FADJ_SHESA
ID FADJ_SHESA Reviewed; 709 AA.
AC A0KV76;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=Shewana3_1461;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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; CP000469; ABK47695.1; -; Genomic_DNA.
DR RefSeq; WP_011716519.1; NC_008577.1.
DR AlphaFoldDB; A0KV76; -.
DR SMR; A0KV76; -.
DR STRING; 94122.Shewana3_1461; -.
DR PRIDE; A0KV76; -.
DR EnsemblBacteria; ABK47695; ABK47695; Shewana3_1461.
DR KEGG; shn:Shewana3_1461; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_1_6; -.
DR OMA; PFRYMDT; -.
DR OrthoDB; 977512at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002589; 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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Fatty acid metabolism; Isomerase; Lipid degradation;
KW Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase.
FT CHAIN 1..709
FT /note="Fatty acid oxidation complex subunit alpha"
FT /id="PRO_0000323530"
FT REGION 1..188
FT /note="Enoyl-CoA hydratase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT REGION 308..709
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT SITE 116
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT SITE 138
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
SQ SEQUENCE 709 AA; 76262 MW; D8DC306F195146AB CRC64;
MEKTFNLTRR EDGIAILMMD VPGETMNTLK AEFGPEISEI LSEIKRDSSI RGLVLISGKK
DSFVAGADIS MLDACQTAGD AKALSQQGHV VFNELEALNI PVVAAIHGAC LGGGLELALA
CHQRVCSDDG KTMLGVPEVQ LGLLPGGGGT QRLPRLVGIT TALDMMLTGK QIRPKQALKM
GLVNDVVPQT ILLQTAVEMA LAGKRTAKPV KKSLVNQLLE GTGFGRNIIF DQAAKQVVKK
TQGNYPAPAK IIDCVRQGMA KGMQKGLEVE ASHFAELVVS KESEALRSIF FATTEMKKET
GAEGATPRKV KKAVILGGGL MGGGIASVTT TKAKIPARVK DINEKGLSNA LSYAYKLLDK
GVKRRHMTPA VRDNLMALMT TTTEYKGVKD ADIVVEAVFE DLALKHQMVK DIERECGEHT
IFASNTSSLP IGQIAQAASR PENVIGLHYF SPVEKMPLVE VIAHAKTSPE TIATTVAFAR
KQGKTPIVVQ DGAGFYVNRI LALYMNEAAQ LLLEGQSIEH LDKALVKFGF PVGPITLLDE
VGIDVGAKIA PILEKELGER FKAPAAFDKL LSDDRKGRKN GKGFYQYAAG NKASSKKKAV
DESVYAVLGI KPGMDKDLSA VAERCVVQML NEAVRCLDDG IIASPRDGDI GAIFGIGFPP
FLGGPFHYID TLGADNLVNI LERYQAQYGD RFEPCPRLKA MAAEKARFF
