ID W0JKG9_9EURY Unreviewed; 657 AA.
AC W0JKG9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=HALLA_09820 {ECO:0000313|EMBL:AHF99098.1};
OS Halostagnicola larsenii XH-48.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHF99098.1, ECO:0000313|Proteomes:UP000019024};
RN [1] {ECO:0000313|EMBL:AHF99098.1, ECO:0000313|Proteomes:UP000019024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XH-48 {ECO:0000313|EMBL:AHF99098.1,
RC ECO:0000313|Proteomes:UP000019024};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP007055; AHF99098.1; -; Genomic_DNA.
DR RefSeq; WP_049952302.1; NZ_CP007055.1.
DR AlphaFoldDB; W0JKG9; -.
DR STRING; 797299.HALLA_09820; -.
DR GeneID; 25144758; -.
DR KEGG; hlr:HALLA_09820; -.
DR PATRIC; fig|797299.3.peg.990; -.
DR eggNOG; arCOG00249; Archaea.
DR HOGENOM; CLU_010448_2_1_2; -.
DR OrthoDB; 39812at2157; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000019024; 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};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000019024}.
FT DOMAIN 8..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 305..385
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 657 AA; 70638 MW; 8DF2C41DA6634F32 CRC64;
MDIEDINTVA VLGAGNMGHG IAEVAAMAGY DVTMRDINEE FVQNGYEQIE WSLNKLAEND
QLTQDEADAA LERVTPLVDM GEAVGDADIV IEAVPEKMEI KKDVYGDLEA VAPDEAIFAT
NTSSLSITEL SEVTDRPERF CGMHFFNPPV RMPLVEVITG EHTDESVLEV TEALAEDFGK
SPVRVHKDAP GFIVNRILVP LMNEASWLVS NGEATIAEVD STTKFDMGLP MGSFELGDQV
GNDVSYHVLK YMHEVLGDAY EPAPLLEEKV ENEELGKKTG KGFYDYEDGD GVDIPTDEQS
DLVKRRLIAS MANEIAKLIG DDVAPPESID EAVMLGAGFP DGPVTVVDGF GLEAALETLE
AAAEETGHAR YEPAPYLRER AEVGTFYDPA DGDDGVDFEA IRVEYPGEMV GHIVLDRPHR
MNTVSEQLLE EVVDAVELLE DDDDIRAILV TGEGEKAFSA GADIQSMAAG GADPLHGTEL
SKKGQSTFGA LESSDLPVVA GIDGYCLGGG MELATCADLR VASERSEFGQ PELDLGLIPG
WGGTQRLPNI VGEGRAKEII LTADRYDAET MESYGFVNEV CESDDLEDRA FELAASLAGG
PPIAAKYTKR AMLAGRNDTN AGLEYEAAAF GQLMGTDDLM EGITAFMGDG DAEFEGQ
//