ID A0A235G935_9NOCA Unreviewed; 905 AA.
AC A0A235G935;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:OYD69727.1};
GN ORFNames=BDB13_3301 {ECO:0000313|EMBL:OYD69727.1};
OS Rhodococcus sp. OK302.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1882769 {ECO:0000313|EMBL:OYD69727.1, ECO:0000313|Proteomes:UP000215121};
RN [1] {ECO:0000313|EMBL:OYD69727.1, ECO:0000313|Proteomes:UP000215121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK302 {ECO:0000313|EMBL:OYD69727.1,
RC ECO:0000313|Proteomes:UP000215121};
RA Pelletier D.;
RT "Populus root and rhizosphere microbial communities from Tennessee, USA.";
RL Submitted (AUG-2017) 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:OYD69727.1}.
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DR EMBL; NPJZ01000001; OYD69727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235G935; -.
DR Proteomes; UP000215121; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR000182; GNAT_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; PF00583; Acetyltransf_1; 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; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 45..199
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 692..730
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 95686 MW; 955BC981DAD847A0 CRC64;
MTEQSDTEPT VSEPTPPNVA PAPDAAHDYP HSWVVDVLAS DGGAVALRPI VPEDADKLVE
FHGKLSERTR YLRYFGPYPT MSQKDVKNFT TVDHHNRVAF VMMLGDEIIA VGRYERLLDI
GDGKSAEVAF VVADAHQGRG LGPILLEYLA AAAAENGLTM FVAEVLSENR NMVTVFREAG
YQVSRSFDGG VLRLEFAIDP TEALVSVRNS RERAAEARSM GNVLRPRSVA VIGASADPAK
VGNAVLTNLL RGGFTGPVYP VNAEHRSVHG VRAYKTVREI PDDVDLAVVA VPAESINSVL
DDCLDKGVKA LVVVSSGFSD SGPDGRASER KLVHAARAHG MRLIGPNALG VANNDPSISL
NATLAPVLPA AGNVGFFCQS GALGIAILDE AARSRIGLSA FVSAGNRADV SGNDLLQYWD
SDQTTEVVLL YLESFGNPRK FSRIARRVAR KKPIVAVKSG RHAVPPVLAA TGVEIDDSVV
RALFEQAGVI QVGSISQLFD CALLFGYQPL PAGPRLAVIG NSTALGVLAA DAARSEGLQV
SDPIDLGAQA SPELFASAVR DALGSFDVDA VIAVFVPPVA IPVEPFAKAL KDAVAGSDKP
ILTTFLAAEG VPEVLTIRDD AGNPTRGSVP SYPGPERAAL ALARAWRYAE WRSKPASKVV
RPAGIDSERA RAMVADWLEN SPGRWLSDVE AAALLACYGV DVVEFRSVLS EDEAVEAADA
LGYPVVVKAT GELWRHRPDL GGVRLDLVGP DSVRLAYSDL AAASGEPLLH VQKMAPKGIG
CVVAVQDDPS FGSLISFGLA GVISDLLGDR AYRVLPLTED AATELIDAPK AAPLLSGYRN
AVPVNKAALV DLVQRISTLA DDIPEVREMA CEPVLASAIG AEITDARVRI GPEPSAVDLG
PRRLR
//
