ID A0A1I3UIA5_9CELL Unreviewed; 382 AA.
AC A0A1I3UIA5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ORFNames=SAMN05216467_1101 {ECO:0000313|EMBL:SFJ81487.1};
OS Cellulomonas sp. KH9.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1855324 {ECO:0000313|EMBL:SFJ81487.1, ECO:0000313|Proteomes:UP000199404};
RN [1] {ECO:0000313|Proteomes:UP000199404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH9 {ECO:0000313|Proteomes:UP000199404};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC glutamate--cysteine ligase activity. {ECO:0000256|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:0000256|ARBA:ARBA00029283, ECO:0000256|HAMAP-
CC Rule:MF_01609};
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609}.
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DR EMBL; FOSE01000001; SFJ81487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3UIA5; -.
DR STRING; 1855324.SAMN05216467_1101; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000199404; Unassembled WGS sequence.
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 Gene3D; 3.30.590.20; -; 1.
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 NCBIfam; TIGR02050; gshA_cyan_rel; 1.
DR PANTHER; PTHR36510; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR PANTHER; PTHR36510:SF1; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR Pfam; PF04107; GCS2; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01609, ECO:0000313|EMBL:SFJ81487.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000199404}.
SQ SEQUENCE 382 AA; 42183 MW; D2AF6ECE5C84791B CRC64;
MAAPVTLPFA LSERSTVGIE WEVALVDADS GDLRQAAQAI FEAVRPADGT DHPHITSELL
LNTVEVSSGK CRTVGEAGAD LQRALDEVAA AARPLRIELM GAGTHPFASW ATQRVTDKQR
YATLIDRTQW WGRQMLIYGV HVHVGIEDRD KVLPLSRAML TVFPHIQSLS ASSPFWGGED
TGYASNRALL FQQLPTAGLP PQFERWEQLE QYVGDMIHTG VIDLVDEVRW DIRPSPRFGT
LEMRIADGAA SLLEVTAISA FTHCLVEHFS SMIDAGEPLP TLPPWFAQEN KWRSARYGMD
AIVITDAAGN EELVTDSVGR WLVELAPVAE RLGCRQELEQ VRTILRRGAS YQRQRAVARR
HAGELEPVVR ALVAELAAGR PL
//
