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Database: UniProt
Entry: Q8YB80_BRUME
LinkDB: Q8YB80_BRUME
Original site: Q8YB80_BRUME 
ID   Q8YB80_BRUME            Unreviewed;       565 AA.
AC   Q8YB80; D0B659;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:AAL54262.1};
DE            EC=1.1.1.157 {ECO:0000313|EMBL:AAL54262.1};
GN   OrderedLocusNames=BMEII1020 {ECO:0000313|EMBL:AAL54262.1};
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL54262.1, ECO:0000313|Proteomes:UP000000419};
RN   [1] {ECO:0000313|EMBL:AAL54262.1, ECO:0000313|Proteomes:UP000000419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094
RC   {ECO:0000313|Proteomes:UP000000419};
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA   Haselkorn R., Kyrpides N., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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DR   EMBL; AE008918; AAL54262.1; -; Genomic_DNA.
DR   PIR; AC3637; AC3637.
DR   AlphaFoldDB; Q8YB80; -.
DR   KEGG; bme:BMEII1020; -.
DR   eggNOG; COG1250; Bacteria.
DR   Proteomes; UP000000419; Chromosome II.
DR   GO; GO:0008691; F:3-hydroxybutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:AAL54262.1}.
FT   DOMAIN          47..225
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          228..325
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          455..500
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   565 AA;  60713 MW;  860BD20EEB46EDC9 CRC64;
     MAHWRLNERL SSFCSIRKTR KRAQPLSSKN ANLPITDART MERSINHIAI VGAGVMGTGI
     AQIAAQAGLV TQIFDAREGA AAASLDRLAS TLAKLAEKGK ISAEDAQTAV SRIEICSSIQ
     ELADCDLVVE AIVEKLDAKQ ALFLELEAVV SGNCILATNT SSLSVTSIAR VCRHPERVAG
     FHFFNPVPLM KVVEVIDGLT TDPAVGDALL VLAKRMGHHG IRAKDMPGFI INHAGRAYGT
     EALKILGECV APRGDIDRIL RESAGFRMGP LELFDLTGLD VSHPVMESIY NQFYQEPRYR
     PSALTRQMLE GGYVGRKVGQ GFYRYEDGKM VAPPVPQPVP AVDIMPSVWI SADCDEDKEQ
     LYALLRSLGA TVETGALPSA EALCLLAPYG YDATTACELA GSDPARTVCI DMLPGLDRHR
     TLMMTPATSP AFRDAAHALL ARDGVNVTVI RDSVGFVAQR TLAAIVNLAC DIAQQGIATA
     DDIDQAVRLG LGYPQGPLAW GGFSDPENIV AYAGINRRPP LQAKPMVAPQ GRAGPFPALR
     GAGYRLEHFR AKSAKRLRGE ISPLD
//
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