(data stored in ACNUC10821 zone)

SWISSPROT: C8U2U2_ECO10

ID   C8U2U2_ECO10            Unreviewed;       372 AA.
AC   C8U2U2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE            Short=GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2 {ECO:0000256|HAMAP-Rule:MF_01609};
GN   Name=ybdK {ECO:0000313|EMBL:BAI29450.1};
GN   OrderedLocusNames=ECO103_0586 {ECO:0000313|EMBL:BAI29450.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29450.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29450.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits
CC       weak glutamate--cysteine ligase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01609}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + H(+) + L-gamma-
CC         glutamyl-L-cysteine + phosphate; Xref=Rhea:RHEA:13285,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173,
CC         ChEBI:CHEBI:456216; EC=6.3.2.2; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01609, ECO:0000256|SAAS:SAAS01123684};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01609}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2
CC       family. YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609,
CC       ECO:0000256|SAAS:SAAS00994483}.
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DR   EMBL; AP010958; BAI29450.1; -; Genomic_DNA.
DR   RefSeq; WP_001130618.1; NC_013353.1.
DR   SMR; C8U2U2; -.
DR   EnsemblBacteria; BAI29450; BAI29450; ECO103_0586.
DR   KEGG; eoh:ECO103_0586; -.
DR   HOGENOM; HOG000220942; -.
DR   KO; K06048; -.
DR   OMA; LDENKWR; -.
DR   BioCyc; ECOL585395:ECO103_RS03055-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR011793; YbdK.
DR   Pfam; PF04107; GCS2; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR02050; gshA_cyan_rel; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2U2.
DR   SWISS-2DPAGE; C8U2U2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916638};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916648, ECO:0000313|EMBL:BAI29450.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916623}.
SQ   SEQUENCE   372 AA;  41677 MW;  19A38CB162E0BE9D CRC64;
     MPLPDFHVSE PFTLGIELEM QVVNPPGYDL SQDSSMLIDA VKNEITAGEV KHDITESMLE
     LATDVCRDIN QAAGQFSAMQ KVVLQAAADH HLEICGGGTH PFQKWQRQEV CDNERYQRTL
     ENFGYLIQQA TVFGQHVHVG CASGDDAIYL LHGLSRFVPH FIALSAASPY MQGTDTRFAS
     SRPNIFSAFP DNGPMPWVSN WQQFEALFRC LSYTTMIDSI KDLHWDIRPS PHFGTVEVRV
     MDTPLTLSHA VNMAGLIQAT AHWLLTERPF KHQEKDYLLY KFNRFQACRY GLEGVITDPH
     TGDRRPLTED TLRLLEKIAP SAHKMGASSA IEALHRQVVS GLNEAQLMRD FVADGGSLIG
     LVKKHCEIWA GD
//

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