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FADJ_ECO81
ID   FADJ_ECO81              Reviewed;         714 AA.
AC   B7MY16;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01617};
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01617};
DE              EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01617};
DE              EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01617};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01617};
DE              EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01617};
GN   Name=fadJ {ECO:0000255|HAMAP-Rule:MF_01617}; OrderedLocusNames=ECED1_2804;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the formation of a hydroxyacyl-CoA by addition of
CC       water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-
CC       hydroxyacyl-CoA dehydrogenase activities. {ECO:0000255|HAMAP-
CC       Rule:MF_01617}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01617};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01617};
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:0000255|HAMAP-Rule:MF_01617};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA;
CC         Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC         EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01617};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains
CC       (FadI). {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01617}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01617}.
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DR   EMBL; CU928162; CAR08982.2; -; Genomic_DNA.
DR   RefSeq; WP_000425022.1; NC_011745.1.
DR   AlphaFoldDB; B7MY16; -.
DR   SMR; B7MY16; -.
DR   EnsemblBacteria; CAR08982; CAR08982; ECED1_2804.
DR   KEGG; ecq:ECED1_2804; -.
DR   HOGENOM; CLU_009834_16_1_6; -.
DR   OMA; PFRYMDT; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000748; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01617; FadJ; 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   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR02440; FadJ; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Fatty acid metabolism; Isomerase; Lipid degradation;
KW   Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase.
FT   CHAIN           1..714
FT                   /note="Fatty acid oxidation complex subunit alpha"
FT                   /id="PRO_1000185939"
FT   REGION          1..190
FT                   /note="Enoyl-CoA hydratase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT   REGION          306..714
FT                   /note="3-hydroxyacyl-CoA dehydrogenase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT   SITE            118
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT   SITE            140
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
SQ   SEQUENCE   714 AA;  77144 MW;  D3098039EC0052FA CRC64;
     MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFVSA
     KPDNFIAGAD INMIGNCKTA QEAEVLARQG QQLMAEIHAL PIPVIAAIHG ACLGGGLELA
     LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAV
     KLGLVDDVVP HSILLEAAVE LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT
     QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTEVKKDPG
     SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPRGINHALK YSWDQLEGKV
     RRRHLKASER DKQLALISGT TDYCGFAHRD LIIEAVFENL ELKQQMVAEV EQNCATHTIF
     ASNTSSLPIG DIAAHAARPE QVIGLHFFSP VEKMPLVEII PHASTSAQTI ATTVKLAKKQ
     GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERIEHID AALVKFGFPV GPIQLLDEVG
     IDTGTKIIPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA
     IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCLDEQVIR SVRDGDIGAV FGIGFPPFLG
     GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCDRLVEMSE RGESFWKTTA TDLQ
 
 
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