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Q54DD0 (AMPD_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AMP deaminase

EC=3.5.4.6
Gene names
Name:amdA
ORF Names:DDB_G0292266
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length790 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

AMP deaminase plays a critical role in energy metabolism. Ref.4

Catalytic activity

AMP + H2O = IMP + NH3.

Cofactor

Zinc Potential.

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

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

Pathway

Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.

Subunit structure

Homodimer. Ref.3

Subcellular location

Cytoplasm Probable Ref.3.

Developmental stage

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. Ref.2 Ref.3

Disruption phenotype

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 (Ref.2). 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 (Ref.4). Ref.2

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Biophysicochemical properties

Kinetic parameters:

KM=1.6 mM for AMP Ref.3

Vmax=1.0 mmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 790790AMP deaminase
PRO_0000327654

Regions

Region292 – 2976Substrate binding By similarity
Region566 – 5694Substrate binding By similarity
Compositional bias745 – 78541Asn-rich

Sites

Active site5101Proton acceptor By similarity
Metal binding2211Zinc; catalytic By similarity
Metal binding2231Zinc; catalytic By similarity
Metal binding4881Zinc; catalytic By similarity
Metal binding5651Zinc; catalytic By similarity
Binding site2231Substrate By similarity
Binding site4911Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q54DD0 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 51ECE82FAA5C6C18

FASTA79090,954
        10         20         30         40         50         60 
MSTPLRGSSP QVSFYESELD QEGGSDASHF TYRNYMEDDK INSFTFNMAR KDQTQLFQRI 

        70         80         90        100        110        120 
ILTNESESEI EEYAEVAEQL LDAINLREKY VFHPKIWKAD APVGEKPPYS PFESDESTNC 

       130        140        150        160        170        180 
ATEHMFKEVN GVYFVYSNET DMKSNKALFS VPHTLASYYK DINNLMMLSS YGPAKTFTFK 

       190        200        210        220        230        240 
RLQLLESKFN MHTLLNDSLE LFQQKTAPHR DFYNVRKVDT HVHHSSSMNQ KHLLKFIKRK 

       250        260        270        280        290        300 
LKENPNEIVI FRDDKYLTLA EVFKSLNLDV DELSVDTLDV HADNNTFHRF DKFNLKYNPC 

       310        320        330        340        350        360 
GQSRLREIFL KTDNLIKGKY LAEISKEVFT DLESSKYQCA EYRLSIYGRK MSEWDTLASW 

       370        380        390        400        410        420 
IVDNDLFSTK VRWLIQVPRL YDVYRETSTT TFQDFLNNVF HPLFEVTKDP SSHPKLHLFL 

       430        440        450        460        470        480 
QQVVGIDCVD DESKFEKKFT EKFPVPGEWS SEHNPPYTYY LYYLYANLYT LNQFREEKGL 

       490        500        510        520        530        540 
NILTLRPHSG EAGEVDHMGA AFYLAHGINH GINLRKTPVL QYLYYLTQIG IAMSPLSNNS 

       550        560        570        580        590        600 
LFLTYNRNPF PAFFARGLNV SISTDDPLQF HYTKEPLMEE YSIATQVWRL SVCDICEIAR 

       610        620        630        640        650        660 
NSVLQSGFEH NVKSHWLGPD YANSGGNDIK KTNISDIRVC FRNETLIEEL HLILKSLQTL 

       670        680        690        700        710        720 
PNFKNLNINF LLDKLPSEIT TGNDYKLKKA QLKLNGANKL RNSSVGSTPN NGTPSSSGTP 

       730        740        750        760        770        780 
SLSSPGAIVH LMKTKPYIPP PLSLNIKQEN NNNNNNNNNN NNNNNNNNTN TNTNSNSTTT 

       790 
NQDDNSKSDK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000189 Genomic DNA. Translation: EAL61257.1.
AF238311 Genomic DNA. Translation: AAF65407.1.

3D structure databases

ProteinModelPortalQ54DD0.
SMRQ54DD0. Positions 48-656.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0191089.

Proteomic databases

PRIDEQ54DD0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0191089; DDB0191089; DDB_G0292266.
KEGGddi:DDB_G0292266.

Organism-specific databases

dictyBaseDDB_G0292266. amdA.

Phylogenomic databases

eggNOGCOG1816.
KOK01490.
OMAYENDSAY.
PhylomeDBQ54DD0.

Enzyme and pathway databases

UniPathwayUPA00591; UER00663.

Family and domain databases

InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMP_deaminase.
[Graphical view]
PANTHERPTHR11359. PTHR11359. 1 hit.
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01429. AMP_deaminase. 1 hit.
PROSITEPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPD_DICDI
AccessionPrimary (citable) accession number: Q54DD0
Secondary accession number(s): Q9NGX0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase