ID A0A0N0N7T8_9ACTN Unreviewed; 685 AA.
AC A0A0N0N7T8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=CoA-binding domain protein {ECO:0000313|EMBL:KPI23391.1};
GN ORFNames=OV320_0906 {ECO:0000313|EMBL:KPI23391.1};
OS Actinobacteria bacterium OV320.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI23391.1, ECO:0000313|Proteomes:UP000037870};
RN [1] {ECO:0000313|EMBL:KPI23391.1, ECO:0000313|Proteomes:UP000037870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV320 {ECO:0000313|EMBL:KPI23391.1,
RC ECO:0000313|Proteomes:UP000037870};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-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:KPI23391.1}.
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DR EMBL; LJCX01000033; KPI23391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0N7T8; -.
DR PATRIC; fig|1592329.3.peg.8710; -.
DR Proteomes; UP000037870; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037870}.
FT DOMAIN 478..514
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 685 AA; 70202 MW; 40972C2C854C05D3 CRC64;
MSSLDALFAP RAIAVLGASA TPGKLGAAMA DSLASFPGPV MKVNSGRLQQ DRGFFRTVGE
AATAHGVTPD LVVSCIPAAV TADALREAAA VGARAALVCA GGFAEAGREG ALHQQALAEV
ARDTGIRVLG PNTSGFLAPH RRLTASFVPG APDLEPGPVA VVAASGGVNH ALAFALAEAG
VGLRLGVGLG NSLDVTQGDV LRHLAEDDGV RAVALAVETA AEGRRLTEAV RRLTDRVPVV
ALVVGRSDIG DFARSHTGAL ATSWRVTRTA LRQAGAVLVD DERDLVDAVT ALSRVRLPAN
PRPGIGLVTA QAGPGLLLTD DLRSHGIQVP PLVERTVKEL RGLLPALTYL NNPVDTGRPS
PVLTQVVERV SEDPGIDVTA VYGLLEPTAV DLPAALTAAR TATPLVAVVG GPVEQARRTR
RELGEAGIPC AATPASGSVM VRALVEDAAA RTRREAVVTA TAAPTLPPPG PVDEHTAKGV
LADLGIRTPV RRVCADPAAA HAALDELGGP VVVKILDAEI LHKTEVGGVQ VGIRTHEELD
EALARMPASP ALLVEQMAPA GPELIVGVRR DPVFGPVVAL GAGGTAAEIL GDVSLRLAPL
SGIEAHAMLD ELATRQMFLG ARGATPVDRA RLTHVLLALA SLAAENSVAE CEINPLRVLP
DGDIVALDAV LMLRDPRDQG GSDDA
//
