ID Q2RLH5_MOOTA Unreviewed; 707 AA.
AC Q2RLH5;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=CoA-binding protein {ECO:0000313|EMBL:ABC18714.1};
GN OrderedLocusNames=Moth_0380 {ECO:0000313|EMBL:ABC18714.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC18714.1};
RN [1] {ECO:0000313|EMBL:ABC18714.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC18714.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000232; ABC18714.1; -; Genomic_DNA.
DR RefSeq; YP_429257.1; NC_007644.1.
DR AlphaFoldDB; Q2RLH5; -.
DR STRING; 264732.Moth_0380; -.
DR EnsemblBacteria; ABC18714; ABC18714; Moth_0380.
DR KEGG; mta:Moth_0380; -.
DR PATRIC; fig|264732.11.peg.412; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_9; -.
DR OrthoDB; 9807426at2; -.
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; 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 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 500..705
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 707 AA; 76091 MW; DF0ACAF28B48AC62 CRC64;
MNAESLQPIF YPRSVAIVGA SNNPDKASHQ FLKTLIEERF TGDIFPVNPR ETKVLGLDCY
PSLKDVSGYV ELVVIAIPAP GVPEVMRQAA ERGDVKGAII VSAGFAETAI PERVKLEKEV
VAIARSAGIR VIGPNCNGVI NTENRLSTSF APGLQMIPGN IGFFTQSGAT GGSILMLTAA
QPKPLGFSKW AHVGNMCDVT NLEILEYYAS DPSVKVIAGY MEGVRDGREL MRLAEKITRK
KPLLVLKVGR TEVGSRATLS HTGTLAGSDK IYDAAFTQSG IVRVDKLEEL VDSAKVLVMA
PPPRGNRVCI LTEAGGLGII AMDEVGSDPA VRLASLTPET QKALAEVLPP MAMICKPNGY
IDMTAAAMER EHAEALRLVL EDPNVDAVLL IGLPPTFLPA ERVAQAIAAV AKKYDKPVLV
CFMTGKAMED GRRYLEERGI PTFDTPDRAA RALINLIKAG NRLNTGNSNL SAVEKQGYTP
HPLVTQASRE GRNLLEPEAI EVLRDYGIKM QPGRITHSRE EAVRCAQEIG YPVVLKIVSP
QIVHKSDYGG VKLNLQTAEE VGRAYEELIA SVQAKAPTAE IKGVLVTPFV SGGTEVIIGV
LRDNQFGPVV MFGLGGIFVE VFKDVSFRVA PFSREEALSM IAETKAYTLL KGIRGGQPKD
ITALADLLVK IGELAISNPQ VKEMDLNPVA VLEEGFAVLD VRMIIKG
//
