FADJ_YERPN
ID FADJ_YERPN Reviewed; 747 AA.
AC Q1CHK2; C4GU81;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 95.
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}; OrderedLocusNames=YPN_2200;
GN ORFNames=YP516_2465;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABG18528.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EEO76268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000305; ABG18528.1; ALT_INIT; Genomic_DNA.
DR EMBL; ACNQ01000013; EEO76268.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q1CHK2; -.
DR SMR; Q1CHK2; -.
DR EnsemblBacteria; ABG18528; ABG18528; YPN_2200.
DR KEGG; ypn:YPN_2200; -.
DR HOGENOM; CLU_009834_16_1_6; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000008936; 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.
FT CHAIN 1..747
FT /note="Fatty acid oxidation complex subunit alpha"
FT /id="PRO_0000273991"
FT REGION 8..197
FT /note="Enoyl-CoA hydratase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT REGION 313..741
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT REGION 590..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 125
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
FT SITE 147
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617"
SQ SEQUENCE 747 AA; 80695 MW; B6D95C35353F458F CRC64;
MGASATNSVT HPAFTLNVRP DNIGIITIDV VGDKVNTLKA EFADQIATIL QQAHALPKLQ
GLVIVSGKPD SFIAGADITM IAACRTAHDA RVLAQKGQSI LAQIAAFPVP VVAAIHGACL
GGGLELALAC HSRICSLDDK TVLGLPEVQL GLLPGSGGTQ RLPRLVGVSK ALDMILTGKQ
IRPRQALKMG LVDDVVPRDI LLDVAIQRAK AGWLNRRALP WQERLLSGPL GKALLFRIVR
KKTLAKTRGH YPAAERIIDV VRKGLDQGGP SGYEAEARAF GELAMSPQSA ALRSLFFATT
SLKKETGSAA TARAIHRVGV LGGGLMGGGI ANVTATRAGL PVRIKDINPQ GINQALKYTW
DALGKRVRSK RMRPTEQQRQ MMLISGSTDY RGFERVDIVV EAVFEDLSLK QQMVADIERF
GAAHTIFASN TSSLPISQIA ALAQRPEQVI GLHYFSPVDK MPLVEVIPHE KTSEETIATT
VALARKQGKT AIVVADRAGF YVNRILAPYI NEAARCLLDG EPIESVDNAL VDFGFPVGPM
MLLDEVGIDV ATKIMPILVE QLGPRFAAPP SFDVILKDGR KGRKNGRGFY LYSNPTKNSS
PTKNGNSPAK RNSFKWRKNK VKPVDASIYT LLGVTPKAHL GAGVITQRCT MLMLNEAVRC
LDESIIRNPR DGDIGAVFGI GFPPFLGGPF RYLDSLGADK VVQALRLLVQ QYGERFEPCQ
RLVTMAEQQQ QFYPVDANID EVTDVAS
