ID A0A1G8T4Y0_9SPHI Unreviewed; 368 AA.
AC A0A1G8T4Y0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04487898_102368 {ECO:0000313|EMBL:SDJ36474.1};
OS Pedobacter sp. ok626.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1761882 {ECO:0000313|EMBL:SDJ36474.1, ECO:0000313|Proteomes:UP000198594};
RN [1] {ECO:0000313|EMBL:SDJ36474.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK626 {ECO:0000313|EMBL:SDJ36474.1};
RA de Groot N.N.;
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; FNEX01000002; SDJ36474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8T4Y0; -.
DR STRING; 1761882.SAMN04487898_102368; -.
DR Proteomes; UP000198594; 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:SDJ36474.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609}.
SQ SEQUENCE 368 AA; 42413 MW; 35FBC7DA977AE897 CRC64;
MMNDFTLGIE EEYMVIDPVT RELSSHDQKI VEAAQKIHKD QVKAEMHQAV VEVGTGICRN
TEQAREEISQ LRHTVSQLAG ELDLKIGASG THPFSRWEKQ LITEHPRYSN IVNELQEAAR
SNLIFGLHVH VGIQSRELAI HIANQVRYFL PHVFALSTNS PFWEGRNTGY KSYRTKIFDK
FPRTGIPDIF NSIEDYDNYV KLLIKTNSID NAKKIWWDIR VHPFFQTIEF RICDCPMLIE
ETMAFAALFQ ALCAKLYKLR LQNMEFISYS RALINENKWR AARYGIDGNL IDFGKEIEVN
CRNLILELLD FIDDVVDELG CRKEINYVLK ILENGTGADK QLAIYEQSGN FEAVIDYITT
QTLIGAKQ
//
