ID   GCS2_JANMA              Reviewed;         370 AA.
AC   A6T1A0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=mma_2607;
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille;
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA   Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the convergent
RT   evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR89614.1; -; Genomic_DNA.
DR   RefSeq; WP_012080459.1; NC_009659.1.
DR   AlphaFoldDB; A6T1A0; -.
DR   SMR; A6T1A0; -.
DR   STRING; 375286.mma_2607; -.
DR   EnsemblBacteria; ABR89614; ABR89614; mma_2607.
DR   KEGG; mms:mma_2607; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_4; -.
DR   OMA; HIHIGCP; -.
DR   OrthoDB; 991285at2; -.
DR   BioCyc; JSP375286:MMA_RS13535-MON; -.
DR   Proteomes; UP000006388; 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..370
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_1000069439"
SQ   SEQUENCE   370 AA;  41750 MW;  B585343AB22A1167 CRC64;
     MLEFNNSTPL TMGVELELQI VNRRDYNLTR GSSDLLVIID KTDHGYDIKP EITESMIEIA
     TSVHTDHKEM LAELTAMRTL LISAADKLNL GLAGGGAHPF QHWEDQRIYP TDRYRLVSEL
     YGYLAKQFTV YGQHIHIGCA TGDEAIRLAH MLARYIPHFI TMSASSPFYQ GVDTTFQSSR
     LTSINAFPLS GYMPFVTDWD SFNAYFDKMS SLGIVASMKD FYWDIRPKPE YGTVEIRVCD
     TPLSIEVAVA LAGYAQTLSK FFFAQQELKP AQDTYLTYSY NRFQACRFGL NGALINPING
     TQTSIKEDIL QTFEMLADIA QELGTTEAIE LLRQRIQAGQ SDADWLRASY EKSGSLSDVV
     RQQSAVWMAR