(data stored in SCRATCH zone)

SWISSPROT: D7A261_STAND

ID   D7A261_STAND            Unreviewed;       374 AA.
AC   D7A261;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 48.
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   OrderedLocusNames=Snov_0344 {ECO:0000313|EMBL:ADH87677.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87677.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87677.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
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   -!- 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; CP002026; ADH87677.1; -; Genomic_DNA.
DR   RefSeq; WP_013165182.1; NC_014217.1.
DR   STRING; 639283.Snov_0344; -.
DR   EnsemblBacteria; ADH87677; ADH87677; Snov_0344.
DR   KEGG; sno:Snov_0344; -.
DR   eggNOG; ENOG4106KXD; Bacteria.
DR   eggNOG; COG2170; LUCA.
DR   HOGENOM; HOG000220943; -.
DR   KO; K06048; -.
DR   OMA; LDENKWR; -.
DR   OrthoDB; 991285at2; -.
DR   BioCyc; SNOV639283:G1GLM-348-MONOMER; -.
DR   Proteomes; UP000006633; 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; D7A261.
DR   SWISS-2DPAGE; D7A261.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916638};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916648, ECO:0000313|EMBL:ADH87677.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916623};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633}.
SQ   SEQUENCE   374 AA;  41919 MW;  4F9CB54EDEA5610D CRC64;
     MTTEEYRIGI EEEYFIVDGE TKSALRRMPA PFMDQARGAL GEAVSGEMLQ SQIEMMTRPH
     VSAADARRQL HGLRRSLGEV AAEFDLAFLA AGTHPTASWQ TGKRTPTQRY DGLMHDLQMV
     GERNMLCGMH VHVELPDADQ RVDVMRRILP YLPIFVALST SSPFWESKRT GLMGYRLAAY
     DELPRTGLPE LFESAKDYQD YVDALVAARA IRDSSYVWWT IRPSQKHPTL ELRAPDSCTR
     VEDSVAIAAL YRALVRHLVR DPKLNAGIDA VDRAIAVENK WRAQRYGIHG SFVDRRTREA
     VPVTQAVETL IDQLREDARA LGGLDELEHL RTILGGGTSA DIQIAVYQEA AHRTGNRNEA
     LNAVKTWLAH ASAQ
//

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