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Database: UniProt
Entry: A0A285HNX3_9RHOB
LinkDB: A0A285HNX3_9RHOB
Original site: A0A285HNX3_9RHOB 
ID   A0A285HNX3_9RHOB        Unreviewed;       697 AA.
AC   A0A285HNX3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:SNY36391.1};
GN   ORFNames=SAMN06297129_0162 {ECO:0000313|EMBL:SNY36391.1};
OS   Pseudooceanicola antarcticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=1247613 {ECO:0000313|EMBL:SNY36391.1, ECO:0000313|Proteomes:UP000231655};
RN   [1] {ECO:0000313|EMBL:SNY36391.1, ECO:0000313|Proteomes:UP000231655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12662 {ECO:0000313|EMBL:SNY36391.1,
RC   ECO:0000313|Proteomes:UP000231655};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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}.
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DR   EMBL; OBEA01000001; SNY36391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285HNX3; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000231655; 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}.
FT   DOMAIN          296..471
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          476..570
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          604..688
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   697 AA;  73596 MW;  DCAA09388B448173 CRC64;
     MPDGVVGEVV TTEVVGDVAL VCIDNPPVNA SGHAVRVGLV GAIEALNAEA GVKAIAIWCA
     GRTFMAGADI REFGKPSKEP VLPEVYNILE ASEIPVVAVM HGTALGGGFE LGLAAHARVA
     IAGSKVGLPE VLIGLLPGAG GTQRLPRLAG VDFALDMSLS GRQVSVEEAQ AAGAIDRVVE
     GNPRDVALSM AQEVVAGTLP TRRTSEISIE IDHTALDGIR AATQKKSPHL VNPLKCIDAI
     AAADQPIAEG LKVERQCFLD CMETPQRAGL IHAFFGERAV SNIPEAKGET RDIQSVGVIG
     GGTMGSGIAT ACLLAGLPVT LVEVAQEGLD RGVATITKNL EGAVSRGKMS EAKKEAALAS
     LSPALELDAL ADVDLVIEAV FEDMGVKREI FGKLDAICKP DAVLASNTSY LDVNEIAEST
     SRPGDVLGLH FFSPAHVMRL LEIVQGKQTA PDVLATGFAL AKRLRKVGVL AQVCDGFIGN
     RILAHYALCS GYLVLDGASP AQVDAALEGF GFAMGPHKVG DLAGLDIGWM TRKRKAATRD
     PAERYAGQIP DRICENGWFG RKTGKGYYLY EGGAPVPNPE VATIIDEVRA EQGITPKSFT
     DDEIVERYMT AMISEAARVV EDGTAKRPLD VDMVFLFGYG FPRFRGGPLH YADTLGAAEL
     VARIERYAEE DPHYWQVPDI LHRMAADGTS FADLNKG
//
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