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Database: UniProt
Entry: U0EHJ8_9NOCA
LinkDB: U0EHJ8_9NOCA
Original site: U0EHJ8_9NOCA 
ID   U0EHJ8_9NOCA            Unreviewed;       901 AA.
AC   U0EHJ8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=CoA-binding protein {ECO:0000313|EMBL:ERB52903.1};
GN   ORFNames=N806_17275 {ECO:0000313|EMBL:ERB52903.1};
OS   Rhodococcus sp. P27.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1384060 {ECO:0000313|EMBL:ERB52903.1, ECO:0000313|Proteomes:UP000016008};
RN   [1] {ECO:0000313|EMBL:ERB52903.1, ECO:0000313|Proteomes:UP000016008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P27 {ECO:0000313|EMBL:ERB52903.1,
RC   ECO:0000313|Proteomes:UP000016008};
RX   PubMed=24072865;
RA   Gouvea Taketani R., Domingues Zucchi T., Soares de Melo I., Mendes R.;
RT   "Whole-Genome Shotgun Sequencing of Rhodococcus erythropolis Strain P27, a
RT   Highly Radiation-Resistant Actinomycete from Antarctica.";
RL   Genome Announc. 1:e00763-13(2013).
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:ERB52903.1}.
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DR   EMBL; AVCO01000027; ERB52903.1; -; Genomic_DNA.
DR   AlphaFoldDB; U0EHJ8; -.
DR   PATRIC; fig|1384060.5.peg.3170; -.
DR   Proteomes; UP000016008; 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          41..195
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          688..726
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   901 AA;  95057 MW;  D0D4FDF2092FD778 CRC64;
     MTEQSDTDAG GASDQAPKTD PAHTYPHSWV VDVLASDGGA VALRPIVPED ADKLVEFHGK
     LSERTRYLRY FGPYPTMSAR DVKNFTTVDH HNRVAFVMML GDEIIAVGRY ERLLDVGDGK
     SAEVAFVVAD AHQGRGLGPI LLEYLAAAAA ENGLTMFVAE VLSENRNMVT VFREAGYQVS
     RSFDGGVLRL EFAIDPTEAL VSVRNSRERA AEARSMGNVL SPRSVAVIGA SADPAKVGNA
     VLTNLLRGGF TGPVYPVNAE HRSVHGVRAY PTVRDIPDDV DLAVVAVPAE SINSVLDDCL
     DKGVKALVVV SSGFSESGPD GRSSERKLVH AARAHGMRLI GPNALGVANN DPAISLNATL
     APVLPVAGNV GFFCQSGALG IAILDEAARS RIGLSAFVSA GNRADVSGND LLQYWDSDQS
     TEVVLLYLES FGNPRKFSRI ARRVARKKPI VAVKSGRHAV PPVLAATGVE IDDSIVRALF
     EQAGVIQVGS ISQLFDCALL FGYQPLPAGP RLAVIGNSTA LGVLAADAAR SEGLQVSDPV
     DLGAQASPEL FAAAVRDALA SFDVDAVIAV FVPPVAIPVE PFAKALKDAV AGSDKPILTT
     FLAAEGVPDV LAVRDEVGNP TRGSVPSYPG PERAALALAR AWRYAEWRSK PASKVVRPAG
     IDSERAQKMV AAWLENSPGR WLSDVEAAAL LECYGVAVVE FRSVLSEDEA VEAADAVGYP
     VAVKATGEMW RHRPDLGGVR LDLSGPESVR LAYRDLAAAS GEPLLHVQKM ATKGIGCVVG
     VQDDPSFGSL ISFGLAGVIS DLLGDRAYRV LPLTEDAATE LIDAPKAAPL LSGYRNAVPV
     NKGALVDLVQ RISALADDIP EVRELACEPV LASATGAEIT DSRVRIGPEP SAIDLGPRRL
     R
//
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