ID K8CSN4_CROSK Unreviewed; 264 AA.
AC K8CSN4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Enoyl-CoA hydratase / 3-hydroxyacyl-CoA dehydrogenase / 3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:CCK07863.1};
DE EC=1.1.1.35 {ECO:0000313|EMBL:CCK07863.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:CCK07863.1};
DE EC=5.1.2.3 {ECO:0000313|EMBL:CCK07863.1};
GN ORFNames=BN128_1839 {ECO:0000313|EMBL:CCK07863.1};
OS Cronobacter sakazakii 696.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=1208664 {ECO:0000313|EMBL:CCK07863.1, ECO:0000313|Proteomes:UP000009356};
RN [1] {ECO:0000313|EMBL:CCK07863.1, ECO:0000313|Proteomes:UP000009356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=696 {ECO:0000313|EMBL:CCK07863.1,
RC ECO:0000313|Proteomes:UP000009356};
RX PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA McClelland M., Furtado M.R., Forsythe S.J.;
RT "Comparative analysis of genome sequences covering the seven cronobacter
RT species.";
RL PLoS ONE 7:e49455-e49455(2012).
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:CCK07863.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CALF01000071; CCK07863.1; -; Genomic_DNA.
DR AlphaFoldDB; K8CSN4; -.
DR Proteomes; UP000009356; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase 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; IPR006180; 3-OHacyl-CoA_DH_CS.
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; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 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.
DR PROSITE; PS00067; 3HCDH; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:CCK07863.1};
KW Lyase {ECO:0000313|EMBL:CCK07863.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CCK07863.1}.
FT DOMAIN 1..37
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 39..133
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 165..250
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 264 AA; 28410 MW; E9891512B8625304 CRC64;
MPLVEVIPHA GTSAETIATT VQLAKKQGKT PIVVADCAGF YVNRILAPYI NEAMRCLIEG
ESIEKIDEAL VKRGFPVGPI QLLDEVGIDV GTKIMPVLER AYGPRFSAPG DAVAAILNDD
RKGRKNGRGF YLYPAKGRKS KKQVDPAVYG LIGVKPGGKL SGEEIAERCV MMMLNEAARC
LDEGVVRSAR DGDIGAVFGI GFPPFLGGPF RYMDTLGAAA ATATLTRLAT RYGDRFTPCD
RLLRMAQTGQ TFWLAGNPQA EMTV
//
