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Database: UniProt
Entry: G8SHW9_ACTS5
LinkDB: G8SHW9_ACTS5
Original site: G8SHW9_ACTS5 
ID   G8SHW9_ACTS5            Unreviewed;       361 AA.
AC   G8SHW9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
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   OrderedLocusNames=ACPL_4694 {ECO:0000313|EMBL:AEV85585.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV85585.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) 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; CP003170; AEV85585.1; -; Genomic_DNA.
DR   RefSeq; WP_014691656.1; NC_017803.1.
DR   AlphaFoldDB; G8SHW9; -.
DR   STRING; 134676.ACPL_4694; -.
DR   KEGG; ase:ACPL_4694; -.
DR   PATRIC; fig|134676.3.peg.4608; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   Proteomes; UP000005440; 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:AEV85585.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005440}.
SQ   SEQUENCE   361 AA;  38243 MW;  76FE7EBF5C3DCD3D CRC64;
     MVRTVGVEEE FLLLDPATGV NLPVAGRVVA ALPESLRRRS RREFRPSMLE MVSDVCVEAD
     DLARQLAQNR GAAGAAAATA GVLLVAVGAS PVAEPDREPD DDPRFRAITD FYGPVARDPA
     LCGCHVHVGV DDPEHAVEVC NRLRPDLPLI QALSANSPLC EGADTGYASW RSVQLRRWPA
     LGPWPHAGSV AEVEETVAAL VAAGEMMDAS MELWWARPSR TFPTVEVRVA DVGPAPADAV
     LLAMLVRGLV ETSTEGPMVS DLLLTAAHGN AARSGMGGTL LCLRTGRARP AWDLVGEMVD
     RIAPALRKAG DLDAVVAGLD RIRREGTGAD RQRRLLAAPG TTIPAMLRAF SVSPGDRPAT
     A
//
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