ID M0JJF0_HALVA Unreviewed; 654 AA.
AC M0JJF0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=C437_08631 {ECO:0000313|EMBL:EMA08089.1};
OS Haloarcula vallismortis ATCC 29715.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662477 {ECO:0000313|EMBL:EMA08089.1, ECO:0000313|Proteomes:UP000011534};
RN [1] {ECO:0000313|EMBL:EMA08089.1, ECO:0000313|Proteomes:UP000011534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29715 {ECO:0000313|EMBL:EMA08089.1,
RC ECO:0000313|Proteomes:UP000011534};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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 -!- 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:EMA08089.1}.
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DR EMBL; AOLQ01000033; EMA08089.1; -; Genomic_DNA.
DR RefSeq; WP_004516522.1; NZ_AOLQ01000033.1.
DR AlphaFoldDB; M0JJF0; -.
DR PATRIC; fig|662477.6.peg.1658; -.
DR OrthoDB; 39812at2157; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000011534; 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}.
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 304..383
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 654 AA; 70717 MW; A3131F9833489300 CRC64;
MDFEDIDTIA VLGAGNMGHG ITEVAALAGY DVRMRDIKDE FVGDGYDNIE WSLNKLAERD
QLTQDEADAA LDRVTPLVDV EEAVSDVDVV IEAVPEKMEI KKDVYTEVEE HAPEDAIFAT
NTSSLSITEL SEVTERPEQF CGMHFFNPPV RMQLVEVISG AHSSDETLDA IEALAEDFGK
TPVRVRKDSP GFIVNRILVP LMNEAAWLVH SDEATIAEVD STTKFDMGLP MGSFELSDQV
GNDVGLHVLE YMHEVLGEPY APCPLLEEKV ENEELGKKTG KGFYDYENGG VDIPTDAGRE
DVKHRLVAVM ANEVGKLVEN DVAPVGDIDQ AVQLGGGFPD GPAKIADKTG LEALVDTLEE
THEETGAERY AVSDGLREAA EDGGFYSTED DTPAEFDNVT VEYPGDMVGH IELDRPHRMN
TVSPELMDDL ADAVDLLEDD DEVRAILLTG AGDKAFSAGA DVQAMASNAT PLDAIELSRK
GQETFGKLEE CSMPVVAGID GYALGGGMEL ATCADLRVAS ERSELGQPEH NLGLLPGWGG
TQRLARIVGE GRAKEIIFTG DRYDADEMAE FGFINEVVDN ESLHEQALEL ARDMAAGPPV
AQKLTKRAML AGRDDIDAGL EVESQAFGHL IGTDDVMEGI NAFMGDGEPD FEGK
//
