ID   FADJ_SHEHH              Reviewed;         708 AA.
AC   B0TL21;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
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};
GN   OrderedLocusNames=Shal_2670;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000931; ABZ77223.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0TL21; -.
DR   SMR; B0TL21; -.
DR   STRING; 458817.Shal_2670; -.
DR   KEGG; shl:Shal_2670; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_16_1_6; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001317; 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   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   HAMAP; MF_01617; FadJ; 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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Fatty acid metabolism; Isomerase; Lipid degradation;
KW   Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase.
FT   CHAIN           1..708
FT                   /note="Fatty acid oxidation complex subunit alpha"
FT                   /id="PRO_1000088063"
FT   REGION          1..190
FT                   /note="Enoyl-CoA hydratase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT   REGION          310..708
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   708 AA;  76230 MW;  A0C731D06441039D CRC64;
     MDMEKTFNLT RRDDGIAILT MDVPGETMNT LRSEFGPEIS DVLAEIKADT SIKGLVLVSG
     KKDSFVAGAD ISMLDACETA TDAKQLSQQG HVVFNELESL PIPVVAAING ACLGGGLELA
     LACHKRVCSL NPKTMMGVPE VQLGLLPGGG GTQRLPRLVG VTTALDMMLT GKQLRPKQAL
     KMGLVDDAVP ESILLRTAVE MALAGKRPAK KKHQSFFNKV LEGTSAGRNI IFDQAGKQVA
     KKTQGNYPAP AKIIDCVRQG MTKGMAKGLE VEASHFADLV MSKESGAMRS VFFATTEMKK
     ETGAGDVEPQ KVNKVMVLGG GLMGGGIASV TTTKAKIPAR VKDISETGLS NALAYAYKLL
     DKGVKRRHMT PAVRDNLMAL MTTTTEYKGI KDADIVVEAV FEDLALKHQM VKDVERECGE
     HTIFASNTSS LPIGQIAEAA SRPENVIGLH YFSPVEKMPL VEVIAHEKTS AETIATTVAF
     AKKQGKTPIV VQDGAGFYVN RILALYMNEA AQLLLEGQSV EHLDKALIKF GFPVGPMTLL
     DEVGIDVGAK ISPILEKELG ERFKAPTAFD KLLADDRKGR KNGKGFYLYG GKKKAKEVDQ
     TVYSVLGLKP GVDTEATEVA QRCVVQMLNE AVRCLEESII ACPRDGDIGA IFGIGFPPFL
     GGPFHYIDTL GAANLVKILE NYQSRYGSRF EPAAKLKQMA EEGTRFFS
//