ID A0A0F2PDH0_9FIRM Unreviewed; 702 AA.
AC A0A0F2PDH0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:KJS12369.1};
GN ORFNames=VR67_09245 {ECO:0000313|EMBL:KJS12369.1};
OS Peptococcaceae bacterium BRH_c8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629715 {ECO:0000313|EMBL:KJS12369.1, ECO:0000313|Proteomes:UP000033493};
RN [1] {ECO:0000313|EMBL:KJS12369.1, ECO:0000313|Proteomes:UP000033493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c8a {ECO:0000313|EMBL:KJS12369.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJS12369.1}.
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DR EMBL; LADP01000021; KJS12369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PDH0; -.
DR STRING; 1629715.VR67_09245; -.
DR PATRIC; fig|1629715.3.peg.4185; -.
DR Proteomes; UP000033493; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
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; 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.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 493..529
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 702 AA; 75018 MW; AB7D89BB6DF240E9 CRC64;
MAELTKMVRP GSVAVVGASA AAGKIGNTIL NNMISSGFDG KIYPINPKEK EIKGIKAYPS
VIDIKEPVDM AVIAVPASRV PDVAEECGKA GVKNLVVVSA GFKEVGPAGL ELEKRLTNVC
RQYGMRMLGP NVVGLIDTHT PINASFSGTF PQQGEIAFFS QSGAMLVAIL DWSAAGGLGF
SRVISLGNKA DLSEIDFIED AADDPNTKVI LCYIEDIVDG RRFLEVVARA ARKKPVIILK
SGTSQAGAQA ASSHTGALAG SDLAYEVAFR QCGVIRAHSM TELFDLAVAF ARAPVPRGSR
VAIVTNAGGP GIIATDNVEN TGLQMARFTK ETIEELRVKL PSEAGLYNPV DVLGDAKADR
YRLALQKVCA DPNVDSVVVL VCPAGVTEPV QTAEAILEMR EAFPEKPIFA AYMGGENLAK
GAGLLVRAGV PCYTFPEPAI ASIRGLVRYN ELLNTPEEGG STNLKGLDRN GVKAIFYDVI
RDQRLVLLGS EAAEVANCYG IPATPITLAT TPQEAVSEAD KMGYPVVMKV ASPKILHKTD
VGGVKIGLKD AAQVREAFTD IMDNVHGYMP QAVIYGIEVQ KMMPKGDELI VGMTRDVQFG
PLIAFGLGGI YVNLLKDVSF RLARGLSARE IEIMLRETKA YTLLRGYRGE KPRDIEAVVD
VIRRVAALVT DFPEITEMDI NPVFAYEEGM GLSALDIKIT IS
//
