FADJ_VIBPA
ID FADJ_VIBPA Reviewed; 703 AA.
AC Q87MM3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=VP2208;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000031; BAC60471.1; -; Genomic_DNA.
DR RefSeq; NP_798587.1; NC_004603.1.
DR RefSeq; WP_005479507.1; NC_004603.1.
DR AlphaFoldDB; Q87MM3; -.
DR SMR; Q87MM3; -.
DR STRING; 223926.28807201; -.
DR EnsemblBacteria; BAC60471; BAC60471; BAC60471.
DR GeneID; 1189721; -.
DR KEGG; vpa:VP2208; -.
DR PATRIC; fig|223926.6.peg.2111; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_1_6; -.
DR OMA; PFRYMDT; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002493; Chromosome 1.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
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.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Fatty acid metabolism; Isomerase; Lipid degradation;
KW Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..703
FT /note="Fatty acid oxidation complex subunit alpha"
FT /id="PRO_0000109312"
FT REGION 1..190
FT /note="Enoyl-CoA hydratase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT REGION 308..703
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 703 AA; 76856 MW; A2A62EDC4047BA3F CRC64;
MSEQKAFSLN VDEQNIAWLA IDVPNEKMNT LQAAFADEMK EIFAQLKDSS GIKGMIIHSL
KPDNFVAGAD VRMLEACTTA NEAQALAKQG QELFQQLSDL PYPVVAAIHG PCLGGGLELA
LACDYRVCTD FDKTRLGLPE VQLGLLPGSG GTQRLPRLIG LLPSLDLILT GKQLRAKKAK
KLGVVDACVP DTILLDVAKQ FIDKGKNKGK KKQSTKEKLM SGSGLGRKLV FEQAAKKTNQ
KTRGNYPATV AILEVIQHGL EKGFAQGQEL EAKRFGELVM SSESKALRSI FFATTEMKKE
HGTDAQPAAV KKVGVLGGGL MGAGISHVTV AKAKVPVRIK DVSNDGVLNA LNYNYKLFEK
QRKRRILSKA DLQAKMLQLS GGVDFTSYNH IDVVIEAVFE DLDLKQQMVA DIEANAKSET
IFATNTSSLP IHKIAEKAER PENIVGLHYF SPVEKMPLVE VIPHETTSDE TISTVVALAK
KQGKTPIVVK DKAGFYVNRI LAPYMNEAAH ILLANEPIEK LDGALLDFGF PVGPITLLDE
VGVDIGAKIM PILVNELGER FKGPDVFDIL LNDGRKGRKS GKGFYTYKGK KKEVDKSIYK
LLKLTPESKL SDNDIALRCV LPMLNEAVRC LDDGIIRSPR DGDIGAIFGI GFPPFLGGPF
RYMDQFGLKE LVEKMNEFAS KYGDRYAPCD GLLTRAGEGR TFY
