ID F3PIH6_9BACE Unreviewed; 687 AA.
AC F3PIH6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=CoA binding domain protein {ECO:0000313|EMBL:EGF51515.1};
GN ORFNames=HMPREF9445_02008 {ECO:0000313|EMBL:EGF51515.1};
OS Bacteroides clarus YIT 12056.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF51515.1, ECO:0000313|Proteomes:UP000010321};
RN [1] {ECO:0000313|EMBL:EGF51515.1, ECO:0000313|Proteomes:UP000010321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF51515.1,
RC ECO:0000313|Proteomes:UP000010321};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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:EGF51515.1}.
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DR EMBL; AFBM01000022; EGF51515.1; -; Genomic_DNA.
DR RefSeq; WP_009122134.1; NZ_GL882595.1.
DR AlphaFoldDB; F3PIH6; -.
DR STRING; 762984.SAMN05444376_2179; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_10; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000010321; 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; 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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 489..525
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 687 AA; 74128 MW; 01E9C4E70980D95E CRC64;
MITSQLLHPA SIVVVGASNN VHKPGGAILK NLIHGGYTGE LRAVNPKETE VQGVQAYADV
KDIPDTDLAI LAIPAVLCPD AVELLASEKR VRAFIILSAG FGEETHEGAL LEDRILETAN
RYGASLIGPN CIGLMNTWHH SVFSQPIPNL HPQGVDLISS SGATAVFILE SAVTKGLQFN
SVWSVGNAKQ IGVEDVLQYM DEHFDSEKDS KIKLLYIESI SDPDRLLFHA SSLIKKGCKI
AAIKSGSSES GSRAASSHTG AIASSDSAVE ALFRKAGIVR CYSREELTTV GCIFTLPELK
GKNFAIITHA GGPGVMLTDA LSKGGLNVPK LEGELAEELK SKLFPGAAVG NPIDILATGT
PEHLRLCLEY CEEKFDNVDA VMAIFGTPGL VTMFEMYDVL HEKMQTCKKP IFPILPSINT
AGAEVAAFLA KGHVNFADEV TLGTALSRIV NASKPANNEI ELFGVDVPRI RRIIDSIPGD
GYIEPHYVQA LLHSAGIPVV EEFVSANKEE ALAFARRAGF PVVAKVVGPV HKSDVGGVVL
NIKSEQHLAL EFERMMQIPE VTGIMVQPML KGTELFIGAK YEEKFGHVVL CGLGGIFVEV
LKDVSSGLAP LSYEEAYSMI RSLRAYKIIK GTRGQKGVNE DKFAEIIVRL STLLRFATEI
KEMDINPLLA TEKYVIAVDA RIRIEKN
//
