ID A0A3S9WAF7_9MICO Unreviewed; 387 AA.
AC A0A3S9WAF7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=CVS47_01652 {ECO:0000313|EMBL:AZS37027.1};
OS Microbacterium lemovicicum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1072463 {ECO:0000313|EMBL:AZS37027.1, ECO:0000313|Proteomes:UP000276888};
RN [1] {ECO:0000313|EMBL:AZS37027.1, ECO:0000313|Proteomes:UP000276888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Viu22 {ECO:0000313|EMBL:AZS37027.1,
RC ECO:0000313|Proteomes:UP000276888};
RA ORTET P.;
RT "Microbacterium lemovicicum sp. nov., a bacterium isolated from a natural
RT uranium-rich soil.";
RL Submitted (AUG-2018) 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; CP031423; AZS37027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9WAF7; -.
DR KEGG; mlv:CVS47_01652; -.
DR OrthoDB; 9769628at2; -.
DR Proteomes; UP000276888; 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 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:AZS37027.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000276888}.
SQ SEQUENCE 387 AA; 42652 MW; E5191B51D797273F CRC64;
MTEPFAPSSR SSVGLEWEIM LADGETGDLV PRAPEVLAGI EDASALERYT VTGELLTNTV
EVTSGIGDTV AAAVDDVADA IAAVRSVSDP LGIELLCAGS HPFAQWYDQR ITDKTRYHTL
IERTQWWGRN MMIWGIHVHV GVDDVKKVFP IINALAIYLP HLQALSASSP FWAGERTGYA
SNRALVFQQL PTAGLPWPLQ DWAQFESYLD DMVATGVIAD ATEVRWDIRP APRWGTIEVR
ACDGMSTLPE LAAVASLVQV LVEHFSRRLD EGRTLPTIPP WFVRENKWRA ARYGLDARVI
VDADGTQRDV VSHLRETMEE VADIAVDLKC AREFGGLETI LSQGASSTRQ TLIADAADGD
LREVVHHLIR EFRAGPTLRE HLASLGH
//
