ID G9ZAL2_9ENTR Unreviewed; 716 AA.
AC G9ZAL2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 69.
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 ORFNames=HMPREF0880_04573 {ECO:0000313|EMBL:EHM44886.1};
OS Yokenella regensburgei ATCC 43003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Yokenella.
OX NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM44886.1, ECO:0000313|Proteomes:UP000003044};
RN [1] {ECO:0000313|EMBL:EHM44886.1, ECO:0000313|Proteomes:UP000003044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM44886.1,
RC ECO:0000313|Proteomes:UP000003044};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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:EHM44886.1}.
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DR EMBL; AGCL01000047; EHM44886.1; -; Genomic_DNA.
DR RefSeq; WP_006821019.1; NZ_JH417874.1.
DR AlphaFoldDB; G9ZAL2; -.
DR STRING; 1002368.HMPREF0880_04573; -.
DR PATRIC; fig|1002368.3.peg.4179; -.
DR HOGENOM; CLU_009834_16_1_6; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000003044; 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; 1.
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 311..489
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 492..586
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 1..190
FT /note="Enoyl-CoA hydratase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617"
FT REGION 306..716
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617"
FT SITE 118
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617"
FT SITE 140
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617"
SQ SEQUENCE 716 AA; 77554 MW; D5268D8D29C98FA4 CRC64;
METMSAFSLN VRPDNVAVIT LDVPGEKMNT LKAEFGTEVR ALLRQIRENH DIRGVVLISA
KEDNFVAGAD INMIGRCKTA LEAEALAKQG QQVMAEIHAM PVPVVAAIHG ACLGGGLELA
LACHARLCTD DAKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRARQAL
KAGLVDEVVA ASILLEAAVE RVKNGVPEHR RLPVRERVLA GPLGRTVLFN LVGKKTEQKT
LGNYPATTRI LQVIETGLAH GISSGYEAEA RAFGELAMTP QSQSLRHIFF ASTDLKKDPG
ASAESGPLRA VGILGGGLMG GGIAFVTACK GKLPVRIKDI NANGINHALK YSWDLLDKKV
RRRHIRASER DSQLALISGT TDYSGFSHRD VVIEAVFEDL ALKQKMVTEV EQHCAPHTVF
ASNTSSLPIG DIAALAARPE QVIGLHFFSP VEKMPLVEVI PHAGTSERTI ATTVKLAKKQ
GKTPIVVADK AGFYVNRILA PYINEAIRLL TEGQRIENID KALVKFGFPV GPIQLLDEVG
IDTGTKIIPV LEEAYGERFR PPANVIDAIL NDDRKGRKNN RGFYLYGEKG RKSKKQPDPA
IYALVGSTGQ KNEFNEQLMA ERCVMLMLNE AARCYDEQVV RSARDGDIGA VFGIGFPPFL
GGPFHYMDTL GAREVVAILQ RLAVQHGPRF TPCESLLQRA EQGLTFWPAK ETDAIS
//