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Q9DBM2

- ECHP_MOUSE

UniProt

Q9DBM2 - ECHP_MOUSE

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Protein

Peroxisomal bifunctional enzyme

Gene

Ehhadh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

(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 regulationi

Enzyme activity enhanced by acetylation.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991Substrate; via amide nitrogenBy similarity
Sitei102 – 1021Important for catalytic activityBy similarity
Sitei122 – 1221Important for catalytic activityBy similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: MGI
  2. coenzyme binding Source: InterPro
  3. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-EC
  4. enoyl-CoA hydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. acyl-CoA metabolic process Source: MGI
  2. fatty acid beta-oxidation Source: MGI
  3. internal protein amino acid acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal bifunctional enzyme
Short name:
PBE
Short name:
PBFE
Including the following 2 domains:
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)
Gene namesi
Name:Ehhadh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1277964. Ehhadh.

Subcellular locationi

Peroxisome By similarity

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. mitochondrion Source: MGI
  3. nucleus Source: Ensembl
  4. peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 718718Peroxisomal bifunctional enzymePRO_0000109248Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-succinyllysine1 Publication
Modified residuei163 – 1631N6-acetyllysine; alternateBy similarity
Modified residuei163 – 1631N6-succinyllysine; alternate1 Publication
Modified residuei172 – 1721N6-acetyllysine; alternate1 Publication
Modified residuei172 – 1721N6-succinyllysine; alternate1 Publication
Modified residuei181 – 1811N6-succinyllysine1 Publication
Modified residuei189 – 1891N6-acetyllysine; alternate1 Publication
Modified residuei189 – 1891N6-succinyllysine; alternate1 Publication
Modified residuei217 – 2171N6-acetyllysine; alternate1 Publication
Modified residuei217 – 2171N6-succinyllysine; alternate1 Publication
Modified residuei240 – 2401N6-succinyllysine1 Publication
Modified residuei248 – 2481N6-acetyllysine1 Publication
Modified residuei252 – 2521N6-succinyllysine1 Publication
Modified residuei274 – 2741N6-acetyllysine; alternate1 Publication
Modified residuei274 – 2741N6-succinyllysine; alternate1 Publication
Modified residuei278 – 2781N6-succinyllysine1 Publication
Modified residuei288 – 2881N6-succinyllysine1 Publication
Modified residuei329 – 3291N6-succinyllysine1 Publication
Modified residuei344 – 3441N6-acetyllysine1 Publication
Modified residuei348 – 3481N6-acetyllysine1 Publication
Modified residuei355 – 3551N6-acetyllysine1 Publication
Modified residuei459 – 4591N6-acetyllysine1 Publication
Modified residuei527 – 5271N6-succinyllysine1 Publication
Modified residuei572 – 5721N6-succinyllysine1 Publication
Modified residuei579 – 5791N6-acetyllysine; alternate1 Publication
Modified residuei579 – 5791N6-succinyllysine; alternate1 Publication
Modified residuei586 – 5861N6-acetyllysine; alternate1 Publication
Modified residuei586 – 5861N6-succinyllysine; alternate1 Publication
Modified residuei705 – 7051N6-acetyllysine; alternate1 Publication
Modified residuei705 – 7051N6-succinyllysine; alternate1 Publication
Modified residuei717 – 7171N6-succinyllysine1 Publication

Post-translational modificationi

Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-344. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9DBM2.
PaxDbiQ9DBM2.
PRIDEiQ9DBM2.

PTM databases

PhosphoSiteiQ9DBM2.

Expressioni

Gene expression databases

BgeeiQ9DBM2.
ExpressionAtlasiQ9DBM2. baseline and differential.
GenevestigatoriQ9DBM2.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ9DBM2. 5 interactions.
MINTiMINT-4121269.

Structurei

3D structure databases

ProteinModelPortaliQ9DBM2.
SMRiQ9DBM2. Positions 1-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 280280Enoyl-CoA hydratase / isomeraseAdd
BLAST
Regioni281 – 5672873-hydroxyacyl-CoA dehydrogenaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi716 – 7183Microbody targeting signalBy similarity

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiQ9DBM2.
KOiK07514.
OMAiLKMRKQH.
OrthoDBiEOG725DH0.
TreeFamiTF316708.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBM2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEYLRLPHS LAMIRLCNPP VNAISPTVIT EVRNGLQKAS LDHTVRAIVI
60 70 80 90 100
CGANDNFCAG ADIHGFKSPT GLTLGSLVDE IQRYQKPVVA AIQGVALGGG
110 120 130 140 150
LELALGCHYR IANAKARVGF PEVMLGILPG ARGTQLLPRV VGVPVALDLI
160 170 180 190 200
TSGRHISTDE ALKLGILDVV VKSDPVEEAI KFAQTVIGKP IEPRRILNKP
210 220 230 240 250
VPSLPNMDSV FAEAIAKVRK QYPGRLAPET CVRSVQASVK HPYEVAIKEE
260 270 280 290 300
AKLFMYLRGS GQARALQYAF FAEKSANKWS TPSGASWKTA SAQPVSSVGV
310 320 330 340 350
LGLGTMGRGI AISFARVGIP VVAVESDPKQ LDTAKKIITS TLEKEASKSG
360 370 380 390 400
QASAKPNLRF SSSTKELSSV DLVIEAVFED MNLKKKVFAE LSALCKPGAF
410 420 430 440 450
LCTNTSALDV DDIASSTDRP QLVIGTHFFS PAHIMRLLEV IPSRYSSPTT
460 470 480 490 500
IATVMSLSKR IGKIGVVVGN CYGFVGNRML APYYNQGYFL IEEGSKPEDV
510 520 530 540 550
DGVLEEFGFR MGPFRVSDLA GLDVGWKVRK GQGLTGPSLP PGTPTRKRGN
560 570 580 590 600
TRYSPIADML CEAGRFGQKT GKGWYQYDKP LGRIHKPDPW LSEFLSQYRE
610 620 630 640 650
THHIKQRSIS KEEILERCLY SLINEAFRIL EEGMAASPEH IDVIYLHGYG
660 670 680 690 700
WPRHVGGPMY YAASVGLPTV LEKLQKYYRQ NPDIPQLEPS DYLRRLVAQG
710
SPPLKEWQSL AGPHSSKL
Length:718
Mass (Da):78,301
Last modified:July 27, 2011 - v4
Checksum:iA405717EC7A3EBD9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti499 – 4991D → G in BAB23628. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK004867 mRNA. Translation: BAB23628.1.
BC016899 mRNA. Translation: AAH16899.1.
CH466521 Genomic DNA. Translation: EDK97607.1.
CCDSiCCDS28063.1.
RefSeqiNP_076226.2. NM_023737.3.
UniGeneiMm.28100.

Genome annotation databases

EnsembliENSMUST00000023559; ENSMUSP00000023559; ENSMUSG00000022853.
GeneIDi74147.
KEGGimmu:74147.
UCSCiuc007yrm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK004867 mRNA. Translation: BAB23628.1 .
BC016899 mRNA. Translation: AAH16899.1 .
CH466521 Genomic DNA. Translation: EDK97607.1 .
CCDSi CCDS28063.1.
RefSeqi NP_076226.2. NM_023737.3.
UniGenei Mm.28100.

3D structure databases

ProteinModelPortali Q9DBM2.
SMRi Q9DBM2. Positions 1-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9DBM2. 5 interactions.
MINTi MINT-4121269.

PTM databases

PhosphoSitei Q9DBM2.

Proteomic databases

MaxQBi Q9DBM2.
PaxDbi Q9DBM2.
PRIDEi Q9DBM2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023559 ; ENSMUSP00000023559 ; ENSMUSG00000022853 .
GeneIDi 74147.
KEGGi mmu:74147.
UCSCi uc007yrm.2. mouse.

Organism-specific databases

CTDi 1962.
MGIi MGI:1277964. Ehhadh.

Phylogenomic databases

eggNOGi COG1250.
GeneTreei ENSGT00720000108673.
HOGENOMi HOG000261347.
HOVERGENi HBG104990.
InParanoidi Q9DBM2.
KOi K07514.
OMAi LKMRKQH.
OrthoDBi EOG725DH0.
TreeFami TF316708.

Enzyme and pathway databases

UniPathwayi UPA00659 .

Miscellaneous databases

NextBioi 339902.
PROi Q9DBM2.
SOURCEi Search...

Gene expression databases

Bgeei Q9DBM2.
ExpressionAtlasi Q9DBM2. baseline and differential.
Genevestigatori Q9DBM2.

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-38; LYS-163; LYS-172; LYS-181; LYS-189; LYS-217; LYS-240; LYS-252; LYS-274; LYS-278; LYS-288; LYS-329; LYS-527; LYS-572; LYS-579; LYS-586; LYS-705 AND LYS-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-189; LYS-217; LYS-248; LYS-274; LYS-344; LYS-348; LYS-355; LYS-459; LYS-579; LYS-586 AND LYS-705, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiECHP_MOUSE
AccessioniPrimary (citable) accession number: Q9DBM2
Secondary accession number(s): Q91W49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3