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Q9DBM2

- ECHP_MOUSE

UniProt

Q9DBM2 - ECHP_MOUSE

Protein

Peroxisomal bifunctional enzyme

Gene

Ehhadh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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.
    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.
    InParanoidiQ91W49.
    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

    MAEYLRLPHS LAMIRLCNPP VNAISPTVIT EVRNGLQKAS LDHTVRAIVI    50
    CGANDNFCAG ADIHGFKSPT GLTLGSLVDE IQRYQKPVVA AIQGVALGGG 100
    LELALGCHYR IANAKARVGF PEVMLGILPG ARGTQLLPRV VGVPVALDLI 150
    TSGRHISTDE ALKLGILDVV VKSDPVEEAI KFAQTVIGKP IEPRRILNKP 200
    VPSLPNMDSV FAEAIAKVRK QYPGRLAPET CVRSVQASVK HPYEVAIKEE 250
    AKLFMYLRGS GQARALQYAF FAEKSANKWS TPSGASWKTA SAQPVSSVGV 300
    LGLGTMGRGI AISFARVGIP VVAVESDPKQ LDTAKKIITS TLEKEASKSG 350
    QASAKPNLRF SSSTKELSSV DLVIEAVFED MNLKKKVFAE LSALCKPGAF 400
    LCTNTSALDV DDIASSTDRP QLVIGTHFFS PAHIMRLLEV IPSRYSSPTT 450
    IATVMSLSKR IGKIGVVVGN CYGFVGNRML APYYNQGYFL IEEGSKPEDV 500
    DGVLEEFGFR MGPFRVSDLA GLDVGWKVRK GQGLTGPSLP PGTPTRKRGN 550
    TRYSPIADML CEAGRFGQKT GKGWYQYDKP LGRIHKPDPW LSEFLSQYRE 600
    THHIKQRSIS KEEILERCLY SLINEAFRIL EEGMAASPEH IDVIYLHGYG 650
    WPRHVGGPMY YAASVGLPTV LEKLQKYYRQ NPDIPQLEPS DYLRRLVAQG 700
    SPPLKEWQSL AGPHSSKL 718
    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 Q91W49.
    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.
    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 1, 2014
    This is version 127 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