ID   GCS2_JANSC              Reviewed;         378 AA.
AC   Q28R34;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=Jann_1911;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC       glutamate--cysteine ligase activity. {ECO:0000255|HAMAP-Rule:MF_01609}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC         cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01609};
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC       YbdK subfamily. {ECO:0000255|HAMAP-Rule:MF_01609}.
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DR   EMBL; CP000264; ABD54828.1; -; Genomic_DNA.
DR   RefSeq; WP_011455033.1; NC_007802.1.
DR   AlphaFoldDB; Q28R34; -.
DR   SMR; Q28R34; -.
DR   STRING; 290400.Jann_1911; -.
DR   EnsemblBacteria; ABD54828; ABD54828; Jann_1911.
DR   KEGG; jan:Jann_1911; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_5; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000008326; 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;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..378
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000255803"
SQ   SEQUENCE   378 AA;  42506 MW;  92FBA03ECAE121F9 CRC64;
     MAQTFSDEHF TLGIEEEYLL VDAETYDLAE APDALMAACA DKLSSKVSPE FLQCQIEVGT
     GVCASIADAR ADLRNLRATV AECAGRFGLA PIAVSCHPFA DWKDQSHTDK DRYNQLARDL
     GGVVERMLIC GAHCHVGLPS ENDRVDIMRQ MTYFLPHLLA LSTSSPFWQG RDTGLASYRL
     TVFDNLPRTG LPPSFASFDE FQRTVDLLVD MEMIEDSSKI WWDLRPSAAF PTLETRICDV
     SPRLEDQLSL SALIQCLTRM LMRLRGSNQR WRVYDRFLIN ENRWRAQRYG VSDGLIDFGR
     GAVVPLPELV DELIELTEQD AEALGCVDEV QRLRDLAVET SSDRQRKIYK GTRAAGGSHQ
     AAMRSVVEHL LEDFHVDL