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Database: UniProt
Entry: D4GJB0_PANAM
LinkDB: D4GJB0_PANAM
Original site: D4GJB0_PANAM 
ID   D4GJB0_PANAM            Unreviewed;       706 AA.
AC   D4GJB0;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE            EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN   Name=fadJ {ECO:0000313|EMBL:ADD77860.1};
GN   OrderedLocusNames=PANA_2693 {ECO:0000313|EMBL:ADD77860.1};
OS   Pantoea ananatis (strain LMG 20103).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD77860.1, ECO:0000313|Proteomes:UP000001702};
RN   [1] {ECO:0000313|EMBL:ADD77860.1, ECO:0000313|Proteomes:UP000001702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD77860.1,
RC   ECO:0000313|Proteomes:UP000001702};
RX   PubMed=20348253; DOI=10.1128/JB.00060-10;
RA   De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA   Coutinho T.A.;
RT   "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT   Eucalyptus blight and dieback.";
RL   J. Bacteriol. 192:2936-2937(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: 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; CP001875; ADD77860.1; -; Genomic_DNA.
DR   RefSeq; WP_013026571.1; NC_013956.2.
DR   AlphaFoldDB; D4GJB0; -.
DR   STRING; 706191.PANA_2693; -.
DR   KEGG; pam:PANA_2693; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_16_1_6; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001702; 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: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; 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; 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; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
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:UP000001702}.
FT   DOMAIN          310..488
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          491..584
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   706 AA;  76269 MW;  C8C0E0514AA12673 CRC64;
     MEQSAFTLQM RDDHVGVITI DVPNEKMNTL KAAFAAQIAA IIAEARKHPQ LLGLVLISGK
     PDNFVAGADI SMIDGCQSAH EAEALARQGQ DVMAAIAALP FPVVAAIHGA CLGGGLELAL
     ACNARICSLD DKTRIGLPEV QLGLLPGSGG TQRLPRLIGV QKALPLILTG KNLRSRQAKK
     LGIVDDAVPQ AILLDAAVEL VKKGKYRRAP LPLRDRLLQG PMARQALFAL VRRETDRKTQ
     GNYPAARRII EVVHIGLEQS SQAGYAAEAR AFGELAMTPE SAALRSLFFA STAIKKENGT
     QAEPRPLQRV GVLGGGLMGG GIASVSAVNA GLPVRIKDIS LKGINHALQT SWDLLSKKVK
     RRQISPAQRQ QQMARISGST DYQGFTQRDI VIEAVFEDLD LKRQMVADVE ANCQPQTIFA
     SNTSSIPIAE IAATARRPEN IIGLHYFSPV EKMPLVEVIP HAMTSPETLA STVMLARKQG
     KTPIVVADKP GFYVNRILTP YINEAMRCVV EGEPIDHIDR ALVKAGFPVG PVQLLDEVGI
     DVGSKISPGL QQAYGERFAA PSALDAVIKD GRKGRKNGRG FYLYGSSRLS RKKVDPAVYG
     LVKTRPVAKQ SGAQIAERCM MMMLNEAVRC LDEQVIRSPR DGDIGAVFGI GFPPFLGGPF
     HYIDRLGAAE IVNRLTRLQQ QYGDRFAPCD ALLRAAEQQT KFYTSS
//
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