ID W1JAM5_9GAMM Unreviewed; 722 AA.
AC W1JAM5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01617};
DE Includes:
DE RecName: Full=Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase {ECO:0000256|HAMAP-Rule:MF_01617};
DE EC=4.2.1.17 {ECO:0000256|HAMAP-Rule:MF_01617};
DE EC=5.1.2.3 {ECO:0000256|HAMAP-Rule:MF_01617};
DE Includes:
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01617};
DE EC=1.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01617};
GN Name=fadJ {ECO:0000256|HAMAP-Rule:MF_01617,
GN ECO:0000313|EMBL:CDL86555.1};
GN ORFNames=XCR1_4210008 {ECO:0000313|EMBL:CDL86555.1};
OS Xenorhabdus cabanillasii JM26.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427517 {ECO:0000313|EMBL:CDL86555.1, ECO:0000313|Proteomes:UP000019197};
RN [1] {ECO:0000313|EMBL:CDL86555.1, ECO:0000313|Proteomes:UP000019197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM26 {ECO:0000313|EMBL:CDL86555.1,
RC ECO:0000313|Proteomes:UP000019197};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacterium,
RT Xenorhabdus cabanillasi strain JM26.";
RL Submitted (NOV-2013) 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:0000256|HAMAP-
CC 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:0000256|HAMAP-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:0000256|ARBA:ARBA00023693, ECO:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01617};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005, ECO:0000256|HAMAP-Rule:MF_01617}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains
CC (FadI). {ECO:0000256|HAMAP-Rule:MF_01617}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01617}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750,
CC ECO:0000256|HAMAP-Rule:MF_01617}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005,
CC ECO:0000256|HAMAP-Rule:MF_01617}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL86555.1}.
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DR EMBL; CBXE010000359; CDL86555.1; -; Genomic_DNA.
DR RefSeq; WP_038266882.1; NZ_NJGH01000043.1.
DR AlphaFoldDB; W1JAM5; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000019197; Unassembled WGS sequence.
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; 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 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.
DR PROSITE; PS00067; 3HCDH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01617};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_01617};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01617};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW Rule:MF_01617}; Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01617};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01617};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01617};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01617};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01617}.
FT DOMAIN 320..499
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 502..595
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 633..718
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 1..200
FT /note="Enoyl-CoA hydratase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617"
FT REGION 316..722
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617"
FT SITE 128
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617"
FT SITE 150
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617"
SQ SEQUENCE 722 AA; 78872 MW; FD5680B5A7D51E93 CRC64;
MAQAEKETIM SETQSVFSFS VRDDKIGVIT IDVPGEKVNT LKAEFVEQFL TVFEKAQQVS
GLKGLVIVSG KPDTFIAGAD ITMIAGCQTQ QEATKLAEKG QELFARIANY SLPIVAAIHG
ACLGGGLELA LACHARVCSL DDKTRLGLPE VQLGLLPGSG GTQRLPRLIG VSSALDMMLT
GRQLKANQAK RLGVVDDAVP LDILLDVAVQ YVKKGIIKRK PLAWSQRLLA SALGRPLLFQ
MVQQKTRAKT HGHYPAPERI IDVVRTGLEK GQKTGFRAEA KAFGELAMSP ESEALRSLFF
AATSLKNETG SSEQPAKIKH VGILGGGLMG GGIASVTATR GNLPVRIKDI NEKGINQALK
YTWDLLSKRV KQRRLKPSEC SRQMSLLSGS TDYIGFKQAD IVVEAVFEDL VLKRKMVSEI
EAHTKPETIF ASNTSSLPIH QIAEVAKRPE QVIGLHYFSP VDKMPLVEVI PHAGTSEKTI
ATAVALAKKQ GKTAIVVGDK AGFYVNRILS PYINEAGYCL VEGEPVNHID KALVDFGFPI
GPINLLDEVG IDVGTKIIPV LVEQLGRRFT PPAILDAVLN DNRKGKKNGR GFYSYEVKKS
RFWSFGKSSK EVDSSIYSLL KIKPNARISP SDIAQRCLMP MLNEAVRCLD EGIIRSPRDG
DIGAVFGIGF PPFLGGPFRY MDKLGSNKVV EILRRLEQQH GERFAPCERL VQMAEQNEKF
YE
//
