ID A0A1H0Q1S1_9BURK Unreviewed; 382 AA.
AC A0A1H0Q1S1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN05216303_10376 {ECO:0000313|EMBL:SDP11020.1};
OS Rhodoferax sp. OV413.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1855285 {ECO:0000313|EMBL:SDP11020.1, ECO:0000313|Proteomes:UP000199151};
RN [1] {ECO:0000313|Proteomes:UP000199151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV413 {ECO:0000313|Proteomes:UP000199151};
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|HAMAP-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; FNJA01000003; SDP11020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0Q1S1; -.
DR STRING; 1855285.SAMN05216303_10376; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000199151; 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:SDP11020.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000199151}.
SQ SEQUENCE 382 AA; 42302 MW; 6F17EA71A92C4B33 CRC64;
MQFHHSKALT FGMELELQIV DDATGSLSPS SGELWSELEK LPEIERYALE ATLSTIEVTS
SIHEDSDEME VESRKLVSTL KDIAQAKGLN LRGGGTHILQ FWNEREFTPT DRAHELESKY
GFLPKRFSTY GMHVHVGMPG KAEAIQVANV LQSLTPLFIA LSAASPFQQG VDTGFCSARP
LEPLVYPYGG PMPKVADWTE FERITDEIFA SGLAKSLKDI YWDVRPKPEF GTVEVRVFDT
PLRMQKGVSL AALTRGCAAL ALSGKLQLPT IHIPYNTDRV SRFLACRDGM AARLYNPMAG
EWMPAHQWLD QLVDLIEQNP LGAADLRRVR ELQGIADGQQ DSDIMRSTWH RLASASDAAE
ANAPGSAAYA ANTREHCDRL LS
//
