ID A0A150J3P3_9EURY Unreviewed; 212 AA.
AC A0A150J3P3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN ORFNames=AMQ22_01138 {ECO:0000313|EMBL:KYC51840.1};
OS Candidatus Methanofastidiosum methylthiophilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC Methanofastidiosum.
OX NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC51840.1, ECO:0000313|Proteomes:UP000075398};
RN [1] {ECO:0000313|EMBL:KYC51840.1, ECO:0000313|Proteomes:UP000075398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U1lsi0528_Bin055 {ECO:0000313|EMBL:KYC51840.1};
RX PubMed=26943620;
RA Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT fastidious methyl-reducing methanogen.";
RL ISME J. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate;
CC Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456216; EC=6.2.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001619};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYC51840.1}.
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DR EMBL; LNGC01000044; KYC51840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150J3P3; -.
DR STRING; 1705564.APG08_01453; -.
DR Proteomes; UP000075398; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 6..42
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 212 AA; 23633 MW; E66D85072B4A93E9 CRC64;
MEHEAKEIMK AYGIKVPKEG IATSEEEVLK ISRQVEYPVV LKIASPDIQH KTDAGAVVLN
LSKAEDILEA YRRVLENSKK FDPTADIRGV IVQHMMPKQR EVIIGVSRDN QFGHVLMFGL
GGIFVEVLKD VSFRIVPIEE EDAYEMISEI RSHQMLCGVR GEKPSDVGAL VDIMLKVSKF
VSDFPEVKEL DLNPVFVCEK GAVAVDALIV ID
//
