ID A0A1G9DS63_9MICO Unreviewed; 378 AA.
AC A0A1G9DS63;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN05216282_11014 {ECO:0000313|EMBL:SDK66696.1};
OS Cryobacterium psychrotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=386301 {ECO:0000313|EMBL:SDK66696.1, ECO:0000313|Proteomes:UP000198701};
RN [1] {ECO:0000313|EMBL:SDK66696.1, ECO:0000313|Proteomes:UP000198701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5382 {ECO:0000313|EMBL:SDK66696.1,
RC ECO:0000313|Proteomes:UP000198701};
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|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; FNFU01000010; SDK66696.1; -; Genomic_DNA.
DR STRING; 386301.SAMN05216282_11014; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000198701; 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:SDK66696.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000198701}.
SQ SEQUENCE 378 AA; 41558 MW; 8B0DDAA00F20727C CRC64;
MGMEFAPSAR SSVGIEWEVA LVDNATGDLV PLAAEVLDAL RADDGSPHPQ ITGELLLNTI
ELVSGVHTNV AGAVADVVAQ LDEVRAVTEP RGVGVICSGS HPFSQWYEQE ITDKPRYHRL
IDRTQWWGRN MMIWGIHVHV GIEDRAKVMP ILNGMLTYIP HLQALSASSP FWAGVDTGYA
SNRALMFQQL PTAGQPWMLP DWEAWERYVD DMTVTGIIED ATEVRWDIRP SARWGTIEVR
VCDGVSTQQE LGAIAALIHC LVEWMSTALD AGEDVPTMPP WFVRENKWRA ARYGLGARVI
LDAAGAERPV TEDIRRLIDV LSPVAERLGC LPELLQLNLI LSHGASYQRQ LEVAEAHGGS
LPAVVAALSR ELRTGLAL
//
