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Database: UniProt
Entry: G9ZAL2_9ENTR
LinkDB: G9ZAL2_9ENTR
Original site: G9ZAL2_9ENTR 
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
//
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