FADJ_KLEP7
ID FADJ_KLEP7 Reviewed; 714 AA.
AC A6TC19;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=KPN78578_26790; ORFNames=KPN_02723;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
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; CP000647; ABR78140.1; -; Genomic_DNA.
DR RefSeq; WP_015958773.1; NC_009648.1.
DR AlphaFoldDB; A6TC19; -.
DR SMR; A6TC19; -.
DR STRING; 272620.KPN_02723; -.
DR EnsemblBacteria; ABR78140; ABR78140; KPN_02723.
DR KEGG; kpn:KPN_02723; -.
DR HOGENOM; CLU_009834_16_1_6; -.
DR OMA; PFRYMDT; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000265; 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;
KW Reference proteome.
FT CHAIN 1..714
FT /note="Fatty acid oxidation complex subunit alpha"
FT /id="PRO_1000069488"
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; 77425 MW; F2701ED8E2714C57 CRC64;
MDTVSAFKLE VRADKIAVIT IDAPGEKMNT LKAEFGSQVR GLIRQLRDDK SVRGVVFISA
KADNFIAGAD INMIARCRSA QEAEALARQG QQIMAEIHGL SIPVIAAIHG ACLGGGLELA
LACHGRICSD DEKTRLGLPE VQLGLLPGSG GTQRLPRLIG VSTALDMMLT GKQLRPRQAL
KAGLVDEVVP QAILLQAAVE LALKGRPTSR EVPVRERVLA GPLGRHLLFQ FVGKQTQRKT
QGNYPAVKRI LQVVENGLAH GCSSGYAEEA RAFGELAMSP QSQALRSIFF ASTDLKKDPG
AEAGPGSLRS VAVLGGGLMG GGIAYVTACK GGLPVRIKDI QPRGINHALK YSWDLLNKQV
RQRRLRPVER DRQMALISGT TDYQGFAHRD VVIEAVFEDL ALKQRMVSEV EQYGGPQTIF
ASNTSSLPIG DIAAHASRPG QVIGLHFFSP VEKMPLVEMI PHKGTDPQTI ATVVQLAKRQ
GKTPIVVADK AGFYVNRILA PYINEAMRLL VEGEPIEVID NALVKFGFPV GPIQLLDEVG
IDTGTKIIPV LESAFGERFS PPANIIDAIL KDDRKGRKNN RGFYLYETKG RKSKKRPDPA
VYPLLGIGRP QSRLSAQQVA ERCVMMMLNE AARCFDEQII RSARDGDIGA VFGIGFPPFL
GGPFRYMDTI GAGEVAAILQ RLAAQFGPRF TPCDTLLRMA EQGTTFWPAD ERLT
