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Database: UniProt
Entry: H1RZ79_9BURK
LinkDB: H1RZ79_9BURK
Original site: H1RZ79_9BURK 
ID   H1RZ79_9BURK            Unreviewed;       808 AA.
AC   H1RZ79;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:EHP44452.1};
GN   ORFNames=OR16_03042 {ECO:0000313|EMBL:EHP44452.1};
OS   Cupriavidus basilensis OR16.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP44452.1, ECO:0000313|Proteomes:UP000005808};
RN   [1] {ECO:0000313|EMBL:EHP44452.1, ECO:0000313|Proteomes:UP000005808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR16 {ECO:0000313|EMBL:EHP44452.1,
RC   ECO:0000313|Proteomes:UP000005808};
RX   PubMed=22461549; DOI=10.1128/JB.06752-11;
RA   Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA   Nagy I., Horvath B., Nagy I., Kukolya J.;
RT   "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL   J. Bacteriol. 194:2109-2110(2012).
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   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
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:EHP44452.1}.
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DR   EMBL; AHJE01000007; EHP44452.1; -; Genomic_DNA.
DR   RefSeq; WP_006156437.1; NZ_AHJE01000007.1.
DR   AlphaFoldDB; H1RZ79; -.
DR   PATRIC; fig|1127483.3.peg.617; -.
DR   OrthoDB; 5287258at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000005808; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd06558; crotonase-like; 1.
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; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 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   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          8..191
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          194..293
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   808 AA;  86153 MW;  9E5A426EF3F3252B CRC64;
     MSNFIVKKVA VLGAGVMGAQ IAAHLVNARV PVVLFDLPAK EGPKNGISLR AIENLKKLSP
     APLGIKDEAG LIQAANYEDD LALLKECDVV IEAIAERMDW KHDLYKKVAP HLASHTIFAT
     NTSGLSITAL SDGFDADLKS RFCGVHFFNP PRYMHLVELI PTATTQPAIL DRLETFLTSA
     LGKGVVRAKD TPNFIANRVG IFSILAVFAE AEKYGIPFDV VDDLTGSKLG RAKSATFRTA
     DVVGLDTMAH VIKTMQDTLQ DDPFAPVYKT PAVLKALVDA GALGQKTGAG FYKKEGKAIK
     VMDPTTGQYV DAGKKADEIV VRMLKKEPAE RIKLLRESTN PQAQFLWAVF RDVFHYIGVY
     LEQIAGSAAD IDLAIRWGFG WNSGPFEDWQ SAGWKQVAEW VKEDIDAGKG LSSAALPSWV
     FEGPVADNQG VHGAQGSWSP AAQAFVQRNA LPVYERQVFR AAVKGTAAAD PRKAGRTVEE
     NDAVRIWVSE GQDDVLVVSF KSKMNTIGPD VIDGLTRAID LAQAEYKGLV VWQPTSLQLG
     APGGPFSAGA NLEAAMPAFM MGGAKGIEPF VKKFQDGMMR VKYSAVPVVS AASGIALGGG
     CELMLHSAKR VAALETYIGL VEVGVGLVPA GGGLKEAALA AARAAQAAGS TNYLQFLTNR
     FQAAAMAKVS ASALEAQKMG YLQPSDTIVY NVHELLYVAQ GEVRALANAG YRAPVPGTLV
     PVAGRSGIAT IKASLANMRD GGFISAHDFL IASRIAEAVC GGDVEAGSLV SEEWLLALER
     KAFVDLLGTG KTQERIMGML QTGKPVRN
//
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