ID A0A0U5CXQ4_9EURY Unreviewed; 698 AA.
AC A0A0U5CXQ4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN Name=acdA1 {ECO:0000313|EMBL:CQH54764.1};
GN ORFNames=HHUB_2126 {ECO:0000313|EMBL:CQH54764.1};
OS Halobacterium hubeiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH54764.1, ECO:0000313|Proteomes:UP000066737};
RN [1] {ECO:0000313|Proteomes:UP000066737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA Yang C., Oksanen H.M., Bamford D.H.;
RT "The complete genome of a viable archaeum isolated from 123-million-year-
RT old rock salt.";
RL Environ. Microbiol. 18:565-579(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};
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DR EMBL; LN831302; CQH54764.1; -; Genomic_DNA.
DR RefSeq; WP_059056565.1; NZ_LN831302.1.
DR AlphaFoldDB; A0A0U5CXQ4; -.
DR STRING; 1407499.HHUB_2126; -.
DR GeneID; 26658789; -.
DR KEGG; hhb:Hhub_2126; -.
DR OrthoDB; 18103at2157; -.
DR Proteomes; UP000066737; Chromosome I.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP 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; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR043938; Ligase_CoA_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
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; PF19045; Ligase_CoA_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.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:CQH54764.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066737}.
FT DOMAIN 8..100
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 698 AA; 73238 MW; A1914A1B6B05D763 CRC64;
MEDDASGLFA PDRVAVVGAT DREGAVGRAI VTNLADFDGD VVAVNPGREE VLGYDCYPDL
QTAPDADLAV VVVPPSVVVD AVRDAGEAGV RNVVVITAGF SETGSEGADR ERDLAAVADD
YDLNLVGPNS LGVLSTPSGL NATFGPSNAL PGSLSFMSQS GAFITAVLDW ANDQGIGFKD
VVSLGNKAVM DETDFLRQWH DDAETNVVLG YLEGIEDGRE FIDTAREVTE DTPAVVVKSG
RTEAGAQAAS SHTGTIAGSE AAYEAGFEQA GVVRAENVQE LFDFARALDG LPLPDSEEVA
VVTNAGGPGV MATDAVGDAR LSMASFGDDT IDALSEMLPA EGNVYNPVDV LGDAGVERFA
DALDTVLGSE DVGCAVVVAA PTAVLDFAEL AEVLAERQAE HGKPVVACLM GGERTERAAD
ALSAAGIPNY FDPARAVDSL DALAVQRAVE AREYEEPAEF DVDRERAREI LTDAADRGSR
RLGVEAMDLL DAYGIPTPEG EVVDDPADAV WVANDIDGDV VMKIVSPDIL HKSDIGGVKV
GVPDDEVRDA YEDLVTRAKN YQPDATILGV QVQEMVDTDA GTETILGVNR DPQFGPLVLF
GLGGIFVEVL EDTSVRVAPV SGREADEMID DLDSAPLLRG ARGREPADEE AITDAVQRLS
QLVTDFPAIL ELDVNPLLAT ADGVQALDVR LTIDPEQL
//
