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Database: UniProt
Entry: A0A1Y6L745_9GAMM
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ID   A0A1Y6L745_9GAMM        Unreviewed;       728 AA.
AC   A0A1Y6L745;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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:SMY18328.1};
GN   ORFNames=PAQU9191_03669 {ECO:0000313|EMBL:SMY18328.1};
OS   Photobacterium aquimaris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=512643 {ECO:0000313|EMBL:SMY18328.1, ECO:0000313|Proteomes:UP000196485};
RN   [1] {ECO:0000313|Proteomes:UP000196485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=type strain: CECT 9192 {ECO:0000313|Proteomes:UP000196485};
RA   Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; FYAH01000014; SMY18328.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6L745; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000196485; Unassembled WGS sequence.
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:InterPro.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196485}.
FT   DOMAIN          320..497
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          499..595
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          630..693
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   728 AA;  78666 MW;  6A25556D3B4DB107 CRC64;
     MIYHGETVSV NYLEDGIAEV IFDAPSPVNK FDLATLESFN LALDALYQQP KLKGVILRST
     KTAFIVGADI TEFLGLFALS ADQLSKWLHH ANTIFNKLED LPVPTIAAIN GYALGGGCEC
     VLATDFRVAD HQARIGLPET KLGIMPGFGG TVRLPRLIGA DSAMEIITAG KDKTAAAALK
     IGLIDAVVAT EMLPTAALAM IKQAIAGDLD WQQRRHQKQA PLPLSTTEAL MSFTTAKAMV
     ANIAGKHYLA PIAAVTAIET AANCNRDPAL AIENKHFVTL AKTDIAQALV GIFLNDQYIK
     NQAKQAKQAI KIAPATQQAM VLGAGIMGGG IAYQSATHHV PVIMKDIAAD ALTLGMEQAA
     KLLNKKLTRG RIDGLQMAAT LATITPTLTY SDSCHVDIVI EAVIENPTIK ATVLAEIEQQ
     VDATTVLTSN TSTIPINLLA QSLQRPQNFC GMHFFNPVHK MPLVEIIRGQ HTSNETIDRV
     VAYAAKMGKT PIVVNDCPGF FVNRVLFPYL AAFSLLLRDG GDYVQIDTIM EQDFGWPMGP
     AYLLDVVGID TAHHAQKVMA QGFPQRMAKN YTDAVDVLYQ HQRFGQKTGA GFFNYSTDKK
     GKPKKIFDPQ TATLLQPIAA TPTDFDSTVV IDRMLIPMIN EVVRCLEENI IATPAEADMA
     LVYGLGFPPF RGGVFRYLDH IGLANYVALA DSYQSLGALY QVPAGLRAKA AADECYYPTA
     TAVTMTHH
//
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