ID   GCS2_METPP              Reviewed;         370 AA.
AC   A2SKM7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Mpe_A3163;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(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; CP000555; ABM96116.1; -; Genomic_DNA.
DR   RefSeq; WP_011830739.1; NC_008825.1.
DR   AlphaFoldDB; A2SKM7; -.
DR   SMR; A2SKM7; -.
DR   STRING; 420662.Mpe_A3163; -.
DR   PRIDE; A2SKM7; -.
DR   EnsemblBacteria; ABM96116; ABM96116; Mpe_A3163.
DR   KEGG; mpt:Mpe_A3163; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_4; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000000366; 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_0000291492"
SQ   SEQUENCE   370 AA;  42199 MW;  AA08F26E406811BD CRC64;
     MALQDFTPSE PLTLGVELEL QLLSTHDFDL APQAEDLLRE TAKHSGAWDI KPEITRSMIE
     IGSSIQRRHG PLREELRDMR NQLTRAARKL NIAIAGGGTH AYQHWSEQQI FPAERFRYIS
     ELYGYLAKQF TVFGQHVHVG CPDGDQALWL LHALSRYVPH FIALSASSPY VQGQDTGFDS
     ARLNSVFAFP LSGRAPFVRS WEEFGGFFDK MTATGVVQSM KDFYWDIRPK PEFGTIELRV
     CDTPLSVDKA AALACYLQCI CRQLREEKPF EPSEDDYLVY TFNRFQACRF GLDGEIVDPK
     TKQRSRLRDD ILRTLTRLDE HALDLEALDA TQLLRDSLFE GNDARWLRTQ RAAMLPLPAV
     VEAAARRWGE