ID A0A1H1VWC3_9ACTN Unreviewed; 443 AA.
AC A0A1H1VWC3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Glutamate--cysteine ligase EgtA {ECO:0000256|HAMAP-Rule:MF_02034};
DE EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_02034};
DE AltName: Full=Gamma-glutamylcysteine synthase {ECO:0000256|HAMAP-Rule:MF_02034};
DE Short=GCS {ECO:0000256|HAMAP-Rule:MF_02034};
DE Short=Gamma-ECS {ECO:0000256|HAMAP-Rule:MF_02034};
GN Name=egtA {ECO:0000256|HAMAP-Rule:MF_02034};
GN ORFNames=SAMN04489717_4237 {ECO:0000313|EMBL:SDS89043.1};
OS Actinopolymorpha singaporensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Actinopolymorphaceae; Actinopolymorpha.
OX NCBI_TaxID=117157 {ECO:0000313|EMBL:SDS89043.1, ECO:0000313|Proteomes:UP000198983};
RN [1] {ECO:0000313|EMBL:SDS89043.1, ECO:0000313|Proteomes:UP000198983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22024 {ECO:0000313|EMBL:SDS89043.1,
RC ECO:0000313|Proteomes:UP000198983};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC).
CC This compound is used as substrate for the biosynthesis of the low-
CC molecular thiol compound ergothioneine. {ECO:0000256|HAMAP-
CC Rule:MF_02034}.
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_02034, ECO:0000256|PIRNR:PIRNR017901};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02034}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC EgtA subfamily. {ECO:0000256|HAMAP-Rule:MF_02034,
CC ECO:0000256|PIRNR:PIRNR017901}.
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DR EMBL; LT629732; SDS89043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1VWC3; -.
DR STRING; 117157.SAMN04489717_4237; -.
DR OrthoDB; 9780152at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000198983; Chromosome i.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.590.20; -; 1.
DR HAMAP; MF_02034; EgtA; 1.
DR InterPro; IPR017809; EgtA_Actinobacteria.
DR InterPro; IPR035434; GCL_bact_plant.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR34378; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR34378:SF1; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR Pfam; PF04107; GCS2; 1.
DR PIRSF; PIRSF017901; GCL; 2.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02034,
KW ECO:0000256|PIRNR:PIRNR017901};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02034, ECO:0000256|PIRNR:PIRNR017901};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02034,
KW ECO:0000256|PIRNR:PIRNR017901};
KW Reference proteome {ECO:0000313|Proteomes:UP000198983}.
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 48504 MW; 616198CC883E2220 CRC64;
MTDTAEVVSC DSVHGHIGRI CFKTGPPTTV GTEIEWLVVS PDHPRELVPL DLLRTTLDQA
GPPPGGSTVT FEPGGQVELS SAPAPGLGAC WSTLQSDIDH VRAALAALDL RLLWTAIDPF
REPRRQLSHP RYDAMEAYFD RRGPEGRLMM CSTASVQVNL DAGADADDIA RRWRILHAIG
PAMVATFANS PWFAGRQTGW KSARQAVWQR LDPRRTRSPH GHDPVAAWAD YALDAPLMMR
RDGDRWHSDP GLTFRQWLHL RPDDEHAGNG RADHAANGAA NGRADGRAAR RADARADGGA
DGSPTAHDLA YHLTTLFPPV RPRGWFEIRY LDVVPAAYWP VPMAVLTALV DDPRAGERAL
AATAPVAGAW WNAARDGLDH RGLAHAARCC FEAALEALHR QGAERALVNL VDDYRIRYVD
RARCPADDGA DPLTSDSDRE ESR
//
