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Database: UniProt
Entry: W8F091_9BACT
LinkDB: W8F091_9BACT
Original site: W8F091_9BACT 
ID   W8F091_9BACT            Unreviewed;       802 AA.
AC   W8F091;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:AHJ95971.1};
DE            EC=1.1.1.35 {ECO:0000313|EMBL:AHJ95971.1};
GN   ORFNames=Hsw_0376 {ECO:0000313|EMBL:AHJ95971.1};
OS   Hymenobacter swuensis DY53.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ95971.1, ECO:0000313|Proteomes:UP000019423};
RN   [1] {ECO:0000313|EMBL:AHJ95971.1, ECO:0000313|Proteomes:UP000019423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY53 {ECO:0000313|EMBL:AHJ95971.1,
RC   ECO:0000313|Proteomes:UP000019423};
RA   Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT   "Complete genome sequence of ionizing-radiation resistance bacterium
RT   Hymenobacter swuensis DY53.";
RL   Submitted (JAN-2014) 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   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
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DR   EMBL; CP007145; AHJ95971.1; -; Genomic_DNA.
DR   RefSeq; WP_044000817.1; NZ_CP007145.1.
DR   AlphaFoldDB; W8F091; -.
DR   STRING; 1227739.Hsw_0376; -.
DR   KEGG; hsw:Hsw_0376; -.
DR   PATRIC; fig|1227739.3.peg.643; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_010448_0_0_10; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000019423; Chromosome.
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};
KW   Oxidoreductase {ECO:0000313|EMBL:AHJ95971.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019423}.
FT   DOMAIN          7..205
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          208..307
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   802 AA;  87690 MW;  5F39855ADA0F4D40 CRC64;
     MNRTIKKVAV LGSGVMGSRI ACHFANIGVQ VLLLDIAPKE LLPAEEAKGL KLDNPAVKNR
     IVNASLQAAV AANPSPLYRK QDVSRIKTGN FDDNLKDIAG CDWTIEVVVE RLDIKKGLFE
     RVEQFRKPGT LITSNTSGIP IHMMTEGRSD DFRKHFCGTH FFNPPRYLKL LEIIPTPETD
     KSVVDFLMHY GDLYLGKTTV LAKDTPAFIA NRVGVFAIMD VVQVMSELGL TVEEVDKLTG
     PVIGHAKSAT FRTSDVVGLD TMINVANGLA QNLPNDEAKH VFQLPDFIKK MAENKWLGDK
     TAQGFYKKVK GAGGKSEIQA LDLNTLEYKP SAKVKFATLE ATKPIEKLAD RFKVLAAGKD
     KAGDFYRKTF AGLFAYVSNR IPEITDSLYK IDDALRAGFG WDLGPFETWD ALGVQKGLEL
     AKAEGKTVAP WVEEMVAAGH TAFYKVSEAG VKQFYDIESK SYQAIPGMEN FIILDNLRAT
     GKVLWKNAGA SVLDMGDGIL NVEFHSKMNA LGSDVIQGLL KGVELAEKDF RGLVVGNDAP
     NFSAGANLGL VYMFALDQEY DELNLMIAQF QQAMMRMRYS SIPVVGAPHG LALGGGCELN
     LHCDRVVAAA ETYMGLVEFG VGLIPGGGGT KEMTLRTALK YEEGEPEYNL LRNAFMTVST
     AKVSTSAHEA FDLGFLRRGD EVVVNSNRVL AQAKAAAIEL AEDGYTQPLQ KTNIKVQGKG
     ALGMFLTGVH AMKEGRYISD HDVKIANKLA YIMCGGDLSS PTEVSEQYLL DLEREAFLSL
     TGERKTLERI QSILTTGKPL RN
//
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