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Peroxisomal bifunctional enzyme (PBE) (PBFE) [Includes: Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC 4.2.1.17) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]

 ECHP_HUMAN              Reviewed;         723 AA.
Q08426; A8K6Y3; B4DWG3; D3DNU0; Q58EZ5;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 3.
18-JUL-2018, entry version 187.
RecName: Full=Peroxisomal bifunctional enzyme;
Short=PBE;
Short=PBFE;
Includes:
RecName: Full=Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase;
EC=4.2.1.17;
EC=5.3.3.8;
Includes:
RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
EC=1.1.1.35;
Name=EHHADH; Synonyms=ECHD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANTS GLY-40; ARG-41; ILE-75; GLY-325; THR-598 AND PRO-606.
TISSUE=Liver;
PubMed=8188243; DOI=10.1006/geno.1994.1013;
Hoefler G., Forstner M., McGuinness M.C., Hulla W., Hiden M.,
Krisper P., Kenner L., Ried T., Lengauer C., Zechner R., Moser H.W.,
Chen G.L.;
"cDNA cloning of the human peroxisomal enoyl-CoA hydratase: 3-
hydroxyacyl-CoA dehydrogenase bifunctional enzyme and localization to
chromosome 3q26.3-3q28: a free left Alu Arm is inserted in the 3'
noncoding region.";
Genomics 19:60-67(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Cherkaoui-Malki M., Surapureddi S., Yeldandi A.V., Rao S.M., Zhu Y.,
Reddy J.K.;
"Structural organization of gene for human peroxisomal enoyl-CoA
hydratase/L-3-hydroxyacyl-CoA dehydrogenase: L-bifunctional enzyme (L-
PBE).";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
THR-274.
TISSUE=Placenta, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 502-723 (ISOFORMS 1/2), AND VARIANTS
THR-598 AND PRO-606.
TISSUE=Liver;
PubMed=1651711; DOI=10.1016/0006-291X(91)91003-U;
Chen G.L., Balfe A., Erwa W., Hoefler G., Gaertner J., Aikawa J.,
Chen W.W.;
"Import of human bifunctional enzyme into peroxisomes of human
hepatoma cells in vitro.";
Biochem. Biophys. Res. Commun. 178:1084-1091(1991).
[9]
ASSOCIATION WITH PERIXOSOMAL DISORDERS.
PubMed=3469675; DOI=10.1073/pnas.84.5.1425;
Chen W.W., Watkins P.A., Osumi T., Hashimoto T., Moser H.W.;
"Peroxisomal beta-oxidation enzyme proteins in adrenoleukodystrophy:
distinction between X-linked adrenoleukodystrophy and neonatal
adrenoleukodystrophy.";
Proc. Natl. Acad. Sci. U.S.A. 84:1425-1428(1987).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-584, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
ACETYLATION AT LYS-165; LYS-171; LYS-346 AND LYS-584, ENZYME
REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
LYS-165; LYS-171; LYS-346 AND LYS-584.
PubMed=20167786; DOI=10.1126/science.1179689;
Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L.,
Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L.,
Chin J., Yang P., Chen X., Lei Q., Xiong Y., Guan K.L.;
"Regulation of cellular metabolism by protein lysine acetylation.";
Science 327:1000-1004(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-548, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
VARIANT FRTS3 LYS-3, CHARACTERIZATION OF VARIANT FRTS3 LYS-3, AND
TISSUE SPECIFICITY.
PubMed=24401050; DOI=10.1056/NEJMoa1307581;
Klootwijk E.D., Reichold M., Helip-Wooley A., Tolaymat A., Broeker C.,
Robinette S.L., Reinders J., Peindl D., Renner K., Eberhart K.,
Assmann N., Oefner P.J., Dettmer K., Sterner C., Schroeder J.,
Zorger N., Witzgall R., Reinhold S.W., Stanescu H.C., Bockenhauer D.,
Jaureguiberry G., Courtneidge H., Hall A.M., Wijeyesekera A.D.,
Holmes E., Nicholson J.K., O'Brien K., Bernardini I., Krasnewich D.M.,
Arcos-Burgos M., Izumi Y., Nonoguchi H., Jia Y., Reddy J.K., Ilyas M.,
Unwin R.J., Gahl W.A., Warth R., Kleta R.;
"Mistargeting of peroxisomal EHHADH and inherited renal Fanconi's
syndrome.";
N. Engl. J. Med. 370:129-138(2014).
-!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CoA + H(2)O.
-!- CATALYTIC ACTIVITY: A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-
CoA.
-!- CATALYTIC ACTIVITY: A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-
CoA.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH.
-!- ENZYME REGULATION: Enzyme activity enhanced by acetylation.
{ECO:0000269|PubMed:20167786}.
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
P63261:ACTG1; NbExp=3; IntAct=EBI-2339219, EBI-351292;
O14503:BHLHE40; NbExp=3; IntAct=EBI-2339219, EBI-711810;
P35520:CBS; NbExp=3; IntAct=EBI-2339219, EBI-740135;
Q68D86:CCDC102B; NbExp=3; IntAct=EBI-2339219, EBI-10171570;
P17661:DES; NbExp=5; IntAct=EBI-2339219, EBI-1055572;
Q8IVP5:FUNDC1; NbExp=3; IntAct=EBI-2339219, EBI-3059266;
Q8NC69:KCTD6; NbExp=3; IntAct=EBI-2339219, EBI-2511344;
Q7L273:KCTD9; NbExp=3; IntAct=EBI-2339219, EBI-4397613;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-2339219, EBI-10172290;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-2339219, EBI-741037;
O15344:MID1; NbExp=5; IntAct=EBI-2339219, EBI-2340316;
Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-2339219, EBI-10172876;
Q8ND90:PNMA1; NbExp=3; IntAct=EBI-2339219, EBI-302345;
Q1KLZ0:PS1TP5BP1; NbExp=3; IntAct=EBI-2339219, EBI-9978131;
O43805:SSNA1; NbExp=3; IntAct=EBI-2339219, EBI-2515299;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-2339219, EBI-2212028;
Q15025:TNIP1; NbExp=3; IntAct=EBI-2339219, EBI-357849;
P29144:TPP2; NbExp=3; IntAct=EBI-2339219, EBI-1044672;
Q13077:TRAF1; NbExp=3; IntAct=EBI-2339219, EBI-359224;
P14373:TRIM27; NbExp=5; IntAct=EBI-2339219, EBI-719493;
Q8WV44:TRIM41; NbExp=5; IntAct=EBI-2339219, EBI-725997;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-2339219, EBI-2130429;
Q96C00:ZBTB9; NbExp=5; IntAct=EBI-2339219, EBI-395708;
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q08426-1; Sequence=Displayed;
Name=2;
IsoId=Q08426-2; Sequence=VSP_042811;
-!- TISSUE SPECIFICITY: Liver and kidney. Strongly expressed in the
terminal segments of the proximal tubule. Lower amounts seen in
the brain. {ECO:0000269|PubMed:24401050,
ECO:0000269|PubMed:8188243}.
-!- PTM: Acetylated, leading to enhanced enzyme activity. Acetylation
is enhanced by up to 80% after treatment either with trichostin A
(TSA) or with nicotinamide (NAM) with highest increase on Lys-346.
Acetylation and enzyme activity increased by about 1.5% on
addition of fatty acids. {ECO:0000269|PubMed:20167786}.
-!- DISEASE: Fanconi renotubular syndrome 3 (FRTS3) [MIM:615605]: A
disease due to a generalized dysfunction of the proximal kidney
tubule resulting in decreased solute and water reabsorption.
Patients have polydipsia and polyuria with phosphaturia,
glycosuria and aminoaciduria. They may develop hypophosphatemic
rickets or osteomalacia, acidosis and a tendency toward
dehydration. Some eventually develop renal insufficiency.
{ECO:0000269|PubMed:24401050}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Absent in patients suffering with peroxisomal
disorders such as Zellweger syndrome, neonatal
adrenoleukodystrophy and infantile Refsum disease.
-!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
hydratase/isomerase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the 3-
hydroxyacyl-CoA dehydrogenase family. {ECO:0000305}.
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EMBL; L07077; AAA53289.1; -; mRNA.
EMBL; AJ427345; CAD22483.1; -; Genomic_DNA.
EMBL; AJ427346; CAD22483.1; JOINED; Genomic_DNA.
EMBL; AJ427347; CAD22483.1; JOINED; Genomic_DNA.
EMBL; AJ427348; CAD22483.1; JOINED; Genomic_DNA.
EMBL; AJ427349; CAD22483.1; JOINED; Genomic_DNA.
EMBL; AJ427350; CAD22483.1; JOINED; Genomic_DNA.
EMBL; AJ427351; CAD22483.1; JOINED; Genomic_DNA.
EMBL; AK291798; BAF84487.1; -; mRNA.
EMBL; AK223460; BAD97180.1; -; mRNA.
EMBL; AK301521; BAG63025.1; -; mRNA.
EMBL; AC007934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC128680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78229.1; -; Genomic_DNA.
EMBL; CH471052; EAW78230.1; -; Genomic_DNA.
EMBL; BC038948; AAH38948.1; -; mRNA.
EMBL; BC110460; AAI10461.1; -; mRNA.
EMBL; S50245; AAB19482.1; -; mRNA.
CCDS; CCDS33901.1; -. [Q08426-1]
CCDS; CCDS54694.1; -. [Q08426-2]
PIR; A49613; A49613.
RefSeq; NP_001159887.1; NM_001166415.1. [Q08426-2]
RefSeq; NP_001957.2; NM_001966.3. [Q08426-1]
RefSeq; XP_011510819.1; XM_011512517.1. [Q08426-2]
UniGene; Hs.429879; -.
ProteinModelPortal; Q08426; -.
SMR; Q08426; -.
BioGrid; 108282; 31.
IntAct; Q08426; 96.
STRING; 9606.ENSP00000231887; -.
DrugBank; DB00157; NADH.
SwissLipids; SLP:000000543; -.
iPTMnet; Q08426; -.
PhosphoSitePlus; Q08426; -.
BioMuta; EHHADH; -.
DMDM; 223590229; -.
EPD; Q08426; -.
MaxQB; Q08426; -.
PaxDb; Q08426; -.
PeptideAtlas; Q08426; -.
PRIDE; Q08426; -.
ProteomicsDB; 58608; -.
ProteomicsDB; 58609; -. [Q08426-2]
DNASU; 1962; -.
Ensembl; ENST00000231887; ENSP00000231887; ENSG00000113790. [Q08426-1]
Ensembl; ENST00000456310; ENSP00000387746; ENSG00000113790. [Q08426-2]
GeneID; 1962; -.
KEGG; hsa:1962; -.
UCSC; uc003fpf.3; human. [Q08426-1]
CTD; 1962; -.
DisGeNET; 1962; -.
DisGeNET; 51807; -.
EuPathDB; HostDB:ENSG00000113790.10; -.
GeneCards; EHHADH; -.
HGNC; HGNC:3247; EHHADH.
HPA; HPA036401; -.
HPA; HPA042021; -.
MalaCards; EHHADH; -.
MIM; 607037; gene.
MIM; 615605; phenotype.
neXtProt; NX_Q08426; -.
OpenTargets; ENSG00000113790; -.
Orphanet; 300; Bifunctional enzyme deficiency.
Orphanet; 3337; Primary Fanconi syndrome.
PharmGKB; PA27682; -.
eggNOG; KOG1683; Eukaryota.
eggNOG; COG1024; LUCA.
eggNOG; COG1250; LUCA.
GeneTree; ENSGT00880000137923; -.
HOGENOM; HOG000261347; -.
HOVERGEN; HBG104990; -.
InParanoid; Q08426; -.
KO; K07514; -.
OMA; IDLCMIL; -.
OrthoDB; EOG091G082G; -.
PhylomeDB; Q08426; -.
TreeFam; TF316708; -.
BioCyc; MetaCyc:HS03720-MONOMER; -.
Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
Reactome; R-HSA-9033241; Peroxisomal protein import.
SABIO-RK; Q08426; -.
UniPathway; UPA00659; -.
GenomeRNAi; 1962; -.
PRO; PR:Q08426; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000113790; -.
CleanEx; HS_EHHADH; -.
ExpressionAtlas; Q08426; baseline and differential.
Genevisible; Q08426; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IBA:GO_Central.
GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
GO; GO:0004300; F:enoyl-CoA hydratase activity; NAS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; TAS:Reactome.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
GO; GO:0006475; P:internal protein amino acid acetylation; IDA:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
InterPro; IPR006108; 3HC_DH_C.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
InterPro; IPR001753; Enoyl-CoA_hydra/iso.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00725; 3HCDH; 2.
Pfam; PF02737; 3HCDH_N; 1.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF48179; SSF48179; 2.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52096; SSF52096; 1.
PROSITE; PS00067; 3HCDH; 1.
PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Disease mutation; Fatty acid metabolism; Isomerase; Lipid metabolism;
Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 723 Peroxisomal bifunctional enzyme.
/FTId=PRO_0000109247.
REGION 1 282 Enoyl-CoA hydratase / isomerase.
REGION 283 572 3-hydroxyacyl-CoA dehydrogenase.
MOTIF 721 723 Microbody targeting signal.
BINDING 101 101 Substrate; via amide nitrogen.
{ECO:0000250}.
SITE 104 104 Important for catalytic activity.
{ECO:0000250}.
SITE 124 124 Important for catalytic activity.
{ECO:0000250}.
MOD_RES 38 38 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 165 165 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:20167786}.
MOD_RES 165 165 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 171 171 N6-acetyllysine.
{ECO:0000269|PubMed:20167786}.
MOD_RES 219 219 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 219 219 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 250 250 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 280 280 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 290 290 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 346 346 N6-acetyllysine.
{ECO:0000269|PubMed:20167786}.
MOD_RES 350 350 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 464 464 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 532 532 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 548 548 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 577 577 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 584 584 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:20167786}.
MOD_RES 584 584 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 591 591 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 591 591 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 710 710 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 710 710 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9DBM2}.
MOD_RES 718 718 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 722 722 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBM2}.
VAR_SEQ 1 96 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042811.
VARIANT 3 3 E -> K (in FRTS3; the mutant is
mistargeted to mitochondria; results in
impaired mitochondrial oxidative
phosphorylation and defects in the
transport of fluids across the epithelium
of renal proximal tubular cells;
dbSNP:rs398124646).
{ECO:0000269|PubMed:24401050}.
/FTId=VAR_070949.
VARIANT 40 40 V -> G (in dbSNP:rs1062551).
{ECO:0000269|PubMed:8188243}.
/FTId=VAR_054329.
VARIANT 41 41 I -> R (in dbSNP:rs1062552).
{ECO:0000269|PubMed:8188243}.
/FTId=VAR_054330.
VARIANT 75 75 T -> I (in dbSNP:rs1062553).
{ECO:0000269|PubMed:8188243}.
/FTId=VAR_047132.
VARIANT 274 274 A -> T (in dbSNP:rs2302819).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_047133.
VARIANT 325 325 A -> G (in dbSNP:rs1062555).
{ECO:0000269|PubMed:8188243}.
/FTId=VAR_054331.
VARIANT 598 598 K -> T (in dbSNP:rs1042437).
{ECO:0000269|PubMed:1651711,
ECO:0000269|PubMed:8188243}.
/FTId=VAR_054332.
VARIANT 606 606 T -> P (in dbSNP:rs1042438).
{ECO:0000269|PubMed:1651711,
ECO:0000269|PubMed:8188243}.
/FTId=VAR_047134.
VARIANT 685 685 Q -> K (in dbSNP:rs11919970).
/FTId=VAR_047135.
VARIANT 715 715 L -> S (in dbSNP:rs11927618).
/FTId=VAR_047136.
MUTAGEN 165 165 K->Q: Greatly reduced acetylation and
insensitive to treatment with TSA and
NAM; when associated with Q-171; Q-346
and Q-584. {ECO:0000269|PubMed:20167786}.
MUTAGEN 171 171 K->Q: Greatly reduced acetylation and
insensitive to treatment with TSA and
NAM; when associated with Q-165; Q-346
and Q-584. {ECO:0000269|PubMed:20167786}.
MUTAGEN 346 346 K->Q: Greatly reduced acetylation and
insensitive to treatment with TSA and
NAM; when associated with Q-165; Q-171
and Q-584. {ECO:0000269|PubMed:20167786}.
MUTAGEN 584 584 K->Q: Greatly reduced acetylation and
insensitive to treatment with TSA and
NAM; when associated with Q-165; Q-171
and Q-346. {ECO:0000269|PubMed:20167786}.
CONFLICT 117 117 E -> D (in Ref. 1; AAA53289).
{ECO:0000305}.
CONFLICT 656 657 WP -> CA (in Ref. 1; AAA53289 and 7;
AAB19482). {ECO:0000305}.
SEQUENCE 723 AA; 79495 MW; FC3B44B030A7BCBD CRC64;
MAEYTRLHNA LALIRLRNPP VNAISTTLLR DIKEGLQKAV IDHTIKAIVI CGAEGKFSAG
ADIRGFSAPR TFGLTLGHVV DEIQRNEKPV VAAIQGMAFG GGLELALGCH YRIAHAEAQV
GLPEVTLGLL PGARGTQLLP RLTGVPAALD LITSGRRILA DEALKLGILD KVVNSDPVEE
AIRFAQRVSD QPLESRRLCN KPIQSLPNMD SIFSEALLKM RRQHPGCLAQ EACVRAVQAA
VQYPYEVGIK KEEELFLYLL QSGQARALQY AFFAERKANK WSTPSGASWK TASARPVSSV
GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLATANKMI TSVLEKEASK MQQSGHPWSG
PKPRLTSSVK ELGGVDLVIE AVFEEMSLKK QVFAELSAVC KPEAFLCTNT SALDVDEIAS
STDRPHLVIG THFFSPAHVM KLLEVIPSQY SSPTTIATVM NLSKKIKKIG VVVGNCFGFV
GNRMLNPYYN QAYFLLEEGS KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT
GPTLLPGTPA RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KPDPWLSKFL
SRYRKTHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY LHGYGWPRHK
GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK LASQGNPPLK EWQSLAGSPS
SKL


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