ID B0R5C0_HALS3 Unreviewed; 659 AA.
AC B0R5C0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN Name=hbd2 {ECO:0000313|EMBL:CAP13937.1};
GN OrderedLocusNames=OE_2871F {ECO:0000313|EMBL:CAP13937.1};
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=478009 {ECO:0000313|EMBL:CAP13937.1, ECO:0000313|Proteomes:UP000001321};
RN [1] {ECO:0000313|EMBL:CAP13937.1, ECO:0000313|Proteomes:UP000001321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1 {ECO:0000313|Proteomes:UP000001321};
RX PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009463}.
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 -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM774415; CAP13937.1; -; Genomic_DNA.
DR RefSeq; WP_010902952.1; NC_010364.1.
DR AlphaFoldDB; B0R5C0; -.
DR EnsemblBacteria; CAP13937; CAP13937; OE_2871F.
DR GeneID; 68694058; -.
DR KEGG; hsl:OE_2871F; -.
DR HOGENOM; CLU_010448_2_1_2; -.
DR PhylomeDB; B0R5C0; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001321; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProt.
DR GO; GO:0004300; F:enoyl-CoA hydratase 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; 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; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 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; PS00067; 3HCDH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAP13937.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:CAP13937.1}.
FT DOMAIN 9..188
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 191..286
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 304..386
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 659 AA; 70012 MW; 14502A2DFB258CEF CRC64;
MDVDDIHSIA VLGAGNMGHG IAEVAAMAGY TVRLRDISAE LVQDGYDQIE WSLGKLAESD
QLTEAAADAA LDRISTHVEV SDAVDDVDVV IEAVPEKMEI KTDVYTEVEA HAPADAVFAT
NTSSLSITDL SEVTERPARF CGMHFFNPPV RMELVEVISG AHTDDAVLEC IESLAADFGK
TPVRVRKDSP GFVVNRILVP LLNEAAWLVH DDEATIAEVD STTKYDMGLP MGAFELADQV
GIDVSHDVLD YMQDVLGTAY EPCPVLVDHV EAGDLGRKSG AGFYDYGDDA AGADVPTDAI
RADIADRLTA VMANEVAKLV GGGVADPAEI DEAVMLGAGY PEGPAKMADA AGITYLHETL
VAAHEATGQA RYEPADTLAE MAAAGESFHG RGDEDADGRR EFDAVSVSVD GNVGHIELDR
PHRMNTISGE LLADLSDAID VLGDDDDVRA VLLTGAGEKA FSAGADVTSM AGNADPVEAV
ELSRMGQQTF GKLEAADEPV VAAIDGYCLG GGMELATCAD MRLASERSEL GQPEHDLGLL
PGWGGTQRLK HIVGEGRAKE IIFTADRFAP ETLADYGFIN EVVTTEAFEE RAWELARDLA
AGPPIAMKYT KRAMRAGRDD TDAGLEIEAQ SFGQLMNTQD LMEGVSAFSA DREPEFNGE
//
