ID   B4EUX9_PROMH            Unreviewed;       886 AA.
AC   B4EUX9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Acyl-CoA synthetase/acetyltransferase {ECO:0000313|EMBL:CAR41007.1};
GN   OrderedLocusNames=PMI0398 {ECO:0000313|EMBL:CAR41007.1};
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR41007.1, ECO:0000313|Proteomes:UP000008319};
RN   [1] {ECO:0000313|EMBL:CAR41007.1, ECO:0000313|Proteomes:UP000008319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320 {ECO:0000313|EMBL:CAR41007.1,
RC   ECO:0000313|Proteomes:UP000008319};
RX   PubMed=18375554; DOI=10.1128/JB.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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DR   EMBL; AM942759; CAR41007.1; -; Genomic_DNA.
DR   RefSeq; WP_004252258.1; NC_010554.1.
DR   AlphaFoldDB; B4EUX9; -.
DR   EnsemblBacteria; CAR41007; CAR41007; PMI0398.
DR   GeneID; 6800346; -.
DR   KEGG; pmr:PMI0398; -.
DR   eggNOG; COG0045; Bacteria.
DR   eggNOG; COG0456; Bacteria.
DR   eggNOG; COG1042; Bacteria.
DR   HOGENOM; CLU_007415_0_2_6; -.
DR   Proteomes; UP000008319; Chromosome.
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          487..523
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          726..881
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   886 AA;  98777 MW;  5709365422CF7763 CRC64;
     MSQRGLEALL RPKSIAVIGA SDKVGRAGTT MMKNLLSGGF NGPVFPVNPT RNSVSGVFTY
     PSIDKLPQVP DLAIICTHHR RNLELLEQLG QSGCKAVIVL SAQSEQFQAI KTLCQQYHIR
     LLGPNSLGLL APWQGLNASF SPLPVKKGKL AFISQSAAVA NTILDWAYYR NIGFSYFIAL
     GDNQDIQVDD LLDFLARDSK TSAILLHLEH IHDARRFMSA SRSASRNKPI LVIKSGRTQK
     AQLLLGDTPS YDVAYDAAFQ RAGLLRVQDT HEMFSAVETL SYMTPLKGEK LMIISNGSAP
     AAMAVDELFL QSGKLAQLSA DTQQQLQAIV QDTSAIRNPL NLGDDTTVER YIRAVNCLLD
     SHDHDALLLI HTPSAIAPSI ETAQKVIEAI NKHPRRKWLT LFTNWGGEYS SQQSRKLFSE
     AGIPTYRTPE GAITAFMHMV EYRRNQKQLK ETPALPLEIK MNTQQAHRCI EDALDKKQYR
     LDTHQVQPIM EAYGFNTLPT WIAHNAQEAV SIAEKIGYPV ALKLRSPDIP HKSEVQGVML
     YLRDSNEVES AAHAIIERVS ELYPQAKIQG LLVQSMANRA GSQELRVAIE QDPIFGPLIL
     LGEGGVEWQI ETKAAVALPP LNMALARYLV INAIKSGKLQ PRSALQPLNI LSLSHFLVQV
     SHLLLDCPQI VRLDIHPLLV SGNDFTLLDV AMELSPIEGD PHQKLSIRPY PNELEETFFL
     RDSKPCFIRP ILPEDEPLLK TFINQVTKED LYYRYFSEIS EFTHDDLANM TQIDYDREMA
     FVAIRHPHDD PEIIGVARAM ADPDNQQAEF AILVRSDLKG NTLGHQLMMK LINYTKAHGI
     KRLTAITMPE NRNMISLAKK LGFSVEVQFD EGIVNLNLLL DPLSDV
//