Q54DD0 (AMPD_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AMP deaminase
EC=3.5.4.6

Gene names

Name:	amdA
ORF Names:	DDB_G0292266

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	790 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Differentiation Nucleotide metabolism Sporulation
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Developmental protein Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	IMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW purine ribonucleoside monophosphate metabolic process Inferred from direct assay Ref.2. Source: dictyBase sporulation resulting in formation of a cellular spore Inferred from mutant phenotype Ref.2. Source: dictyBase
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	AMP deaminase activity Inferred from direct assay Ref.2. Source: dictyBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 790	790	AMP deaminase		PRO_0000327654
Regions
	Region	292 – 297	6	Substrate binding By similarity
	Region	566 – 569	4	Substrate binding By similarity
	Compositional bias	745 – 785	41	Asn-rich
Sites
	Active site	510	1	Proton acceptor By similarity
	Metal binding	221	1	Zinc; catalytic By similarity
	Metal binding	223	1	Zinc; catalytic By similarity
	Metal binding	488	1	Zinc; catalytic By similarity
	Metal binding	565	1	Zinc; catalytic By similarity
	Binding site	223	1	Substrate By similarity
	Binding site	491	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54DD0 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 51ECE82FAA5C6C18	FASTA	790	90,954
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
RefSeq	XP_629711.1. XM_629709.1.
3D structure databases
HSSP	HSSP built from PDB template 2A3L based on UniProtKB O80452.
ProteinModelPortal	Q54DD0.
SMR	Q54DD0. Positions 48-656.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0191089.
Proteomic databases
PRIDE	Q54DD0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0191089; DDB0191089; DDB_G0292266.
GeneID	8628625.
KEGG	ddi:DDB_G0292266.
Organism-specific databases
dictyBase	DDB_G0292266. amdA.
Phylogenomic databases
eggNOG	COG1816.
KO	K01490.
OMA	GFEHNVK.
Enzyme and pathway databases
UniPathway	UPA00591; UER00663.
Family and domain databases
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006329. AMP_deaminase. [Graphical view]
PANTHER	PTHR11359. PTHR11359. 1 hit.
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01429. AMP_deaminase. 1 hit.
PROSITE	PS00485. A_DEAMINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPD_DICDI

Accession

Primary (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:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)