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Database: UniProt
Entry: R0D381_CAUVI
LinkDB: R0D381_CAUVI
Original site: R0D381_CAUVI 
ID   R0D381_CAUVI            Unreviewed;       292 AA.
AC   R0D381;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:ENZ83081.1};
GN   ORFNames=OR37_00855 {ECO:0000313|EMBL:ENZ83081.1};
OS   Caulobacter vibrioides OR37.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ83081.1, ECO:0000313|Proteomes:UP000013063};
RN   [1] {ECO:0000313|EMBL:ENZ83081.1, ECO:0000313|Proteomes:UP000013063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR37 {ECO:0000313|EMBL:ENZ83081.1,
RC   ECO:0000313|Proteomes:UP000013063};
RX   PubMed=23792749;
RA   Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA   Palumbo A.V., Brown S.D.;
RT   "Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
RT   Tolerant to Heavy Metals.";
RL   Genome Announc. 1:0-0(2013).
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009463}.
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:ENZ83081.1}.
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DR   EMBL; APMP01000003; ENZ83081.1; -; Genomic_DNA.
DR   RefSeq; WP_004616184.1; NZ_APMP01000003.1.
DR   AlphaFoldDB; R0D381; -.
DR   STRING; 1292034.OR37_00855; -.
DR   PATRIC; fig|1292034.3.peg.849; -.
DR   eggNOG; COG1250; Bacteria.
DR   OrthoDB; 9771883at2; -.
DR   Proteomes; UP000013063; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR022694; 3-OHacyl-CoA_DH.
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; IPR013328; 6PGD_dom2.
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; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PIRSF; PIRSF000105; HCDH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          6..179
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          188..283
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   BINDING         11..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         93
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         144
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         275
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   SITE            141
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   292 AA;  31358 MW;  765302F1300FA30A CRC64;
     MSEIKTVGVI GAGQMGSGIA HVVALGGYDV RLHDVSRERI EAGIAVIEKN MARQVGRGII
     DDAAMKAALA RIQPAEGLEA VGAADLAIEA ATENEEIKKS IFRSLQPHLK DGTLLASNTS
     SISITRLASA TDRPERFIGL HFMNPVPLMK LVEIIRGIAT DVPTYETAVA FAKSLGKITS
     NAEDFPAFIV NRVLVPMINE AIYTLYEGVG TVDAIDTAMK LGANHPMGPL ELGDFIGLDT
     VLSIMNVLHE GLADSKYRPC PLLVKYVEAG WLGKKTGRGF YDYRGETPVP TR
//
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