ID A0A0F2PW38_9FIRM Unreviewed; 702 AA.
AC A0A0F2PW38;
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:KJS17556.1};
GN ORFNames=VR69_04245 {ECO:0000313|EMBL:KJS17556.1};
OS Peptococcaceae bacterium BRH_c4b.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS17556.1, ECO:0000313|Proteomes:UP000033446};
RN [1] {ECO:0000313|EMBL:KJS17556.1, ECO:0000313|Proteomes:UP000033446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS17556.1};
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:KJS17556.1}.
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DR EMBL; LADO01000017; KJS17556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PW38; -.
DR STRING; 1629717.VR69_04245; -.
DR PATRIC; fig|1629717.3.peg.1780; -.
DR Proteomes; UP000033446; 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; 75426 MW; C4F031EE2B6FBA65 CRC64;
MGVLTNFFNP QSVAVIGASS SPGKIGHAIL KNVIESGYAG KILPVNPRED EILGLKAYPD
IKAVPGRVEM AVISVPAAGV LKVAGECGRA GVKNLVVITA GFKEVGKEGL DMEKELLATC
REYGMHMLGP NCLGMIDTHM RINTSFAKVY PLKGNIAFFS QSGAMQVALL DWSLTAGIGF
SKVVSLGNKA DLSEIDFIEE AAEDPYTRVI LCYIEDVANG ERFLQAVSRA TRKKPVVILK
SGTSQAGAQA ASSHTGALAG SDIAYETAFK QCGVIRVKTM TELFDLATAF SKCALPAGDK
VAIVSNSGGP GIIATDNVET HRLRMARFNK DTLEVLRGGL PPESGIYNPV DVLGDARADR
YRFALEKVCA DSNTDVLMLL LSQTATTQAM ETGRALIEMK ETYPDKTFFA SFMGGDALKE
GVNLLAESGI PCYTFPEPAI SAISQMVKYR QFINSPLQED GLEFPDVDKK AVKAIFYDVL
KDNRLVLLGS EAAEVARAYG IPAAPVALAT TTDEAVEEAE KIGYPVVLKV ASPKILHKTD
VGGVKVSLDS PAAVKNGFLE IMESVRRLMP QAVVYGVEVN KMMPRGTELI IGMSRDIQFG
PMIACGLGGI YVNLFKDVSF RLARGLTRDE IVKMITETKS YSLLRGYRGS EPQDVNAVVD
AVGRVARLAL DFQEITELDV NPVFVYPNGL SALDVKITIS MS
//
