ID A0A1H3MIL1_9BURK Unreviewed; 724 AA.
AC A0A1H3MIL1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=SAMN04515617_12155 {ECO:0000313|EMBL:SDY76542.1};
OS Collimonas sp. OK242.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1798195 {ECO:0000313|EMBL:SDY76542.1, ECO:0000313|Proteomes:UP000198586};
RN [1] {ECO:0000313|EMBL:SDY76542.1, ECO:0000313|Proteomes:UP000198586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK242 {ECO:0000313|EMBL:SDY76542.1,
RC ECO:0000313|Proteomes:UP000198586};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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; FNOR01000021; SDY76542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3MIL1; -.
DR STRING; 1798195.SAMN04515617_12155; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000198586; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00725; 3HCDH; 1.
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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 327..505
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 508..608
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 724 AA; 78262 MW; 896895E303662C6A CRC64;
MADYPAPDTL ESQIMSVNFQ KDADNIVTLT LDMPGRSMNV LNEALTAPFM AAIANIEADP
AIAGVIITSG KADFVAGADI EKLFQITEAQ AAFDLAQEFK GLLRRLELCG RPVVAALNGT
ALGGGLELAL ACHYRIAIDN PKAKFGLPEV KLGLLPGGGG TQRLPRMIGI QSALQLMLEG
KELRAEEALQ QGIVQELASD REDLLARAKA WCLANPKAKQ PWDDKKFRWP GGDSRSPGNG
QLWAIAPSMA SAKTHGNYPA ATNIMSCVFE GGIVDFDTGC EIESRYFVNC ALSPVAKNMI
GTLWFQLNAI NKGKSRPQGI APSKVRKVGI LGAGMMGAGI AYASAKAGIE VVLLDNSMAT
AESGKDYSGK LLDKAIRRKQ QTAEGKETLL NRIRPTVDFN DLASCDLIIE AVFEDRQVKA
EVTRKTEALI SPDAVFASNT STLPITGLAQ ASVRPENFIG LHFFSPVDKM PLVEIIIGQH
TSPQTLARGF DYVQQIKKTP IVVNDSRGFY TSRVFGTYVM EGLKLLMEGQ HPRAIEMAGL
QAGMPVGPLA VHDEVSLSLS LHILEQTRKD FAAAGQTFAG HPADPGLEKM VKQLDRKGKK
AGKGFYDYPE NASKHLWPGL QQAFPLAATQ LPQKDLIERM MFVQANEAAK CYEEKVVMTV
ADTNIGSIFG WGFAPFQGGA LQYINAYGVA NFVKRAHQLS AQFGSYFAPA AILVKMAEQG
KHFE
//
