Q08426 (ECHP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisomal bifunctional enzyme
Short name=PBE
Short name=PBFE

Including the following 2 domains:

1. Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
   EC=4.2.1.17
   EC=5.3.3.8
2. 3-hydroxyacyl-CoA dehydrogenase
   EC=1.1.1.35

Gene names

Name:	EHHADH
Synonyms:	ECHD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	723 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.
Enzyme regulation	Enzyme activity enhanced by acetylation. Ref.11
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Monomer.
Subcellular location	Peroxisome.
Tissue specificity	Liver and kidney. Lower amounts seen in the brain. Ref.1
Post-translational modification	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.
Miscellaneous	Absent in patients suffering with peroxisomal disorders such as Zellweger syndrome, neonatal adrenoleukodystrophy and infantile Refsum disease.
Sequence similarities	In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Non-traceable author statement Ref.1. Source: UniProtKB internal protein amino acid acetylation Inferred from direct assay Ref.11. Source: UniProtKB
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA peroxisome Inferred from direct assay Ref.8PubMed 2895531PubMed 9053548. Source: UniProtKB
Molecular_function	3-hydroxyacyl-CoA dehydrogenase activity Non-traceable author statement Ref.1. Source: UniProtKB coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from electronic annotation. Source: EC enoyl-CoA hydratase activity Non-traceable author statement Ref.1. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q08426-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q08426-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 723	723	Peroxisomal bifunctional enzyme		PRO_0000109247
Regions
	Region	1 – 282	282	Enoyl-CoA hydratase / isomerase
	Region	283 – 572	290	3-hydroxyacyl-CoA dehydrogenase
	Motif	721 – 723	3	Microbody targeting signal
Sites
	Binding site	101	1	Substrate; via amide nitrogen By similarity
	Site	104	1	Important for catalytic activity By similarity
	Site	124	1	Important for catalytic activity By similarity
Amino acid modifications
	Modified residue	165	1	N6-acetyllysine Ref.11
	Modified residue	171	1	N6-acetyllysine Ref.11
	Modified residue	346	1	N6-acetyllysine Ref.11
	Modified residue	584	1	N6-acetyllysine Ref.10 Ref.11
Natural variations
	Alternative sequence	1 – 96	96	Missing in isoform 2.		VSP_042811
	Natural variant	40	1	V → G. Ref.1 Corresponds to variant rs1062551 [ dbSNP | Ensembl ].		VAR_054329
	Natural variant	41	1	I → R. Ref.1 Corresponds to variant rs1062552 [ dbSNP | Ensembl ].		VAR_054330
	Natural variant	75	1	T → I. Ref.1 Corresponds to variant rs1062553 [ dbSNP | Ensembl ].		VAR_047132
	Natural variant	274	1	A → T. Ref.3 Corresponds to variant rs2302819 [ dbSNP | Ensembl ].		VAR_047133
	Natural variant	325	1	A → G. Ref.1 Corresponds to variant rs1062555 [ dbSNP | Ensembl ].		VAR_054331
	Natural variant	598	1	K → T. Ref.1 Ref.8 Corresponds to variant rs1042437 [ dbSNP | Ensembl ].		VAR_054332
	Natural variant	606	1	T → P. Ref.1 Ref.8 Corresponds to variant rs1042438 [ dbSNP | Ensembl ].		VAR_047134
	Natural variant	685	1	Q → K. Corresponds to variant rs11919970 [ dbSNP | Ensembl ].		VAR_047135
	Natural variant	715	1	L → S. Corresponds to variant rs11927618 [ dbSNP | Ensembl ].		VAR_047136
Experimental info
	Mutagenesis	165	1	K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584. Ref.11
	Mutagenesis	171	1	K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584. Ref.11
	Mutagenesis	346	1	K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584. Ref.11
	Mutagenesis	584	1	K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346. Ref.11
	Sequence conflict	117	1	E → D in AAA53289. Ref.1
	Sequence conflict	656 – 657	2	WP → CA in AAA53289. Ref.1
	Sequence conflict	656 – 657	2	WP → CA in AAB19482. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 10, 2009. Version 3. Checksum: FC3B44B030A7BCBD	FASTA	723	79,495
	10 20 30 40 50 60 MAEYTRLHNA LALIRLRNPP VNAISTTLLR DIKEGLQKAV IDHTIKAIVI CGAEGKFSAG 70 80 90 100 110 120 ADIRGFSAPR TFGLTLGHVV DEIQRNEKPV VAAIQGMAFG GGLELALGCH YRIAHAEAQV 130 140 150 160 170 180 GLPEVTLGLL PGARGTQLLP RLTGVPAALD LITSGRRILA DEALKLGILD KVVNSDPVEE 190 200 210 220 230 240 AIRFAQRVSD QPLESRRLCN KPIQSLPNMD SIFSEALLKM RRQHPGCLAQ EACVRAVQAA 250 260 270 280 290 300 VQYPYEVGIK KEEELFLYLL QSGQARALQY AFFAERKANK WSTPSGASWK TASARPVSSV 310 320 330 340 350 360 GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLATANKMI TSVLEKEASK MQQSGHPWSG 370 380 390 400 410 420 PKPRLTSSVK ELGGVDLVIE AVFEEMSLKK QVFAELSAVC KPEAFLCTNT SALDVDEIAS 430 440 450 460 470 480 STDRPHLVIG THFFSPAHVM KLLEVIPSQY SSPTTIATVM NLSKKIKKIG VVVGNCFGFV 490 500 510 520 530 540 GNRMLNPYYN QAYFLLEEGS KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT 550 560 570 580 590 600 GPTLLPGTPA RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KPDPWLSKFL 610 620 630 640 650 660 SRYRKTHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY LHGYGWPRHK 670 680 690 700 710 720 GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK LASQGNPPLK EWQSLAGSPS SKL
	Isoform 2 [UniParc]. Checksum: F1F1A30F0E89ED98	FASTA	627	69,154
	10 20 30 40 50 60 MAFGGGLELA LGCHYRIAHA EAQVGLPEVT LGLLPGARGT QLLPRLTGVP AALDLITSGR 70 80 90 100 110 120 RILADEALKL GILDKVVNSD PVEEAIRFAQ RVSDQPLESR RLCNKPIQSL PNMDSIFSEA 130 140 150 160 170 180 LLKMRRQHPG CLAQEACVRA VQAAVQYPYE VGIKKEEELF LYLLQSGQAR ALQYAFFAER 190 200 210 220 230 240 KANKWSTPSG ASWKTASARP VSSVGVVGLG TMGRGIVISF ARARIPVIAV DSDKNQLATA 250 260 270 280 290 300 NKMITSVLEK EASKMQQSGH PWSGPKPRLT SSVKELGGVD LVIEAVFEEM SLKKQVFAEL 310 320 330 340 350 360 SAVCKPEAFL CTNTSALDVD EIASSTDRPH LVIGTHFFSP AHVMKLLEVI PSQYSSPTTI 370 380 390 400 410 420 ATVMNLSKKI KKIGVVVGNC FGFVGNRMLN PYYNQAYFLL EEGSKPEEVD QVLEEFGFKM 430 440 450 460 470 480 GPFRVSDLAG LDVGWKSRKG QGLTGPTLLP GTPARKRGNR RYCPIPDVLC ELGRFGQKTG 490 500 510 520 530 540 KGWYQYDKPL GRIHKPDPWL SKFLSRYRKT HHIEPRTISQ DEILERCLYS LINEAFRILG 550 560 570 580 590 600 EGIAASPEHI DVVYLHGYGW PRHKGGPMFY ASTVGLPTVL EKLQKYYRQN PDIPQLEPSD 610 620 YLKKLASQGN PPLKEWQSLA GSPSSKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." 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. Genomics 19:60-67(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS GLY-40; ARG-41; ILE-75; GLY-325; THR-598 AND PRO-606. Tissue: Liver.
[2]	"Structural organization of gene for human peroxisomal enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase: L-bifunctional enzyme (L-PBE)." Cherkaoui-Malki M., Surapureddi S., Yeldandi A.V., Rao S.M., Zhu Y., Reddy J.K. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT THR-274. Tissue: Placenta.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Kidney.
[5]	"The DNA sequence, annotation and analysis of human chromosome 3." 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. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[8]	"Import of human bifunctional enzyme into peroxisomes of human hepatoma cells in vitro." Chen G.L., Balfe A., Erwa W., Hoefler G., Gaertner J., Aikawa J., Chen W.W. Biochem. Biophys. Res. Commun. 178:1084-1091(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 502-723 (ISOFORMS 1/2), VARIANTS THR-598 AND PRO-606. Tissue: Liver.
[9]	"Peroxisomal beta-oxidation enzyme proteins in adrenoleukodystrophy: distinction between X-linked adrenoleukodystrophy and neonatal adrenoleukodystrophy." Chen W.W., Watkins P.A., Osumi T., Hashimoto T., Moser H.W. Proc. Natl. Acad. Sci. U.S.A. 84:1425-1428(1987) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH PERIXOSOMAL DISORDERS.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-584, MASS SPECTROMETRY.
[11]	"Regulation of cellular metabolism by protein lysine acetylation." 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. Science 327:1000-1004(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-165; LYS-171; LYS-346 AND LYS-584, ENZYME REGULATION, MASS SPECTROMETRY, MUTAGENESIS OF LYS-165; LYS-171; LYS-346 AND LYS-584.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L07077 mRNA. Translation: AAA53289.1. AJ427345 , AJ427346, AJ427347, AJ427348, AJ427349, AJ427350, AJ427351 Genomic DNA. Translation: CAD22483.1. AK291798 mRNA. Translation: BAF84487.1. AK223460 mRNA. Translation: BAD97180.1. AK301521 mRNA. Translation: BAG63025.1. AC007934 Genomic DNA. No translation available. AC128680 Genomic DNA. No translation available. CH471052 Genomic DNA. Translation: EAW78229.1. CH471052 Genomic DNA. Translation: EAW78230.1. BC038948 mRNA. Translation: AAH38948.1. BC110460 mRNA. Translation: AAI10461.1. S50245 mRNA. Translation: AAB19482.1.
IPI	IPI00216164.
PIR	A49613.
RefSeq	NP_001159887.1. NM_001166415.1. NP_001957.2. NM_001966.3.
UniGene	Hs.429879.
3D structure databases
ProteinModelPortal	Q08426.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q08426. 3 interactions.
STRING	9606.ENSP00000231887.
PTM databases
PhosphoSite	Q08426.
Polymorphism databases
DMDM	223590229.
Proteomic databases
PaxDb	Q08426.
PRIDE	Q08426.
Protocols and materials databases
DNASU	1962.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000231887; ENSP00000231887; ENSG00000113790. ENST00000456310; ENSP00000387746; ENSG00000113790.
GeneID	1962.
KEGG	hsa:1962.
UCSC	uc003fpf.3. human.
Organism-specific databases
CTD	1962.
GeneCards	GC03M184908.
HGNC	HGNC:3247. EHHADH.
HPA	HPA036401.
MIM	607037. gene.
neXtProt	NX_Q08426.
Orphanet	50812. Zellweger-like syndrome without peroxisomal anomalies.
PharmGKB	PA27682.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1250.
HOGENOM	HOG000261347.
HOVERGEN	HBG104990.
InParanoid	Q08426.
KO	K07514.
OMA	NYEAQVK.
OrthoDB	EOG47PX5F.
PhylomeDB	Q08426.
Enzyme and pathway databases
UniPathway	UPA00659.
Gene expression databases
ArrayExpress	Q08426.
Bgee	Q08426.
CleanEx	HS_EHHADH.
Genevestigator	Q08426.
GermOnline	ENSG00000113790. Homo sapiens.
Family and domain databases
Gene3D	1.10.1040.10. 2 hits. 3.40.50.720. 1 hit.
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR008927. 6-PGluconate_DH_C-like. IPR001753. Crotonase_core_superfam. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 2 hits.
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00157. NADH.
GenomeRNAi	1962.
NextBio	7961.
SOURCE	Search...

Entry information

Entry name

ECHP_HUMAN

Accession

Primary (citable) accession number: Q08426
Secondary accession number(s): A8K6Y3 , B4DWG3, D3DNU0, Q58EZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.