ID A0A166B810_9EURY Unreviewed; 698 AA.
AC A0A166B810;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN Name=sucD_1 {ECO:0000313|EMBL:KZX12994.1};
GN ORFNames=MBORA_08950 {ECO:0000313|EMBL:KZX12994.1};
OS Methanobrevibacter oralis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=66851 {ECO:0000313|EMBL:KZX12994.1, ECO:0000313|Proteomes:UP000077428};
RN [1] {ECO:0000313|EMBL:KZX12994.1, ECO:0000313|Proteomes:UP000077428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7256 {ECO:0000313|EMBL:KZX12994.1,
RC ECO:0000313|Proteomes:UP000077428};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter oralis DSM 7256.";
RL Submitted (APR-2016) 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};
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:KZX12994.1}.
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DR EMBL; LWMU01000059; KZX12994.1; -; Genomic_DNA.
DR RefSeq; WP_042694033.1; NZ_LWMU01000059.1.
DR AlphaFoldDB; A0A166B810; -.
DR STRING; 66851.MBORA_08950; -.
DR PATRIC; fig|66851.6.peg.986; -.
DR OrthoDB; 18103at2157; -.
DR Proteomes; UP000077428; Unassembled WGS sequence.
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; IPR014089; AcCoA-synth-alpha.
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 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; 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:KZX12994.1}.
FT DOMAIN 7..102
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 698 AA; 74835 MW; 3CBAF9069DBA5771 CRC64;
MKDLNKMFKP ESVAIIGASS TSGKVGHIIV DNLINDGFKG EIYPVNPKGG EILGKTAYAS
IKDIPKTVDL AIITIPSVFV NDTVRDCGEV GVKNIVVITA GFKEVGEEGA KLEAELTKLG
EEYGINIIGP NSLGITDSHT PLNGSFSQMM TPKGNIAFIS QSGAMMVAII DWSITSGIGF
SKVISLGNKA GVNEIELLKY LSEDDETAVI ICYLESISED EDFIRTMREV AIKKPIIILK
SGSSSAGAEA ASSHTGALAG SDLAFDTAFK QSGIIRVGTM AELFDLGLAF SKAPLPKGDH
VAIITNAGGG GVLTVDAMEK AGLKLVQFDD ETKAKLKECI PDEGSVNNPI DVLGDAPVDR
YKKSLDIVLK DEQVDSLIIM VCPTASADPD GIANVILEER HKFSKPIIVV NMGGPSFEDA
NNALRANDVP TYVFPETAVT ALEAMTRFAR LEDRSYDDVI EKVSDVDKNA VRAIFDKVTS
AGRDTLLGSE AYAVAEAYRI SAAPIRLSKS AEEAAELAEE MEFPVVLKIA SDKILHKSDI
GGVKVGITNS NEAKKAYNEI IANAKKAHPD IIPDGVEVQK MMDSGEEVIV GMIKDKQFGP
MIAFGMGGIY VNLIEDVSFN LARGLSSEEI EKQIESTKVS KLLEGYRGEA PCDIDEVKEA
IKRVARLTLD FPEISELDIN PIFVYEKGSS ALDIKIKL
//
