ID A0A0D5AH67_9NOCA Unreviewed; 707 AA.
AC A0A0D5AH67;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Enoyl-CoA hydratase {ECO:0000313|EMBL:AJW42181.1};
GN ORFNames=NY08_4178 {ECO:0000313|EMBL:AJW42181.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW42181.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW42181.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW42181.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
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: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR EMBL; CP010797; AJW42181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D5AH67; -.
DR STRING; 1564114.NY08_4178; -.
DR KEGG; rhb:NY08_4178; -.
DR PATRIC; fig|1564114.4.peg.4122; -.
DR HOGENOM; CLU_009834_15_3_11; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000032410; Chromosome.
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; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
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 PRINTS; PR00081; GDHRDH.
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.
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 318..496
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 499..599
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 707 AA; 75464 MW; 2862FB935CBEB6C6 CRC64;
MIQWDQDADG IVVLTMDDPN QGANTMNQLY KDSMGATVDR LEAEVDSITG VVITSAKKTF
FAGGDLHTLI AAKPEDAQQV FDEVQEVKGQ LRRIEKLGKP VVSAINGAAL GGGLEIALAT
HHRIAADVPG VQIGLPEVSL GLLPGGGGVA RITRLLGIQT GFMTVLAQGT RFRPAKALEI
GLIHELVGSI DELVPTAKAW IKANPEGGVA PWDVKGYKIP GGTPSNPKLA QILPAFPSNL
RKQIKGAPMP APRAILAAAV EGAQVDFDNA CTIESRYFTE LVTGLVSKNM IQAFFFDLQA
INAGKSRPDG IEKTTFTKVA VLGAGMMGAG IAYVCAKAGI DVVLKDVALE AAQKGKAYSE
AIEAKALSRG KTTQEKSDAL LARIHPTADA KDVEGADLVI EAVFESEELK QKVFQEIEDL
VDPTALLGSN TSTLPITSLA QGIKRQEDFI GIHFFSPVDK MPLVEIIRGE KTSDAALAKA
FDLVQIIKKT PIVVNDSRGF FTSRVIGTFI NEAIAMLGEG VEPSTIEQAG LQAGYPAAPL
QLSDELTLNL MQKIRKETYD ALIAAGQTPP EDPAGAVIDK MVDEFERPSK AKGAGFYEYE
DGKRTGLWPG LRDAFKSGSA DIPFEDLKER MLFIEAIETQ KCFDEGVLNT TADANIGSIF
GIGFPAWTGG VHQYVVGYPG GQAGFVTRAD ELAKKYGDRF QVPASLR
//
