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Q54DD0

- AMPD_DICDI

UniProt

Q54DD0 - AMPD_DICDI

Protein

AMP deaminase

Gene

amdA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    AMP deaminase plays a critical role in energy metabolism.1 Publication

    Catalytic activityi

    AMP + H2O = IMP + NH3.

    Cofactori

    Zinc.Curated
    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Activated by ATP, inhibited by GTP, EDTA and inorganic phosphate.

    Kineticsi

    1. KM=1.6 mM for AMP1 Publication

    Vmax=1.0 mmol/min/mg enzyme1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi221 – 2211Zinc; catalyticBy similarity
    Metal bindingi223 – 2231Zinc; catalyticBy similarity
    Binding sitei223 – 2231SubstrateBy similarity
    Metal bindingi488 – 4881Zinc; catalyticBy similarity
    Binding sitei491 – 4911SubstrateBy similarity
    Active sitei510 – 5101Proton acceptorPROSITE-ProRule annotation
    Metal bindingi565 – 5651Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. AMP deaminase activity Source: dictyBase
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. IMP salvage Source: UniProtKB-UniPathway
    2. multicellular organismal development Source: UniProtKB-KW
    3. purine ribonucleoside monophosphate metabolic process Source: dictyBase
    4. sporulation resulting in formation of a cellular spore Source: dictyBase

    Keywords - Molecular functioni

    Developmental protein, Hydrolase

    Keywords - Biological processi

    Differentiation, Nucleotide metabolism, Sporulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00591; UER00663.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AMP deaminase (EC:3.5.4.6)
    Gene namesi
    Name:amdA
    ORF Names:DDB_G0292266
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 6, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0292266. amdA.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells grow normally until development occurs. Then they make a significantly increased proportion of prestalk cells, and develop fruiting bodies with short thick stalks and glassy sori with less than 5% normal spores. They have an increased content of pstA-type prestalk cells. Intracellular levels of inosine increase dramatically during development. This is cell autonomous, as the presence of equal numbers of wild-type cells does not alter the cell type proportion nor improve sporulation. Overexpression of the gene has no apparent effect on development (PubMed:11784104). Mutants lacking amdA form aspidocytes (a cell type able to resist detergent lysis and which are also resistant to some antibiotics) more readily than wild-type cells; their induction may involve AMP or other purine metabolites (PubMed:17259634).2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 790790AMP deaminasePRO_0000327654Add
    BLAST

    Proteomic databases

    PRIDEiQ54DD0.

    Expressioni

    Developmental stagei

    Expressed during normal growth and slightly more for the first 4 hours of development. Enzymatic activity increases for the first 5 hours of development and then tapers off.2 Publications

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi44689.DDB_0191089.

    Structurei

    3D structure databases

    ProteinModelPortaliQ54DD0.
    SMRiQ54DD0. Positions 48-656.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni292 – 2976Substrate bindingBy similarity
    Regioni566 – 5694Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi745 – 78541Asn-richAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1816.
    KOiK01490.
    OMAiYENDSAY.
    PhylomeDBiQ54DD0.

    Family and domain databases

    InterProiIPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view]
    PANTHERiPTHR11359. PTHR11359. 1 hit.
    PfamiPF00962. A_deaminase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
    PROSITEiPS00485. A_DEAMINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q54DD0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPLRGSSP QVSFYESELD QEGGSDASHF TYRNYMEDDK INSFTFNMAR    50
    KDQTQLFQRI ILTNESESEI EEYAEVAEQL LDAINLREKY VFHPKIWKAD 100
    APVGEKPPYS PFESDESTNC ATEHMFKEVN GVYFVYSNET DMKSNKALFS 150
    VPHTLASYYK DINNLMMLSS YGPAKTFTFK RLQLLESKFN MHTLLNDSLE 200
    LFQQKTAPHR DFYNVRKVDT HVHHSSSMNQ KHLLKFIKRK LKENPNEIVI 250
    FRDDKYLTLA EVFKSLNLDV DELSVDTLDV HADNNTFHRF DKFNLKYNPC 300
    GQSRLREIFL KTDNLIKGKY LAEISKEVFT DLESSKYQCA EYRLSIYGRK 350
    MSEWDTLASW IVDNDLFSTK VRWLIQVPRL YDVYRETSTT TFQDFLNNVF 400
    HPLFEVTKDP SSHPKLHLFL QQVVGIDCVD DESKFEKKFT EKFPVPGEWS 450
    SEHNPPYTYY LYYLYANLYT LNQFREEKGL NILTLRPHSG EAGEVDHMGA 500
    AFYLAHGINH GINLRKTPVL QYLYYLTQIG IAMSPLSNNS LFLTYNRNPF 550
    PAFFARGLNV SISTDDPLQF HYTKEPLMEE YSIATQVWRL SVCDICEIAR 600
    NSVLQSGFEH NVKSHWLGPD YANSGGNDIK KTNISDIRVC FRNETLIEEL 650
    HLILKSLQTL PNFKNLNINF LLDKLPSEIT TGNDYKLKKA QLKLNGANKL 700
    RNSSVGSTPN NGTPSSSGTP SLSSPGAIVH LMKTKPYIPP PLSLNIKQEN 750
    NNNNNNNNNN NNNNNNNNTN TNTNSNSTTT NQDDNSKSDK 790
    Length:790
    Mass (Da):90,954
    Last modified:May 24, 2005 - v1
    Checksum:i51ECE82FAA5C6C18
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000189 Genomic DNA. Translation: EAL61257.1.
    AF238311 Genomic DNA. Translation: AAF65407.1.
    RefSeqiXP_629711.1. XM_629709.1.

    Genome annotation databases

    EnsemblProtistsiDDB0191089; DDB0191089; DDB_G0292266.
    GeneIDi8628625.
    KEGGiddi:DDB_G0292266.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000189 Genomic DNA. Translation: EAL61257.1 .
    AF238311 Genomic DNA. Translation: AAF65407.1 .
    RefSeqi XP_629711.1. XM_629709.1.

    3D structure databases

    ProteinModelPortali Q54DD0.
    SMRi Q54DD0. Positions 48-656.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0191089.

    Proteomic databases

    PRIDEi Q54DD0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0191089 ; DDB0191089 ; DDB_G0292266 .
    GeneIDi 8628625.
    KEGGi ddi:DDB_G0292266.

    Organism-specific databases

    dictyBasei DDB_G0292266. amdA.

    Phylogenomic databases

    eggNOGi COG1816.
    KOi K01490.
    OMAi YENDSAY.
    PhylomeDBi Q54DD0.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00663 .

    Family and domain databases

    InterProi IPR006650. A/AMP_deam_AS.
    IPR001365. A/AMP_deaminase_dom.
    IPR006329. AMPD.
    [Graphical view ]
    PANTHERi PTHR11359. PTHR11359. 1 hit.
    Pfami PF00962. A_deaminase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
    PROSITEi PS00485. A_DEAMINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    2. "Altered cell-type proportioning in Dictyostelium lacking adenosine monophosphate deaminase."
      Chae S.-C., Fuller D., Loomis W.F.
      Dev. Biol. 241:183-194(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-790, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
      Strain: AX4.
    3. "Purification and characterization of developmentally regulated AMP deaminase from Dictyostelium discoideum."
      Malliaros D.P., Kozwich D.L., Jahngen E.G.E.
      Differentiation 46:153-160(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
      Strain: AX3.
    4. "A new environmentally resistant cell type from Dictyostelium."
      Serafimidis I., Bloomfield G., Skelton J., Ivens A., Kay R.R.
      Microbiology 153:619-630(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN ASPIDOCYTE FORMATION.
      Strain: AX2.

    Entry informationi

    Entry nameiAMPD_DICDI
    AccessioniPrimary (citable) accession number: Q54DD0
    Secondary accession number(s): Q9NGX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3