Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5KPU2

- MTAP_CRYNJ

UniProt

Q5KPU2 - MTAP_CRYNJ

Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

CNA01530

Organism
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.UniRule annotation

    Catalytic activityi

    S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei15 – 151PhosphateUniRule annotation
    Sitei178 – 1781Important for substrate specificityUniRule annotation
    Binding sitei196 – 1961Substrate; via amide nitrogenUniRule annotation
    Binding sitei197 – 1971PhosphateUniRule annotation
    Sitei233 – 2331Important for substrate specificityUniRule annotation

    GO - Molecular functioni

    1. phosphorylase activity Source: InterPro
    2. S-methyl-5-thioadenosine phosphorylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB-HAMAP
    2. purine ribonucleoside salvage Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Enzyme and pathway databases

    UniPathwayiUPA00904; UER00873.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-methyl-5'-thioadenosine phosphorylaseUniRule annotation (EC:2.4.2.28UniRule annotation)
    Alternative name(s):
    5'-methylthioadenosine phosphorylaseUniRule annotation
    Short name:
    MTA phosphorylaseUniRule annotation
    Short name:
    MTAPUniRule annotation
    Short name:
    MTAPaseUniRule annotation
    Gene namesi
    Ordered Locus Names:CNA01530
    OrganismiCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
    Taxonomic identifieri214684 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex
    ProteomesiUP000002149: Chromosome 1

    Subcellular locationi

    Cytoplasm UniRule annotation. Nucleus UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 303303S-methyl-5'-thioadenosine phosphorylasePRO_0000415127Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi214684.CNA01530.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5KPU2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 592Phosphate bindingUniRule annotation
    Regioni91 – 922Phosphate bindingUniRule annotation
    Regioni220 – 2223Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000228986.
    KOiK00772.
    OrthoDBiEOG77DJGM.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    HAMAPiMF_01963. MTAP.
    InterProiIPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01694. MTAP. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5KPU2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENNEKVLVG CIGGSGLYHL DNLTFVKTVH IETPWGKPSS PINISSLPSG    50
    ALVAFISRHG SHHSITPSEV PCRANIAALK HIGCEAIIAF SAVGSLREEI 100
    APGHFIIPDQ IIDRTKGIRE DTFFRGEGLV VHSMFGEPFS QKLNAFVAPR 150
    VEKILKETGD VVLHTGKTVV CMEGPAFSTR AESLMYRQWG GDIINMSVIP 200
    EAKLAREAEL DYTLICTSTD FDAWRTGYDP VTVEEVVKVL HTNAGNSRAV 250
    AAGILQDVHD VVVEGKTLTD IKGSMKFACV TRKDIQPEAS RKKLSYILPY 300
    FSD 303
    Length:303
    Mass (Da):33,121
    Last modified:February 15, 2005 - v1
    Checksum:i852840F01808DC68
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017341 Genomic DNA. Translation: AAW40807.1.
    RefSeqiXP_566626.1. XM_566626.1.

    Genome annotation databases

    EnsemblFungiiAAW40807; AAW40807; CNA01530.
    GeneIDi3253655.
    KEGGicne:CNA01530.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017341 Genomic DNA. Translation: AAW40807.1 .
    RefSeqi XP_566626.1. XM_566626.1.

    3D structure databases

    ProteinModelPortali Q5KPU2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 214684.CNA01530.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii AAW40807 ; AAW40807 ; CNA01530 .
    GeneIDi 3253655.
    KEGGi cne:CNA01530.

    Phylogenomic databases

    HOGENOMi HOG000228986.
    KOi K00772.
    OrthoDBi EOG77DJGM.

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00873 .

    Family and domain databases

    Gene3Di 3.40.50.1580. 1 hit.
    HAMAPi MF_01963. MTAP.
    InterProi IPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view ]
    PANTHERi PTHR11904. PTHR11904. 1 hit.
    Pfami PF01048. PNP_UDP_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53167. SSF53167. 1 hit.
    TIGRFAMsi TIGR01694. MTAP. 1 hit.
    PROSITEi PS01240. PNP_MTAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans."
      Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S.
      , Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.
      Science 307:1321-1324(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JEC21 / ATCC MYA-565.

    Entry informationi

    Entry nameiMTAP_CRYNJ
    AccessioniPrimary (citable) accession number: Q5KPU2
    Secondary accession number(s): Q560U2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3