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Q9DCU9

- HOGA1_MOUSE

UniProt

Q9DCU9 - HOGA1_MOUSE

Protein

4-hydroxy-2-oxoglutarate aldolase, mitochondrial

Gene

Hoga1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the final step in the metabolic pathway of hydroxyproline.By similarity

    Catalytic activityi

    4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate.

    Enzyme regulationi

    Inhibited by divalent cations.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei162 – 1621Involved in proton transfer during cleavageBy similarity
    Active sitei190 – 1901Schiff-base intermediate with substrateBy similarity
    Binding sitei192 – 1921SubstrateBy similarity
    Binding sitei216 – 2161Substrate; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. 4-hydroxy-2-oxoglutarate aldolase activity Source: UniProtKB

    GO - Biological processi

    1. 4-hydroxyproline catabolic process Source: Ensembl
    2. glyoxylate catabolic process Source: UniProtKB
    3. oxalate metabolic process Source: Ensembl
    4. pyruvate biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Schiff base

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxy-2-oxoglutarate aldolase, mitochondrial (EC:4.1.3.16)
    Alternative name(s):
    Dihydrodipicolinate synthase-like
    Short name:
    DHDPS-like protein
    Probable 2-keto-4-hydroxyglutarate aldolase
    Short name:
    Probable KHG-aldolase
    Gene namesi
    Name:Hoga1
    Synonyms:Dhdpsl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1914682. Hoga1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2323MitochondrionBy similarityAdd
    BLAST
    Chaini24 – 3212984-hydroxy-2-oxoglutarate aldolase, mitochondrialPRO_0000273347Add
    BLAST

    Proteomic databases

    MaxQBiQ9DCU9.
    PaxDbiQ9DCU9.
    PRIDEiQ9DCU9.

    PTM databases

    PhosphoSiteiQ9DCU9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9DCU9.
    BgeeiQ9DCU9.
    CleanExiMM_0610010D20RIK.
    GenevestigatoriQ9DCU9.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    IntActiQ9DCU9. 2 interactions.
    MINTiMINT-1860303.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DCU9.
    SMRiQ9DCU9. Positions 27-321.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni71 – 722Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the DapA family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0329.
    GeneTreeiENSGT00530000063604.
    HOVERGENiHBG081405.
    InParanoidiQ9DCU9.
    KOiK18123.
    OMAiLADHENI.
    PhylomeDBiQ9DCU9.
    TreeFamiTF324600.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR002220. DapA-like.
    IPR020625. Dihydrodipicolinate_synth_AS.
    [Graphical view]
    PANTHERiPTHR12128. PTHR12128. 1 hit.
    PfamiPF00701. DHDPS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001365. DHDPS. 1 hit.
    PRINTSiPR00146. DHPICSNTHASE.
    PROSITEiPS00666. DHDPS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9DCU9-1 [UniParc]FASTAAdd to Basket

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    MLGPQIWASM RQGLSRGLSR NVKGKKVDIA GIYPPVTTPF TATAEVDYGK    50
    LEENLNRLAT FPFRGFVVQG STGEFPFLTS LERLEVVSRV RQAIPKDKFL 100
    IAGSGCESTQ ATVEMTVSMA QVGADVAMVV TPCYYRGRMS SAALIHHYTK 150
    VADVSPIPVV LYSVPANTGL ELPVDAVVTL SQHPNIIGLK DSGGDVTRIG 200
    LIVHKTSKQD FQVLAGSAGF LLASYAVGAV GGICGLANVL GAQVCQLERL 250
    CLTGQWEAAQ ELQHRLIEPN TAVTRRFGIP GLKKTMDWFG YYGGPCRAPL 300
    QELSPTEEEA LRLDFSNNGW L 321
    Length:321
    Mass (Da):34,644
    Last modified:June 1, 2001 - v1
    Checksum:i75B3DC959756D5A7
    GO

    Sequence cautioni

    The sequence BAB27226.1 differs from that shown. Reason: Frameshift at position 270.
    The sequence AAH16430.1 differs from that shown. Reason: Erroneous termination at position 322. Translated as stop.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251K → M in BAB27226. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002457 mRNA. Translation: BAB22114.1.
    AK010857 mRNA. Translation: BAB27226.1. Frameshift.
    BC016430 mRNA. Translation: AAH16430.1. Sequence problems.
    CCDSiCCDS29820.1.
    RefSeqiNP_080428.1. NM_026152.1.
    UniGeneiMm.24196.

    Genome annotation databases

    EnsembliENSMUST00000081714; ENSMUSP00000080414; ENSMUSG00000025176.
    GeneIDi67432.
    KEGGimmu:67432.
    UCSCiuc008hnb.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002457 mRNA. Translation: BAB22114.1 .
    AK010857 mRNA. Translation: BAB27226.1 . Frameshift.
    BC016430 mRNA. Translation: AAH16430.1 . Sequence problems.
    CCDSi CCDS29820.1.
    RefSeqi NP_080428.1. NM_026152.1.
    UniGenei Mm.24196.

    3D structure databases

    ProteinModelPortali Q9DCU9.
    SMRi Q9DCU9. Positions 27-321.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9DCU9. 2 interactions.
    MINTi MINT-1860303.

    PTM databases

    PhosphoSitei Q9DCU9.

    Proteomic databases

    MaxQBi Q9DCU9.
    PaxDbi Q9DCU9.
    PRIDEi Q9DCU9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081714 ; ENSMUSP00000080414 ; ENSMUSG00000025176 .
    GeneIDi 67432.
    KEGGi mmu:67432.
    UCSCi uc008hnb.1. mouse.

    Organism-specific databases

    CTDi 112817.
    MGIi MGI:1914682. Hoga1.

    Phylogenomic databases

    eggNOGi COG0329.
    GeneTreei ENSGT00530000063604.
    HOVERGENi HBG081405.
    InParanoidi Q9DCU9.
    KOi K18123.
    OMAi LADHENI.
    PhylomeDBi Q9DCU9.
    TreeFami TF324600.

    Miscellaneous databases

    ChiTaRSi HOGA1. mouse.
    NextBioi 324548.
    PROi Q9DCU9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DCU9.
    Bgeei Q9DCU9.
    CleanExi MM_0610010D20RIK.
    Genevestigatori Q9DCU9.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR002220. DapA-like.
    IPR020625. Dihydrodipicolinate_synth_AS.
    [Graphical view ]
    PANTHERi PTHR12128. PTHR12128. 1 hit.
    Pfami PF00701. DHDPS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001365. DHDPS. 1 hit.
    PRINTSi PR00146. DHPICSNTHASE.
    PROSITEi PS00666. DHDPS_2. 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: Kidney and Liver.
    2. "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.

    Entry informationi

    Entry nameiHOGA1_MOUSE
    AccessioniPrimary (citable) accession number: Q9DCU9
    Secondary accession number(s): Q91W74, Q9CY60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3