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Database: UniProt
Entry: B1TF73_9BURK
LinkDB: B1TF73_9BURK
Original site: B1TF73_9BURK 
ID   B1TF73_9BURK            Unreviewed;       549 AA.
AC   B1TF73;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:EDT37786.1};
DE            EC=5.1.2.3 {ECO:0000313|EMBL:EDT37786.1};
GN   ORFNames=BamMEX5DRAFT_6439 {ECO:0000313|EMBL:EDT37786.1};
OS   Burkholderia ambifaria MEX-5.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT37786.1, ECO:0000313|Proteomes:UP000004814};
RN   [1] {ECO:0000313|EMBL:EDT37786.1, ECO:0000313|Proteomes:UP000004814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEX-5 {ECO:0000313|EMBL:EDT37786.1,
RC   ECO:0000313|Proteomes:UP000004814};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA   Tiedje J., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT   5.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00023693};
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:EDT37786.1}.
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DR   EMBL; ABLK01000385; EDT37786.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1TF73; -.
DR   PATRIC; fig|396597.7.peg.969; -.
DR   Proteomes; UP000004814; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR   PANTHER; PTHR23309:SF9; PEROXISOMAL BIFUNCTIONAL ENZYME; 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; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:EDT37786.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          146..321
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          326..419
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          455..539
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   549 AA;  59047 MW;  4D0F41B9CFF91157 CRC64;
     MLTGRHASAD EALALGLVDR LAHSDDTLAE GLAYAQELVS LGAPARRTRD AQGLADRASA
     QAAIDAARAD LPKKSRGLFS PAKIVDAVEA ALTLSFDAGM KLERSLFLQC IDSPQRAGLV
     HAFFAEREAA KAPEARRASA RPVERIGVVG GGTMGAGIAV AALDAGLPVT MIERDEASLA
     RGRAHVEKVY DGLVAKGRMT PAAHAARLAR FKGSTSYDAL AQADVVIEAV FEDMAVKKAV
     FAELARVCKP GAVLATNTSY LDIDELAASV DRPADVIGLH FFSPANVMKL LEIVVPARVS
     AEVVATAFAL AKQLKKTPVR AGVCDGFIGN RILAVYRTAA DYLMEDGASP YQIDRAVREF
     GFPMGPFQVV DLAGGDIGWA TRKRRAATRD PRARYVEISD RLCERGWFGQ KTARGYYLYP
     DGARVGTPDP EVEAIVADER AKKGITPRAF SDDEILRRYL AALINEGANV VHEKIALRPL
     DVDAVFLHGY GFPRYRGGPM HYADTIGLAN VLADIRAFAK EDPLFWKPSP LIVELVERGA
     DFASLNHID
//
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