ID A0A2I0NZV0_9EURY Unreviewed; 482 AA.
AC A0A2I0NZV0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
DE Flags: Fragment;
GN ORFNames=CVV33_07475 {ECO:0000313|EMBL:PKL59506.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013820 {ECO:0000313|EMBL:PKL59506.1, ECO:0000313|Proteomes:UP000233538};
RN [1] {ECO:0000313|EMBL:PKL59506.1, ECO:0000313|Proteomes:UP000233538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-4 {ECO:0000313|EMBL:PKL59506.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
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:PKL59506.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PGYJ01000402; PKL59506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0NZV0; -.
DR Proteomes; UP000233538; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
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; 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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
PE 4: Predicted;
FT DOMAIN 32..125
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PKL59506.1"
SQ SEQUENCE 482 AA; 51824 MW; 4604D25AD94AB9F4 CRC64;
EGACAVDARI FVKTGPEDIL SPVQILPPVP DLLHPSSIAV VGASRTPGKV GYAVFRNLLN
FQGELYPVNP HAEDIMGKKA FSTITSIPGP VEMVVIATPA EFVPDIVEEA GNKGVKSAVI
LSAGFKETGE EGQKLENKLL SVARETGIRI VGPNCLGIVI PPLDLNATFD VQSPLSGYIG
FISQSGAIIT TVLDWSISRR IGFSSVISVG NQTDMGFLEY LQVLDQDPHT YAIILYVEEI
RDGCAFLQYA ESMRGRKPII ALKSGSSVRG REAASSHTGS LAGSYETYIA AFKQAGIIPA
YSLAEAFDVA RLVVSEGYPK GKRTIILTNA GGFGVLAADY ADINGMELIN LPEVVVDELS
KILPDSWSHK NPVDLLGDSN ASRFAKVFDV MTKYQHLWDI AVVITAPVAM MDPKNLAHEM
IRLSRFTHAM VVGCLLGGDS MKSAIDMLGE AHIPNYQDLQ DAFRTVGAIL ESCNLNENSE
QP
//
