISNTYGTDYVQNLNLLQC
|
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
|
P05507
|
Q0TFH3
|
RBN_ECOL5
|
Ribonuclease Z homolog
|
Escherichia
|
MELIFLGTSAGVPTRTRNVTAILLNLQHPTQSGLWLFDCGEGTQHQLLHTAFNPGKLDKIFISHLHGDHLFGLPGLLCSRSMSGIVQPLTIYGPQGIREFVETALRISGSWTDYPLEIVEIGAGEIFDDGLRKVTAYPLEHPLECYGYRIEEHDKPGALNAQALKAAGVPPGPLFQELKAGKTIMLDDGRQINGADYLAAPVPGKALAIFGDTGPCDAALELAKGVDVMVHEATLDMAMEAKANSRGHSSTRQAAALAREAGVGKLIITHVSSRYDDKGCQHLLRECRSIFPATELANDFAVFNV
|
Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities.
|
Q0TFH3
|
A8W3E9
|
PSBN_CUSEX
|
Protein PsbN
|
Cuscuta subgen. Monogynella
|
METATLITIFLSGLLVSFTGYALYTAFGQPSQQLRDPFEEHGD
|
May play a role in photosystem I and II biogenesis.
|
A8W3E9
|
A1RAW1
|
DCDB_PAEAT
|
DCD-DUT
|
Paenarthrobacter
|
MLISDRDIRAEIDSQRIVLEPYDPAMVQPSSVDVRIDRFFRLFDNHKYAHIDPAEEQPELTRLVEVEGDEPFILHPGEFVLGSTYETVSLADDIAARLEGKSSLGRLGLLTHSTAGFIDPGFSGHVTLELSNVATLPIKLWPGMKIGQLCFFRLTSSAEHPYGSGEYGNRYQGQRGPTASRSHQNFHRTSI
|
Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
|
A1RAW1
|
A8ESZ6
|
URED_ALIB4
|
Urease accessory protein UreD
|
Aliarcobacter
|
MSIKFSFKDEVFSLDKLQLPSRHYHFNDNENYIKLLNIGEGIFPKDKIRTSLSLDNSNLIFTTESATKIYPSKKEYGIQKIDIVLKNNSNLEFINDELILYKDSRYIQFFNLKSDENSTFFYTDILSRGRSFENFDFSNMLIKNSFFCEKSMEYMEKFDVKGAELKDYINRKSSSNFIFAKIYIKTNNNEEFLNRIYLEKFESFTYTKNKKIILGVISSNNMFELKNQIFKIWELYRKELNKSKFNLGKQ
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
A8ESZ6
|
A8EV23
|
HTPG_ALIB4
|
High temperature protein G
|
Aliarcobacter
|
MAKHQFQTEVGQLLHLMTHSLYSNKEIFIRELVSNASDAIDKLNYLRLTDENLKDKYAQWKGEINISFDEKDKSLSIIDNGIGMNEADLIASIGTIAKSGTKSFVEALTGDAKKDSNLIGQFGVGFYSVFMVADKVDVISKKAGEEQAYKWSSTGTGEFDLTPCTKESNGTVIYIKLKDEEAGEFASKYRIKNIVEKYSNHIAYPIFLNYDEEVSEALSEEDEKAGKKPEKKIERKHEQINAATALWMQPKAKLKEQDYNDFYKSISHDSSDPMLTIHTKTEGVNEYTTLFYIPKIAPMDMYRADFQSGVKLYVKRVFITDDEKELLPTYLRFVRGIIDSEDLPLNVSREILQENRILANIKQGSVKKILAEIKKLSKDEEKYAEFVAQYIRPLKEGVYQDYTNKEAILELLRYKSSKTEAGKMTSLEAYKERANSEQKAIYYIVGENEKVLRNSPLLESYKKNDIEVLILDDKEIDEIITPAIGAFKEWEFKDITAIEPPKVEQSEEEKKEVEEKFQDILSKIKDKLGDAVKDVKVTSRLSESPSCVVKDAADAQMAAMAHMFRAMGQAMPESAPILEINPEHEIVKKLNGCADEATIEDVSWILLDQAKLSEGMEITDTVAFAQRLSRITAKAL
|
Molecular chaperone. Has ATPase activity.
|
A8EV23
|
B2AC45
|
MEP1_PODAN
|
Extracellular metalloprotease PODANS_2_14170
|
Podospora anserina
|
MRFSLALAAAGLAQTAFAAPQPSRGFGCGAPEPSEELLQVSQQFAVEEAQALAESYRSGNLTARDVTAQAISVKVYIHVVAASTALSGGYLTDTMINNQFSVLQSAFAPYGISFTLAGTDKTVNANWADDSKGYEMTMKRALRKGTYKDLNLYFLQKMGGNLGYCYFPTTASPGSTAYIRDGCTILYSTTPGGSSTNYNLGHTATHEVGHWFGLYHTFQGGCTGAGDSVSDTPAQASASSGCPVGRDSCPSQAGVDPIHNYMDYSIDSCYEEFTPGQQTRINSFWTSYRQNAS
|
Secreted metalloproteinase that allows assimilation of proteinaceous substrates.
|
B2AC45
|
Q8CXB4
|
UVRC_OCEIH
|
Excinuclease ABC subunit C
|
Oceanobacillus
|
MNENIEKKLSILPQQPGCYLMKDKNGTVIYVGKSKKLRNRVRSYFRGANDRKTQRLVQEIRDFEYMVTSSEIEALILEMNLIKKYDPRYNVMLKDDKSYPYLKITSERHPRLIVTRRLKKDKGKYFGPYPNVIAARETKKLLDRMYPLRKCNNPSGRPCLYYHMGQCKACAENPPSVKEYQEIVQEISSFLQGGFKDIRKNLAGEMQKASEALNFERAKEIRDTIQHIDATMEQQKMTLTDQMDRDIFGYSYDKGWMCVQVFFIRQGKLIERDTSVFPFFDSPEETIVSFIGRFYLHENHLKPKQVLVPVGIDNELLAKVLEIQVHIPLRGRKKELVQLAVKNAEISLNEKFQLIEKDEERTIQAIEDLGEQLNIETPHRIEAFDNSNIQGTDPVSAMIVFEDGKPNKKEYRKYKIRDVKGPDDYDTMREVVRRRYSRVLKENLPLPDLIIVDGGKGQMSAALEVLEDELGLDIPLAGLAKDDRHKTSELLYGMPPIVVPLERQSQAFYLVQRIQDEVHRFAITFHRQLRGKSLFQSELDKIPGVGEKRRKLLLSHFKSINQIKKASIEDMRKLGIPSNIAELVLNHLNSPNDDET
|
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.
|
Q8CXB4
|
Q7M8Z2
|
ISPG_WOLSU
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Wolinella
|
MQERVKTKKIFVGDVAIGGDAPISVQSMTFSKTADIGATKAQIDRLALAGCDIVRVAVSDHEDANALKELKRLSPLPLVADIHFRYKLALIAAQSVDCIRINPGNIGSKEKIKAVADACAERGIPIRIGVNGGSLEEMFEQKYGATPRGMVESALYNIKLLEDFGFANIKVSLKASDVERTVLAYRELRPLVEYPFHLGVTEAGTLFHSMIKSSMALGGLLLEGIGDTMRVSITGELEQEVEVARAILKYSGRQKEGVYLISCPTCGRIEADLVSAVKRVEERVKHIRAPLQISVMGCAVNALGEAKHADIAIAFGRGDGLIIKKGEILCKLPEEELVDRLVEEAEKLEREYLEDSFKN
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
Q7M8Z2
|
Q9VKW2
|
PIE_DROME
|
Pineapple eye protein
|
Sophophora
|
MEDNKELQCLICKYSDTDDLVFGEWMIVRNLQVHYFCLLLSTHLPQRGGDSSGILGFLLRDIREEAAAAEKRKCWYCNKIGASLQCDRCRSLFHLKCGLENRAVFEFCGQYKSYCYKCRPMDDYKRQLQSNPPRNATCPICFSSIYKVELHCVVYGDCCRLGFAHKKCMRQYALTSGYYLRCIWCRSERFRDSIRLQSVFVPDRDATWEKQRNAYRELHERNLKCDQPNCLCPSGRTYNRLSWVILCCSSCAATSAHLKCLVGALRLPKKRERTDFKCSMCLDVERRIAEGPARTTEETNADGDNQVDGSFYVQKLGPDAATRSLTQTPVFSEEDESERSSNITVIFSQPKSNATSERLSLSPPQEEMIVEIPDSPEASPKTSIDENHSPQPIARRDTSDSPQPIAASEIPDSPQPTAASEIPDLPQTTAINVNPELTQQTALNTIPHSPQPEASFSTQLVSQTFDCPQPQEQAVAKAPNSPSLPKEDPNTLLVLKSGFQCPGEPFFYLVIYEFEHGTCMGECIGTCVLRFKEDDPRIQDTSQAALERVNITPDDVWCRSEDRGIFEHIEKFHEWYRSEGFS
|
Required for survival of imaginal disk cells possibly by regulation of cell apoptosis . Required for germline stem cell self-renewal through mediation of BMP signaling .
|
Q9VKW2
|
C4L690
|
GATA_EXISA
|
Glutamyl-tRNA(Gln) amidotransferase subunit A
|
unclassified Exiguobacterium
|
MSLFDHGVAKLHTLLKEGEVTVTDLVKESFDRIEATDDQIGAFLTLNEDAFEQAKRMDELAKMSDNPLFGMPIGVKDNIVTKGMRTTCASTFLENFVPAHDATVVERLHDAGALTIGKLNMDEFAMGSSNENSAFKPVRNPWDPTRVPGGSSGGSAASVAAGQVLFSLGSDTGGSIRQPAAYCGVVGMKPTYGLVSRFGLVAFASSLDQIGPLTRTVEDNAYLLNTIAGHCDMDSTSAEVEVPDYTAALNQDLTGMKFALPEEFMAEGVAPGVREQIEKAIETLKSLGATIETVSIPSVKYALSAYYLLASSEASSNLARFDGIRYGRRAEADTLDEVFTYSREQGFGDEVKRRIMLGTYALSSGYYDAFYKKAQQVRTLMKQDFAKVFEEYDAIVGPTAPTTAFKLGEQLDDPLTMYANDIMTIPVNLVGIPAISVPAGLSEGLPVGLQIIGNYFDESTLYRVAHAFEQANGGFKMPQL
|
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).
|
C4L690
|
Q06GS9
|
MATK_PIPCE
|
Intron maturase
|
Piper
|
MEKFKRYLETFRSEQKYFLYPLLFQEYIYALGHDHGLNGPIPYESIENLGYGDKSSSLIVKRLIIRMHKQNHFLISCNENDFQQNRLLGRKNNLDSKIISEAFSIIVEIPFSFQLVSCLEKKREIAKSHNLRSIHSIFPFFEDNIFYLYHISDVLIPYPIHPEILVQTLRYWIQDVPSLHLLRIFLYEYCHSGSFISKKKFFSFSKKENERLSLFIYNSYVYEWESIFLFIRKQSSHLRSISWEALLERVHFYGKIEHLVVVLCNDFQKALWVFKDCFMHYVRYQGKSLLISKGTDLLMKKWKYHFIYLWQCNFHLWSQPHRIHINQLDNRSFHFLGYASSVRINLSVVKSQILENSFLMETSVKKFETTVPIISLIGSLSKEKFCNLSGHPTSKAIWADSSDSDIMERFGRVCRNLSHYYSGCSKKQILYRIKYILRLSCARTLARKHKSTVRVFLKRLGSGFLKEFLAEEEQVLSFFFPRSYPTSYRSNKDKERIWYLDITHTNDLANHE
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q06GS9
|
B0VYX4
|
COX5A_PONPY
|
Cytochrome c oxidase polypeptide Va
|
Pongo
|
MLGAALRRCAVAAATRAGPRGLLHSTRTPGPAAAIQSVRCYSHGSQETDEEFDARWVTYFNKPDIDAWELRKGINTLVTYDMVPEPKIIDAALRACRRLNDFASTVRILEAVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKL
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
B0VYX4
|
B0BTV5
|
SUCC_ACTPJ
|
Succinyl-CoA synthetase subunit beta
|
Actinobacillus
|
MNLHEYQAKQIFAQYRLPVSKGIVCHSLDDAVSAIHTLAGDTWAAKCQVHAGGRGKAGGVKLVRSEAEIREFCHQWLGQRLVTFQTDKNGQLVNTIYLEETCLIERELYLGAVIDRSSQKIVFMASNAGGMNIEDVAAQTPELIHKATIDPLTGAQAFQGRELAFKLGLSGDQIKQFAHLFVQLAKLFIEKDLALLEVNPLVLTKQGQLLCLDAKMVIDSNALYRHPELKALQDPSQEDAREADAAKWDLNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGRPANFLDVGGGATKERVSEAFKLILSDQNVKAVLVNIFGGIVRCDLIAEGIIAAVNEVGINIPVIVRLEGTNAELGREILANSGLRLIAANTLTQAAQLAVKAAEGK
|
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
|
B0BTV5
|
Q76K27
|
SIAT2_MOUSE
|
Sialyltransferase 2
|
Mus
|
MKPHLKQWRQRMLFGIFVWGLLFLAIFIYFTNSNPAAPMPSSFSFLERRGLLPLQGKQRVIMGALQEPSLPRSLDASKVLLDSHPENPFHPWPGDPQKWDQAPNGFDNGDEFFTSQVGRKSQSAFYPEEDSYFFVADQPELYHHRQGALELPSPGETSWRSGPVQPKQKLLHPRRGSLPEEAYDSDMLSASMSRAFLYRLWKGAVSSKMLNPRLQKAMRYYMSFNKHGVRFRRRGRREATRTGPELLCEMRRRVRVRTLDGREAPFSGLGWRPLVPGVPLSQLHPRGLSSCAVVMSAGAILNSSLGEEIDSHDAVLRFNSAPTRGYEKDVGNKTTVRIINSQILANPSHHFIDSALYKDVILVAWDPAPYSANLNLWYKKPDYNLFTPYIQHRRKYPTQPFYILHPKFIWQLWDIIQENTREKIQPNPPSSGFIGILIMMSMCKEVHVYEYIPSVRQTELCHYHELYYDAACTLGAYHPLLYEKLLVQRLNTGTQADLHHKGKVVLPGFQTLRCPVTSPNNTHS
|
Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. Has alpha-2,6-sialyltransferase activity toward oligosaccharides that have the Gal-beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups, but it has weak or no activities toward glycoproteins and glycolipids.
|
Q76K27
|
B2SYV2
|
OBG_PARPJ
|
GTP-binding protein Obg
|
Paraburkholderia
|
MKFIDEARIEVIAGDGGDGSASMRREKFVPFGGPDGGDGGRGGSVIAVADRNINTLIDYRYAKKHLARNGENGRGADCYGKGGDDITLRMPVGTTITDMETGELIADLTEHNQSVQIAQGGAGGLGNLHFKSSTNRAPRQKTDGKPGERRMVRLELKVLADVGLLGMPNAGKSTFIASVSNAKPKIADYPFTTLAPNLGVVRVGPSRSFVIADIPGLIEGAAEGAGLGHQFLRHLQRTGLLLHIVDLAPFDDAVDPVAEAKAIVNELRKYDELLYEKPRWLVLNKLDMVPEDEREARVSAFLEGFGWDGPVFEISALTGQGCENLCYAVFDHISAHSDAQRAAEAEDLAADVRFREKPQAPAAADDAGTDPQV
|
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
|
B2SYV2
|
O35586
|
IDI1_MESAU
|
Isopentenyl pyrophosphate isomerase 1
|
Mesocricetus
|
MPEINTSHLDEQQVQLLAEMCILIDENDNKIGADTKKNCHLNENIDKGLLHRAFSVFLFNTENKLLLQQRSDAKITFPGCFTNSCCSHPLSNPGELEENDAIGVKRAAQRRLKAELGIPLEEVDPNEMHYLTRIYYKAQSDGIWGEHEIDYILFLKKNVTLNPDPNEIKSYCYVSKEELKELVKKAASGEVKLTPWFKIIVDTFLFKWWDNLNHLSQFVDHEKIHRM
|
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
|
O35586
|
Q0ZJ40
|
PSBA_VITVI
|
Photosystem II Q(B) protein
|
Vitis
|
MTVILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAAAAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANAGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPSING
|
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
|
Q0ZJ40
|
B1WUG7
|
AROE_CROS5
|
Shikimate dehydrogenase (NADP(+))
|
Crocosphaera subtropica
|
MSIITGKTKLLGIIGHPVEHSLSPVMQNAEIKRLGVDYIYIPFPVKPENLETALDGFATIGVMGFNATIPHKQAIIPLLSEVTTTAKLVGAVNTVWRTEIGWKGTNTDVIGFVTPLKALNRDWNTIKPIILGNGGAARAVVVGLAELGCRDICVVGRDKDKLGQFKQSWDTSELQASITVHSWDELSGMVSESQLIVNTTPIGMFPHTQNSPVDSNLWEKLPNNAIAYDLIYNPSPTQFLKDAKQQGLTVIDGLDMLVYQGAAALEIWLQQPVSATVMSEALKQSLFS
|
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
|
B1WUG7
|
Q0BPL3
|
GLGA_GRABC
|
Starch [bacterial glycogen] synthase
|
Granulibacter
|
MRVLNVASEAYPWIKTGGLADVAGALPAALAEHDVDMRTLLPAYAGLRQRPETRPVHHYADLFGGAASILEARLTGGLTLYLLDAPHLYDRPGGPYTDANGRDWADNAERFAAFCRAAADIALGILPDWTPDIVHAHDWQAGLVPAYLALSEASPRPPVLFTIHNLAFQGVVPRDRLAALLLPPDSFSVDGVEYYGQIGLLKAGLHYADALTTVSPSYAREIQTDTGGMGLGGLLRDRAAVLNGLLNGIDMTEWNPAHDPHVKAHFDRHSLEHRTINREALRTRFGLDSSAGPLFGIVSRLTGQKGIDLVLNALPFLISQQAQLVVLGSGDKGLEQGLLQAAQTHPRQIAVFSGYDEALSRQIFSGADAMLIPSRFEPCGLTQLYAMRYGAVPIVSRVGGLADTIIDANTAACEAGVATGLMFQPDGEDSLIEPLSRAIRLFHQAEIWERLQHRGMETDSSWTLRSTAYVALYTRLLSLR
|
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
|
Q0BPL3
|
Q58670
|
DPHB_METJA
|
Diphthamide biosynthesis methyltransferase
|
Methanocaldococcus
|
MLILAGLGLYDENDMTLKTLKFAKKAEKIYAEFYTAVLTGTTTEKIEEVLGKKIHVLSRKDVEYNGYKLIEEAKDKDIMFLTAGDPMVATTHVDLAIEAKKKGIEVLIINAPSIYSAVGITGLQLYKFGKTTSIVFPEENYFPETPYNVIKENLERGLHTLCLLDIRIDENEKRFMTANEGLKVLLELENRKKEGIINEDTKAVVVARAGSLKPKLVYGKIKDLINYDFGEPLHCIIIPGKLHFMEEDALKYLCENI
|
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.
|
Q58670
|
O82381
|
U71C1_ARATH
|
UDP-glycosyltransferase 71C1
|
Arabidopsis
|
MGKQEDAELVIIPFPFSGHILATIELAKRLISQDNPRIHTITILYWGLPFIPQADTIAFLRSLVKNEPRIRLVTLPEVQDPPPMELFVEFAESYILEYVKKMVPIIREALSTLLSSRDESGSVRVAGLVLDFFCVPMIDVGNEFNLPSYIFLTCSAGFLGMMKYLPERHREIKSEFNRSFNEELNLIPGYVNSVPTKVLPSGLFMKETYEPWVELAERFPEAKGILVNSYTALEPNGFKYFDRCPDNYPTIYPIGPILCSNDRPNLDSSERDRIITWLDDQPESSVVFLCFGSLKNLSATQINEIAQALEIVDCKFIWSFRTNPKEYASPYEALPHGFMDRVMDQGIVCGWAPQVEILAHKAVGGFVSHCGWNSILESLGFGVPIATWPMYAEQQLNAFTMVKELGLALEMRLDYVSEDGDIVKADEIAGTVRSLMDGVDVPKSKVKEIAEAGKEAVDGGSSFLAVKRFIGDLIDGVSISK
|
Possesses quercetin 7-O-glucosyltransferase and 3'-O-glucosyltransferase activities in vitro. Also active in vitro on benzoates and benzoate derivatives. Glucosylates other secondary metabolites in vitro like trans-resveratrol, curcumin, vanillin and etoposide.
|
O82381
|
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