(data stored in SCRATCH zone)

SWISSPROT: E6V5D9_VARPE

ID   E6V5D9_VARPE            Unreviewed;       402 AA.
AC   E6V5D9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 51.
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=Varpa_0524 {ECO:0000313|EMBL:ADU34745.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34745.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34745.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34745.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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; CP002417; ADU34745.1; -; Genomic_DNA.
DR   RefSeq; WP_013538991.1; NC_014931.1.
DR   STRING; 595537.Varpa_0524; -.
DR   EnsemblBacteria; ADU34745; ADU34745; Varpa_0524.
DR   GeneID; 29719980; -.
DR   KEGG; vpe:Varpa_0524; -.
DR   eggNOG; ENOG4106KXD; Bacteria.
DR   eggNOG; COG2170; LUCA.
DR   HOGENOM; HOG000220942; -.
DR   KO; K06048; -.
DR   OMA; LDENKWR; -.
DR   OrthoDB; 991285at2; -.
DR   BioCyc; VPAR595537:G1GQO-527-MONOMER; -.
DR   Proteomes; UP000008917; 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; E6V5D9.
DR   SWISS-2DPAGE; E6V5D9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916638};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916648, ECO:0000313|EMBL:ADU34745.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609,
KW   ECO:0000256|SAAS:SAAS00916623};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917}.
SQ   SEQUENCE   402 AA;  45484 MW;  193C9C62E80AFD43 CRC64;
     MSTALQTPID PDSDDVRSAP LAADPDSRAV KLEPFNKSEA LSLGVELELQ LVNTHDYDLA
     PYAEDMLRLM AQTPLPGSVV PEMTSSMIEI STDICHSAAD VIKQLSPIRE ALIKNADKLN
     IAVVGGGTHA FQQWHERRIY DKPRFRELSE LYGYLSKQFT IFGQHVHIGC PDADAALLML
     HRMSRYIPHF IALSASSPFV QGQDTQFDSA RLNSVFAFPL SGRAPFTTSW KEFEAYFERM
     TRTGVVRSMK DFYWDIRPKP EFGTIEIRVF DTPLTVERAA ALAGYVQSLA AWFLQEQPFE
     PSEDDYLVYT YNRFQACRFG LDAVYVDPAS GQHMPLRDHI LMTMTQLEWH SEALNATQAL
     GELRTSVEAN RNDARWLREK QGKERLLAEV VRQAALRFRG AA
//

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