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Protein

AMP deaminase

Gene

ada1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

AMP deaminase plays a critical role in energy metabolism.

Catalytic activityi

AMP + H2O = IMP + NH3.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi319 – 3191Zinc; catalyticBy similarity
Metal bindingi321 – 3211Zinc; catalyticBy similarity
Binding sitei321 – 3211SubstrateBy similarity
Metal bindingi587 – 5871Zinc; catalyticBy similarity
Binding sitei590 – 5901SubstrateBy similarity
Active sitei609 – 6091Proton acceptorPROSITE-ProRule annotation
Metal bindingi664 – 6641Zinc; catalyticBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. IMP salvage Source: UniProtKB-UniPathway
  2. regulation of transcription from RNA polymerase II promoter Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_206933. Purine salvage.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase (EC:3.5.4.6)
Alternative name(s):
Myoadenylate deaminase
Gene namesi
Name:ada1
ORF Names:SPBC106.04
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC106.04.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 831831AMP deaminasePRO_0000194413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791Phosphoserine1 Publication
Modified residuei84 – 841Phosphoserine1 Publication
Modified residuei758 – 7581Phosphoserine1 Publication
Modified residuei776 – 7761Phosphoserine1 Publication
Modified residuei780 – 7801Phosphoserine1 Publication
Modified residuei782 – 7821Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP50998.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi276642. 73 interactions.
MINTiMINT-4690806.
STRINGi4896.SPBC106.04-1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 3956Substrate bindingBy similarity
Regioni665 – 6684Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
HOGENOMiHOG000092200.
InParanoidiP50998.
KOiK01490.
OrthoDBiEOG7N63W7.

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]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50998-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNMEQEDDQV PAVAAETVPL KRYVTNPGAN RDEEVAAAPS SQDTPYFDYA
60 70 80 90 100
YERSLRHQDA KFLAMNGTQN GRDGLPSKSP RRPSVSASTV RNSDDVNHSK
110 120 130 140 150
AGPGSGKLLN DTLQSKISSI HMPHVQQGDN AVVSSVGGPE TDPGNMETTD
160 170 180 190 200
PLFSDELAEI YLSIHKCMDM RHKYIRVSLQ GELDNPIDDD SWIIYPDCKE
210 220 230 240 250
GEDDTGLFNF ADCKIPGIEN EMEYHMDHQG IFQVYENDSA YIAGTPSFHI
260 270 280 290 300
PTIRDYYIDL EFLLSASSDG PSKSFSFRRL QYLEGRWNMY MLLNEYQELA
310 320 330 340 350
DTKKVPHRDF YNVRKVDTHV HHSALANQKH LLRFIKAKLR KCPNEKVIWR
360 370 380 390 400
DGKFLTLQEV FDSLKLTSYD LSIDTLDMHA HTDTFHRFDK FNLKYNPIGE
410 420 430 440 450
SRLRTIFLKT DNDINGRYLA ELTKEVFTDL RTQKYQMAEY RISIYGRNRE
460 470 480 490 500
EWDKLAAWII DNELFSPNVR WLIQVPRLYD VYKKSGIVET FEEVVRNVFE
510 520 530 540 550
PLFEVTKDPR THPKLHVFLQ RVIGFDSVDD ESKPERRTFR KFPYPKHWDI
560 570 580 590 600
NLNPPYSYWL YYMYANMTSL NSWRKIRGFN TFVLRPHCGE AGDTDHLASA
610 620 630 640 650
FLLSHGINHG ILLRKVPFLQ YLWYLDQIPI AMSPLSNNAL FLAYDKNPFL
660 670 680 690 700
TYFKRGLNVS LSTDDPLQFA FTREPLIEEY AVAAQIYKLS AVDMCELARN
710 720 730 740 750
SVLQSGFERQ LKERWLGVDF QDIDRTNVPI IRLAYRALTL TQEIALVNKH
760 770 780 790 800
VQPSKHPSNH DLEELIHKYD AMTGTSDPLS ASPRTNDATI SSRLSLHDGH
810 820 830
DHGAFFPGLS VISERRRRKD SMASSSQDLK D
Length:831
Mass (Da):95,887
Last modified:July 11, 2012 - v3
Checksum:iF027B33C7AD0C63D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti468 – 50538NVRWL…PLFEV → TFVGLFKYLVCMMCIRSPVL LRLLKRSSEMSLNHCSKF in CAA62797 (Ref. 1) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91498 Genomic DNA. Translation: CAA62797.1. Sequence problems.
CU329671 Genomic DNA. Translation: CAB53720.2.
PIRiT39261.
RefSeqiNP_595153.2. NM_001021062.2.

Genome annotation databases

EnsemblFungiiSPBC106.04.1; SPBC106.04.1:pep; SPBC106.04.
GeneIDi2540105.
KEGGispo:SPBC106.04.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91498 Genomic DNA. Translation: CAA62797.1. Sequence problems.
CU329671 Genomic DNA. Translation: CAB53720.2.
PIRiT39261.
RefSeqiNP_595153.2. NM_001021062.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276642. 73 interactions.
MINTiMINT-4690806.
STRINGi4896.SPBC106.04-1.

Proteomic databases

MaxQBiP50998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC106.04.1; SPBC106.04.1:pep; SPBC106.04.
GeneIDi2540105.
KEGGispo:SPBC106.04.

Organism-specific databases

PomBaseiSPBC106.04.

Phylogenomic databases

eggNOGiCOG1816.
HOGENOMiHOG000092200.
InParanoidiP50998.
KOiK01490.
OrthoDBiEOG7N63W7.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00663.
ReactomeiREACT_206933. Purine salvage.

Miscellaneous databases

NextBioi20801241.

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]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Rochet M., Levesque H., Gaillardin C.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  4. "Yeast AMP deaminase. Catalytic activity in Schizosaccharomyces pombe and chromosomal location in Saccharomyces cerevisiae."
    Sollitti P., Merkler D.J., Estupinan B., Schramm V.L.
    J. Biol. Chem. 268:4549-4555(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  5. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-84; SER-758; SER-776; SER-780 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiAMPD_SCHPO
AccessioniPrimary (citable) accession number: P50998
Secondary accession number(s): Q9URV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 11, 2012
Last modified: January 7, 2015
This is version 105 of the entry and version 3 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.