ID A0A1H1TM65_9ACTN Unreviewed; 379 AA.
AC A0A1H1TM65;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN04489717_3259 {ECO:0000313|EMBL:SDS61343.1};
OS Actinopolymorpha singaporensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Actinopolymorphaceae; Actinopolymorpha.
OX NCBI_TaxID=117157 {ECO:0000313|EMBL:SDS61343.1, ECO:0000313|Proteomes:UP000198983};
RN [1] {ECO:0000313|EMBL:SDS61343.1, ECO:0000313|Proteomes:UP000198983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22024 {ECO:0000313|EMBL:SDS61343.1,
RC ECO:0000313|Proteomes:UP000198983};
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; LT629732; SDS61343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1TM65; -.
DR STRING; 117157.SAMN04489717_3259; -.
DR OrthoDB; 9803842at2; -.
DR Proteomes; UP000198983; Chromosome i.
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:SDS61343.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000198983}.
SQ SEQUENCE 379 AA; 40628 MW; AACEEE8FFD97B602 CRC64;
MDIETVGVEE EFLLVDPSSR LPVPLAVEVL DTARAGRVPV GASFQPELVR TQVEAATGIC
AEMSTVEDHL GVLRDVLGRA ARTHHARIVS VGHPVLSDGP PPLTPGERFG RIHQRYAEIV
GSYQSCGCHV HIGLPDRETA VAVLNHLRPW LPTLLALSAN SALTEGRDTG YDSWRMVTQA
RFPGSGIPPY FTSATAYDRE VARLVDCGVL VDPDMTFWLA RPSSRYATLE VRAADAAATV
EDALLQAALT RALVRTARAD LASGRAAPVV HDQVGAAAVW SAARHGLAGP AVDPVLGRQV
PTKELLHQLL LRVRPALAET GDLPFVHRYV RHLLAAGTSA ARQRATYDQT KEPRAVVDML
VTQTARTAPP PPFAADAPG
//
