ID A0A075WCH8_ARCFL Unreviewed; 685 AA.
AC A0A075WCH8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN ORFNames=AFULGI_00013100 {ECO:0000313|EMBL:AIG98085.1};
OS Archaeoglobus fulgidus DSM 8774.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=1344584 {ECO:0000313|EMBL:AIG98085.1, ECO:0000313|Proteomes:UP000028501};
RN [1] {ECO:0000313|EMBL:AIG98085.1, ECO:0000313|Proteomes:UP000028501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8774 {ECO:0000313|EMBL:AIG98085.1,
RC ECO:0000313|Proteomes:UP000028501};
RA Fiebig A., Birkeland N.-K.;
RT "Genome of Archaeoglobus fulgidus.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP006577; AIG98085.1; -; Genomic_DNA.
DR RefSeq; WP_048095590.1; NZ_CP006577.1.
DR AlphaFoldDB; A0A075WCH8; -.
DR GeneID; 24794816; -.
DR KEGG; afg:AFULGI_00013100; -.
DR HOGENOM; CLU_007415_3_1_2; -.
DR Proteomes; UP000028501; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR014089; AcCoA-synth-alpha.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR02717; AcCoA-syn-alpha; 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 Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
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 477..513
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 685 AA; 74668 MW; D2E4346996026139 CRC64;
MERLFYPKVV AVIGASPQEG KVGNTIMKNL RNFSGTVYAV NPKYSEILGF PCYPSVLKIP
ENVDLAIIVV PAKLVPKAVE ECGRRGVEGA VVISAGFKEA GIEGAKLERE LVEVAERYGV
KLVGPNCLGM INTEIAMNAT FSRVAPEKGR IAFLSQSGAF ILAVLEWSKR NGVGFSKVVS
LGNKAMIDES DFLEYLAKDD STDVILIYME GVEDGRKFMR VAKSVARRKP VVVMKAGKSQ
SGAKAASSHT GSLAGSYEAY RAAFRQSGVI EASSVEELFD FALLLLKYRK AGNLAILTNS
GGPGVIAADA CDQFGVPLAN FNFETIRKLK EFLPAESNFY NPVDILGDAS AERFSRSLQI
LSEDENVDIV LAILTPTAQM DFLKAAESVV GKNAVCCFMG GESVDEPERI LRSSGIPNFF
DPVRAVRAIS VLRRYSEISA KERVEEDLDV SVEREKAEEI IEKLLESGGR VVGAEGLPVL
EAYGIEVAPY GIARNVDEAR DIAESIGYPV VLKVVSPDVV HKSDVGGVKL NVGENDFEKA
FFEILSNVEG RMPKARIEGV LVQKMVDGGK ELIVGMKRDP QFGPMIMFGM GGVYVEVLKD
VSFRIAPITK REAHEMVREV KAYRILRGLR GEKPADIDAI ADLLLRVSKL SLDHPEVLEM
DLNPVKVFES GYAVVDFRMV LGEEV
//
