ID E1SQ60_FERBD Unreviewed; 708 AA.
AC E1SQ60;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN OrderedLocusNames=Fbal_2630 {ECO:0000313|EMBL:ADN76832.1};
OS Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN76832.1, ECO:0000313|Proteomes:UP000006683};
RN [1] {ECO:0000313|EMBL:ADN76832.1, ECO:0000313|Proteomes:UP000006683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC {ECO:0000313|Proteomes:UP000006683};
RX DOI=10.4056/sigs.1161239;
RA Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL Stand. Genomic Sci. 3:174-182(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; CP002209; ADN76832.1; -; Genomic_DNA.
DR RefSeq; WP_013346138.1; NC_014541.1.
DR AlphaFoldDB; E1SQ60; -.
DR STRING; 550540.Fbal_2630; -.
DR GeneID; 67182860; -.
DR KEGG; fbl:Fbal_2630; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_1_6; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000006683; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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: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; 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; IPR012802; FadJ.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02440; FadJ; 1.
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; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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, ECO:0000313|EMBL:ADN76832.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADN76832.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006683}.
FT DOMAIN 313..492
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 495..588
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 620..701
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 708 AA; 75958 MW; 79D664B83E36E838 CRC64;
MSDKTFSLDV GNDGVAIITM DVPGESMNTL RDSFAAEVRD LLGEIVQDSS IKGVVFTSGK
PGSFIAGADI AMLAACKTTD DAYQISRGAQ QLFNELAALK VPVVAAIDGP CLGGGLELAL
ACDYRICSDS AKTVLGVPEV QLGLLPGGGG TQRLPRLVGV ARSLDMMLSG RQLRAKQAKK
FGLVEETVPL SVLVDVAREY ALKGKRKAVK PNLKGAEKLL ESTAFGRKVI FDQAGKKVLA
KTQGNYPAPL KIIDCVRTGL EKGLDAGYEV EARHFGELVM TPESEALRSI FFATTEMKKE
SGAGDAKPLP LNKVMVLGGG LMGGGIASVT ALKAKLPARI KDIAEPGLQN ALAYSYKQVD
KRVKKRQMTP AQRDKAMSLL STTTRYDGIK DVDIVVEAVF EDLNLKHQMV KDVEANCGEH
TIFASNTSSL PIGQIAEAAS RPDKVIGLHY FSPVEKMPLV EVIAHKGTSA ETIATTVAFA
RKQGKTPIVV QDGAGFYVNR ILALYMNEAA NLLLDGEPVE ALDKALVKFG FPVGPVTLLD
EVGIDVGAKI SPILESELGS RFAAPAAFAK LLADDRKGRK NGKGFYQYGG KAKGKKPVDE
SVYQVLGIQP QGRLSQSELA ERCVVQMLNE AVRCLEEGII ASPRDGDIGA IFGIGFPPFL
GGPFRYIDRL GAKSLVERLR SYQERFGDRF APADKLVAMA EQDERFYP
//
