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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]

 S5J2W2_VIBPH            Unreviewed;       703 AA.
S5J2W2;
16-OCT-2013, integrated into UniProtKB/TrEMBL.
16-OCT-2013, sequence version 1.
20-JUN-2018, entry version 39.
RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01617};
Includes:
RecName: Full=Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase {ECO:0000256|HAMAP-Rule:MF_01617};
EC=4.2.1.17 {ECO:0000256|HAMAP-Rule:MF_01617};
EC=5.1.2.3 {ECO:0000256|HAMAP-Rule:MF_01617};
Includes:
RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01617};
EC=1.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01617};
Name=fadJ {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000313|EMBL:AGQ91401.1};
ORFNames=M634_13435 {ECO:0000313|EMBL:AGQ91401.1};
Vibrio parahaemolyticus O1:Kuk str. FDA_R31.
Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
Vibrionaceae; Vibrio.
NCBI_TaxID=1338034 {ECO:0000313|EMBL:AGQ91401.1, ECO:0000313|Proteomes:UP000014929};
[1] {ECO:0000313|EMBL:AGQ91401.1, ECO:0000313|Proteomes:UP000014929}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FDA_R31 {ECO:0000313|EMBL:AGQ91401.1};
PubMed=25814612;
Ludeke C.H., Kong N., Weimer B.C., Fischer M., Jones J.L.;
"Complete Genome Sequences of a Clinical Isolate and an Environmental
Isolate of Vibrio parahaemolyticus.";
Genome Announc. 3:0-0(2015).
-!- FUNCTION: Catalyzes the formation of a hydroxyacyl-CoA by addition
of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase
and 3-hydroxyacyl-CoA dehydrogenase activities.
{ECO:0000256|HAMAP-Rule:MF_01617, ECO:0000256|SAAS:SAAS00643143}.
-!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CoA + H(2)O. {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00999126}.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH. {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00379695}.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
hydroxybutanoyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00643142}.
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
{ECO:0000256|HAMAP-Rule:MF_01617, ECO:0000256|SAAS:SAAS00649747}.
-!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta
chains (FadI). {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00643147}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00643134}.
-!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
hydratase/isomerase family. {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00649729}.
-!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-
CoA dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00643136}.
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EMBL; CP006004; AGQ91401.1; -; Genomic_DNA.
RefSeq; WP_020841141.1; NC_021847.1.
EnsemblBacteria; AGQ91401; AGQ91401; M634_13435.
KEGG; vpf:M634_13435; -.
KO; K01782; -.
UniPathway; UPA00659; -.
Proteomes; UP000014929; Chromosome I.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule.
GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
HAMAP; MF_01617; FadJ; 1.
InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
InterPro; IPR006108; 3HC_DH_C.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
InterPro; IPR001753; Enoyl-CoA_hydra/iso.
InterPro; IPR012802; FadJ.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00725; 3HCDH; 2.
Pfam; PF02737; 3HCDH_N; 1.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF48179; SSF48179; 2.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR02440; FadJ; 1.
PROSITE; PS00067; 3HCDH; 1.
PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000014929};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00643137};
Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00456821};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00656496, ECO:0000313|EMBL:AGQ91401.1};
Lipid degradation {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00643150};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00456821, ECO:0000256|SAAS:SAAS00643150};
Lyase {ECO:0000256|HAMAP-Rule:MF_01617, ECO:0000256|SAAS:SAAS00999128,
ECO:0000313|EMBL:AGQ91401.1};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00999134};
NAD {ECO:0000256|HAMAP-Rule:MF_01617, ECO:0000256|SAAS:SAAS00830857};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01617,
ECO:0000256|SAAS:SAAS00649305, ECO:0000313|EMBL:AGQ91401.1}.
DOMAIN 312 491 3HCDH_N. {ECO:0000259|Pfam:PF02737}.
DOMAIN 494 587 3HCDH. {ECO:0000259|Pfam:PF00725}.
DOMAIN 616 691 3HCDH. {ECO:0000259|Pfam:PF00725}.
REGION 1 190 Enoyl-CoA hydratase. {ECO:0000256|HAMAP-
Rule:MF_01617}.
REGION 308 703 3-hydroxyacyl-CoA dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_01617}.
SITE 118 118 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_01617}.
SITE 140 140 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_01617}.
SEQUENCE 703 AA; 76778 MW; FDC6EC86C6256FC8 CRC64;
MSEQKAFSLN VDEQNIAWLA IDVPNEKMNT LQAAFADEMK EIFAQLKDSS GIKGMIIHSL
KPDNFVAGAD VRMLEACTTA NEAQALAKQG QELFQQLSDL PYPVVAAIHG PCLGGGLELA
LACDYRVCTD SDKTRLGLPE 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
VGVDIGAKII PILVNELGER FKGPDVFDIL LNDGRKGRKS GKGFYTYKGK KKEVDKSIYK
LLKLTPESKL SDNDIALRCV LPMLNEAVRC LDDGIIRSPR DGDIGAIFGI GFPPFLGGPF
RYMDQFGLKE LVEKMNEFAS KYGDRYAPCD GLLTRAGEGR TFY


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