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Database: UniProt
Entry: A0A2T6KR07_9RHOB
LinkDB: A0A2T6KR07_9RHOB
Original site: A0A2T6KR07_9RHOB 
ID   A0A2T6KR07_9RHOB        Unreviewed;       696 AA.
AC   A0A2T6KR07;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:PUB18989.1};
GN   ORFNames=C8N45_101580 {ECO:0000313|EMBL:PUB18989.1};
OS   Yoonia sediminilitoris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Yoonia.
OX   NCBI_TaxID=1286148 {ECO:0000313|EMBL:PUB18989.1, ECO:0000313|Proteomes:UP000244523};
RN   [1] {ECO:0000313|EMBL:PUB18989.1, ECO:0000313|Proteomes:UP000244523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29955 {ECO:0000313|EMBL:PUB18989.1,
RC   ECO:0000313|Proteomes:UP000244523};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (APR-2018) 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}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|RuleBase:RU003707}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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:PUB18989.1}.
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DR   EMBL; QBUD01000001; PUB18989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6KR07; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000244523; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
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   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.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
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   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244523}.
FT   DOMAIN          293..469
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          474..567
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          603..688
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   696 AA;  73918 MW;  FA18BCC4C73C1520 CRC64;
     MASVTYEIVQ NVATITVDNA PVNALSHAVR QGLSDAFARF ENDPDARVAV VVGAGRLFLG
     GADISEFGKP SQPPILPDVI NQIEACSKPV VAGIHGAALG GGLEVALGAH YRIARAGTKL
     GLPEVKLGLL PGAGGTQRLP RLVGLDPAID MITSGAPVLA DRARDIGLID RVDTGNDICA
     AAQAYAQELL QTGAPVRPVS GLGVQQADEL LADRRAKLAK TARGEVAALV ALDAVDAATK
     LPFAEGLAEE RRLFLYLIDT PQRAGMIHAF FAERAVAKLP EIKGVAPRGF ARIGVIGGGT
     MGAGIATSAV LNNMRVTLVE RDKDAADRAH ATITRNLGSA MKRGKLDQAG YDRILNDNLR
     TVVGYGALSD ADLVIEAVFE DMAVKKEVFA ELDRVLPQGA ILATNTSYLD VNEIAGATSR
     PADVIGLHFF SPAHIMKLLE VVVADKTAPD VTATAFALAK TLGKAAVRAG VCDGFIGNRI
     LSHYRAAADH MVLDGASPYQ IDKALTDFGF AMGPYQVSDL AGLDIGYATR QRKLATAHPR
     DRAPTFADAL FHAGRLGQKT GRGYYIYDSD SPKGRSDPEL EAIVTQARSD AGITPRRFSD
     DEIVHRYMAA MVNEGARVVT EGIAQRPSDV DVVFLYGYGF PRWRGGPMKY ADMQGLDVIL
     ADIQGFAKDD NHFWTPAPLL TQLVAEGRNF DSLNKA
//
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