ID A0A1M5V291_9EURY Unreviewed; 659 AA.
AC A0A1M5V291;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=SAMN05443636_3215 {ECO:0000313|EMBL:SHH69296.1};
OS Halobaculum gomorrense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halobaculum.
OX NCBI_TaxID=43928 {ECO:0000313|EMBL:SHH69296.1, ECO:0000313|Proteomes:UP000184357};
RN [1] {ECO:0000313|EMBL:SHH69296.1, ECO:0000313|Proteomes:UP000184357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9297 {ECO:0000313|EMBL:SHH69296.1,
RC ECO:0000313|Proteomes:UP000184357};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQWV01000014; SHH69296.1; -; Genomic_DNA.
DR RefSeq; WP_073311457.1; NZ_FQWV01000014.1.
DR AlphaFoldDB; A0A1M5V291; -.
DR STRING; 43928.SAMN05443636_3215; -.
DR OrthoDB; 51300at2157; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000184357; Unassembled WGS sequence.
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:UP000184357}.
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 307..385
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 659 AA; 71185 MW; A94BFE1855DCA945 CRC64;
MDVDDVETVA VLGAGNMGHG IAEVAALAGF DVTLRDINEE FVQNGYNQIE WSLDKLAEKD
QISEEDADAA LDRVTPVVPV ADAVAEADLV IEAVPEKMDI KKDVYAEVEE HAPDRAVFAS
NTSSLSITEL SEVTDREERF CGMHFFNPPV RMQLVEVISG AHTSAGTMDL VEAVAERMGK
TPVRVRKDSP GFIVNRVLVP LMNEAAWLVH EGEATVESVD STTKYEMGLP MGSFELADQV
GIDVGVHVLE YMHEVLGDAY EPCPLLTEKV EDEHLGKKTG KGFYDYEDGP GAEVPSDEAD
EGVKHALLAV MANEVAGLIG NDVADAGDID QAVKLGAGFP DGPAKMADAV GLDALLSTLD
ERREETGAER YEAVDYLREL VEEGRGFYAD TDGEDDDGVD FETIRIEREG RVGHIVLDRP
HRMNTISEEL LDELGVAIEE LEADDGVRAV LVTGEGERAF SAGADVQSMA AGGGDPLHAV
ELSRKGQSTF GKFESSDLPV VAGIDGYCLG GGMEFATCAD LRVASERSEL GQPEHNLGLL
PGWGGTQRLR HIVGEGRAKE IIFTAERYDA ETMERYGFVN EVVGNDELLD HAMDIAQDLA
AGPPVAQRYT KRAMHAGRDD TDAGLEIEAQ AFGQLMNTED LMEGVMAFMS DEEPAFEGK
//
