ID E1SKS4_PANVC Unreviewed; 727 AA.
AC E1SKS4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN Name=fadB {ECO:0000313|EMBL:ADO11574.1};
GN OrderedLocusNames=Pvag_3442 {ECO:0000313|EMBL:ADO11574.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO11574.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO11574.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO11574.1,
RC ECO:0000313|Proteomes:UP000006631};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
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}.
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DR EMBL; CP002206; ADO11574.1; -; Genomic_DNA.
DR RefSeq; WP_013359721.1; NC_014562.1.
DR AlphaFoldDB; E1SKS4; -.
DR KEGG; pva:Pvag_3442; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_3_6; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000006631; Chromosome.
DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:InterPro.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:InterPro.
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; 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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR012799; FadB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02437; FadB; 1.
DR PANTHER; PTHR43612:SF8; FATTY ACID OXIDATION COMPLEX SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADO11574.1};
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 315..493
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 495..591
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 626..687
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 727 AA; 78533 MW; FE23659CA605AC4C CRC64;
MLYQGANLTL HWLDDGIAEL VFDATGSVNK LDTQTVASLG EAIAVLEQQP DLRGLLLSSA
KPAFIVGADI TEFLSLFDAP TEKLSQWLSY ANSIFNRLED LPVPTLAAID GYALGGGCEC
VLATDLRIAT ADARIGLPET KLGIMPGFGG SVRLPRLLGA DSALEIIAAG KDVDGNAALK
LGLVDAVVVR EKLREAGITM LKAAAADDSW RARRAPKLAP LKLSPIEAAM SFTIAKAMVL
QTAGKHYPAP LMAVKTIEAA ASLGRDDALK LETAAFVPLA QSDEARALVG IFLNDQYVKS
LAKKRGSESG APAQAAVLGA GIMGGGISYQ SAWKGVPVRM KDINPQALTL GMNEASKLLN
KLLERGKIDG SKLASVIATI QPTLDYAGFD QADVVVEAVV ENPLIKAKVL AETEQHLRQD
AILASNTSTI PISQLAQALQ RPENFCGMHF FNPVPRMPLV EVVRGEKTSE ATLSKVVAWA
SKMGKTPIVV NDCPGFFVNR VLFPYFAAFS LLLRDGADFR QIDKVMEKQF GWPMGPSWLL
DVVGIDTAHH AQSVMADGFP DRMKHDYRDA IDLLFDAGRF GQKNGKGFWR WEEDKKGKLK
KVPDAEVDTL LQQVCQPARV FSDEEILNRM MLPMLNEVVR CLEEKIIASP AEADMALVYG
LGFPPFRGGA FRYLDTLGNS NVVDQARRYS ALGGLYALPA LLVQKAHQHE SWYPAAKPID
EAALKSA
//
