ID A0A1Q4DAN5_9PSEU Unreviewed; 723 AA.
AC A0A1Q4DAN5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:OJY41444.1};
GN ORFNames=BGP03_20115 {ECO:0000313|EMBL:OJY41444.1};
OS Pseudonocardia sp. 73-21.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY41444.1, ECO:0000313|Proteomes:UP000186163};
RN [1] {ECO:0000313|EMBL:OJY41444.1, ECO:0000313|Proteomes:UP000186163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-21 {ECO:0000313|EMBL:OJY41444.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJY41444.1}.
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DR EMBL; MKVV01000079; OJY41444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4DAN5; -.
DR STRING; 1895809.BGP03_20115; -.
DR Proteomes; UP000186163; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 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.
PE 4: Predicted;
FT DOMAIN 16..107
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 452..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 71835 MW; 868D84F497C22649 CRC64;
MRARAPQAPP VGLGALFAPR GVAVVGASRS PAKLGAVMAR SLAGFAGPVA LVNARDPELC
PSVAEAVHRH GPIDLAMICV PAAASAGAVE EAALAGAGAA VVCGGGFAES GPDGERHQAA
LAEVVARTGI RVLGPNTSGF LVPGRGLTAT FVPGVADVPA GRVAVVAASG GVNHALAFLL
AEAGHGVSVA VGLGNGVDVT APDVLDHLAD DPSTAAVALH VESVADGPRL MAAVERLTAT
RPVVALVVGR NDVAAFAQSH TGALATSWRT TRAALRQAGA VLVDDERELV DAVGALSLTR
LAPGATGVGV LTAQAGPGLL LLDDLRGRGA SVPELTGATR SRLGALLPPL THQSNPVDTG
RPDPAFGKVL AAVAADPGVD VVAAYALHEP DALDLAAAVD EADAAVPLVV GVGGAGPAVT
AARAALLARG VPALPDPRGV AAAVAALLAD ARRPAPEDAD SRTRNGRLAH AKPPTRARET
ADSRGVAPRR ESGSPCPRVG VSVSVGRGVG ALDEDLAKGV LDGLGIATMP RVRCSGRAEA
QAALAGLGGP VAVKLLDAAV LHKTEVGGVR LNVRTPEEMD AAADAIGSGS LLVERMAPDG
VDLVVGARRD PVFGPTVLVG LGGTVAEALA DVAVRVAPVA HAAAMVDELA GRALLDGWRG
GPVLDRAALA HVVTALGDLL LDNPHVEDVE INPLRLTADG LVALDAVIVG SHGLEVDDAH
PDR
//
