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P22907

- HEM3_MOUSE

UniProt

P22907 - HEM3_MOUSE

Protein

Porphobilinogen deaminase

Gene

Hmbs

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.

    Catalytic activityi

    4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH3.

    Cofactori

    Binds 1 dipyrromethane group covalently.

    Pathwayi

    GO - Molecular functioni

    1. hydroxymethylbilane synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. peptidyl-pyrromethane cofactor linkage Source: InterPro
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_203298. Heme biosynthesis.
    UniPathwayiUPA00251; UER00319.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Porphobilinogen deaminase (EC:2.5.1.61)
    Short name:
    PBG-D
    Alternative name(s):
    Hydroxymethylbilane synthase
    Short name:
    HMBS
    Pre-uroporphyrinogen synthase
    Gene namesi
    Name:Hmbs
    Synonyms:Uros1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:96112. Hmbs.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 361360Porphobilinogen deaminasePRO_0000143035Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei74 – 741N6-acetyllysine1 Publication
    Modified residuei261 – 2611S-(dipyrrolylmethanemethyl)cysteineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP22907.
    PRIDEiP22907.

    Expressioni

    Gene expression databases

    ArrayExpressiP22907.
    BgeeiP22907.
    CleanExiMM_HMBS.
    GenevestigatoriP22907.

    Interactioni

    Protein-protein interaction databases

    BioGridi200321. 1 interaction.
    IntActiP22907. 1 interaction.
    MINTiMINT-4097350.

    Structurei

    3D structure databases

    ProteinModelPortaliP22907.
    SMRiP22907. Positions 18-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HMBS family.Curated

    Phylogenomic databases

    eggNOGiCOG0181.
    GeneTreeiENSGT00390000009083.
    HOGENOMiHOG000228587.
    HOVERGENiHBG000967.
    InParanoidiQ3TIV0.
    KOiK01749.
    OMAiGIECRTD.
    OrthoDBiEOG7W41C4.
    TreeFamiTF105389.

    Family and domain databases

    Gene3Di3.30.160.40. 1 hit.
    HAMAPiMF_00260. Porphobil_deam.
    InterProiIPR000860. 4pyrrol_synth_OHMeBilane_synth.
    IPR022419. Porphobilin_deaminase_cofac_BS.
    IPR022417. Porphobilin_deaminase_N.
    IPR022418. Porphobilinogen_deaminase_C.
    [Graphical view]
    PANTHERiPTHR11557. PTHR11557. 1 hit.
    PfamiPF01379. Porphobil_deam. 1 hit.
    PF03900. Porphobil_deamC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001438. 4pyrrol_synth_OHMeBilane_synth. 1 hit.
    PRINTSiPR00151. PORPHBDMNASE.
    SUPFAMiSSF54782. SSF54782. 2 hits.
    TIGRFAMsiTIGR00212. hemC. 1 hit.
    PROSITEiPS00533. PORPHOBILINOGEN_DEAM. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P22907-1) [UniParc]FASTAAdd to Basket

    Also known as: Non-erythropoietic

    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.

    « Hide

    MSGNGGAATT AEENGSKMRV IRVGTRKSQL ARIQTDTVVA MLKALYPGIQ    50
    FEIIAMSTTG DKILDTALSK IGEKSLFTKE LENALEKNEV DLVVHSLKDV 100
    PTILPPGFTI GAICKRENPC DAVVFHPKFI GKTLETLPEK SAVGTSSLRR 150
    VAQLQRKFPH LEFKSIRGNL NTRLRKLDEL QEFSAIVLAV AGLQRMGWQN 200
    RVGQILHPEE CMYAVGQGAL AVEVRAKDQD ILDLVSVLHD PETLLRCIAE 250
    RAFLRHLEGG CSVPVAVHTV MKDGQLYLTG GVWSLDGSDS MQETMQATIQ 300
    VPVQQEDGPE DDPQLVGITA RNIPRGAQLA AENLGISLAS LLLNKGAKNI 350
    LDVARQLNDV R 361
    Length:361
    Mass (Da):39,344
    Last modified:July 27, 2011 - v2
    Checksum:iF184C439F4F7B55D
    GO
    Isoform 2 (identifier: P22907-2) [UniParc]FASTAAdd to Basket

    Also known as: Erythrocyte

    The sequence of this isoform differs from the canonical sequence as follows:
         2-17: Missing.

    Show »
    Length:345
    Mass (Da):37,912
    Checksum:iD74599AABD83A6BA
    GO

    Sequence cautioni

    The sequence AAA39890.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361D → E in AAA39890. (PubMed:2768242)Curated
    Sequence conflicti36 – 361D → E in AAA39891. (PubMed:2768242)Curated
    Sequence conflicti64 – 641L → V in AAA39890. (PubMed:2768242)Curated
    Sequence conflicti64 – 641L → V in AAA39891. (PubMed:2768242)Curated
    Sequence conflicti117 – 1171E → Q in AAA39890. (PubMed:2768242)Curated
    Sequence conflicti117 – 1171E → Q in AAA39891. (PubMed:2768242)Curated
    Sequence conflicti160 – 1601H → N in AAA39890. (PubMed:2768242)Curated
    Sequence conflicti160 – 1601H → N in AAA39891. (PubMed:2768242)Curated
    Sequence conflicti271 – 2711M → I in AAA39890. (PubMed:2768242)Curated
    Sequence conflicti271 – 2711M → I in AAA39891. (PubMed:2768242)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 1716Missing in isoform 2. CuratedVSP_002068Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28666
    , M28663, M28664, M28665 Genomic DNA. Translation: AAA39890.1. Sequence problems.
    M28666
    , M28663, M28664, M28665 Genomic DNA. Translation: AAA39891.1.
    AK166734 mRNA. Translation: BAE38979.1.
    AK167702 mRNA. Translation: BAE39746.1.
    CCDSiCCDS23106.1. [P22907-1]
    PIRiA36513. IBMSN.
    RefSeqiNP_038579.2. NM_013551.2. [P22907-1]
    UniGeneiMm.247676.

    Genome annotation databases

    EnsembliENSMUST00000077353; ENSMUSP00000076575; ENSMUSG00000032126. [P22907-1]
    GeneIDi15288.
    KEGGimmu:15288.
    UCSCiuc009pcz.2. mouse. [P22907-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28666
    , M28663 , M28664 , M28665 Genomic DNA. Translation: AAA39890.1 . Sequence problems.
    M28666
    , M28663 , M28664 , M28665 Genomic DNA. Translation: AAA39891.1 .
    AK166734 mRNA. Translation: BAE38979.1 .
    AK167702 mRNA. Translation: BAE39746.1 .
    CCDSi CCDS23106.1. [P22907-1 ]
    PIRi A36513. IBMSN.
    RefSeqi NP_038579.2. NM_013551.2. [P22907-1 ]
    UniGenei Mm.247676.

    3D structure databases

    ProteinModelPortali P22907.
    SMRi P22907. Positions 18-356.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200321. 1 interaction.
    IntActi P22907. 1 interaction.
    MINTi MINT-4097350.

    Proteomic databases

    PaxDbi P22907.
    PRIDEi P22907.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000077353 ; ENSMUSP00000076575 ; ENSMUSG00000032126 . [P22907-1 ]
    GeneIDi 15288.
    KEGGi mmu:15288.
    UCSCi uc009pcz.2. mouse. [P22907-1 ]

    Organism-specific databases

    CTDi 3145.
    MGIi MGI:96112. Hmbs.

    Phylogenomic databases

    eggNOGi COG0181.
    GeneTreei ENSGT00390000009083.
    HOGENOMi HOG000228587.
    HOVERGENi HBG000967.
    InParanoidi Q3TIV0.
    KOi K01749.
    OMAi GIECRTD.
    OrthoDBi EOG7W41C4.
    TreeFami TF105389.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00319 .
    Reactomei REACT_203298. Heme biosynthesis.

    Miscellaneous databases

    NextBioi 287927.
    PROi P22907.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22907.
    Bgeei P22907.
    CleanExi MM_HMBS.
    Genevestigatori P22907.

    Family and domain databases

    Gene3Di 3.30.160.40. 1 hit.
    HAMAPi MF_00260. Porphobil_deam.
    InterProi IPR000860. 4pyrrol_synth_OHMeBilane_synth.
    IPR022419. Porphobilin_deaminase_cofac_BS.
    IPR022417. Porphobilin_deaminase_N.
    IPR022418. Porphobilinogen_deaminase_C.
    [Graphical view ]
    PANTHERi PTHR11557. PTHR11557. 1 hit.
    Pfami PF01379. Porphobil_deam. 1 hit.
    PF03900. Porphobil_deamC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001438. 4pyrrol_synth_OHMeBilane_synth. 1 hit.
    PRINTSi PR00151. PORPHBDMNASE.
    SUPFAMi SSF54782. SSF54782. 2 hits.
    TIGRFAMsi TIGR00212. hemC. 1 hit.
    PROSITEi PS00533. PORPHOBILINOGEN_DEAM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mouse porphobilinogen deaminase gene. Structural organization, sequence, and transcriptional analysis."
      Beaumont C., Porcher C., Picat C., Nordmann Y., Grandchamp B.
      J. Biol. Chem. 264:14829-14834(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
    2. "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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Amnion.
    3. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiHEM3_MOUSE
    AccessioniPrimary (citable) accession number: P22907
    Secondary accession number(s): Q3TIV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The porphobilinogen subunits are added to the dipyrromethane group.By similarity

    Keywords - Technical termi

    Complete proteome, 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