AMPD_DICDI
ID AMPD_DICDI Reviewed; 790 AA.
AC Q54DD0; Q9NGX0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=AMP deaminase {ECO:0000303|PubMed:1916064};
DE Short=AMPD1 {ECO:0000303|PubMed:11784104};
DE EC=3.5.4.6 {ECO:0000269|PubMed:11784104, ECO:0000269|PubMed:1916064};
GN Name=amdA; ORFNames=DDB_G0292266;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-790, DISRUPTION PHENOTYPE,
RP DEVELOPMENTAL STAGE, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=AX4;
RX PubMed=11784104; DOI=10.1006/dbio.2001.0491;
RA Chae S.-C., Fuller D., Loomis W.F.;
RT "Altered cell-type proportioning in Dictyostelium lacking adenosine
RT monophosphate deaminase.";
RL Dev. Biol. 241:183-194(2002).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=AX3;
RX PubMed=1916064; DOI=10.1111/j.1432-0436.1991.tb00876.x;
RA Malliaros D.P., Kozwich D.L., Jahngen E.G.E.;
RT "Purification and characterization of developmentally regulated AMP
RT deaminase from Dictyostelium discoideum.";
RL Differentiation 46:153-160(1991).
RN [4]
RP FUNCTION.
RC STRAIN=AX2;
RX PubMed=17259634; DOI=10.1099/mic.0.2006/000562-0;
RA Serafimidis I., Bloomfield G., Skelton J., Ivens A., Kay R.R.;
RT "A new environmentally resistant cell type from Dictyostelium.";
RL Microbiology 153:619-630(2007).
CC -!- FUNCTION: Catalyzes the conversion of adenosine monophosphate (AMP) to
CC inosine monophosphate (IMP) and ammonia (NH4(+)) (PubMed:11784104,
CC PubMed:1916064). Participates in the regulation of the adenylated
CC nucleotide pool and the interconversion to guanylated nucleotides
CC during early morphodifferentiation (PubMed:1916064, PubMed:17259634).
CC {ECO:0000269|PubMed:11784104, ECO:0000269|PubMed:1916064,
CC ECO:0000303|PubMed:17259634, ECO:0000303|PubMed:1916064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6;
CC Evidence={ECO:0000269|PubMed:11784104, ECO:0000269|PubMed:1916064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778;
CC Evidence={ECO:0000269|PubMed:11784104, ECO:0000269|PubMed:1916064};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by ATP, inhibited by GTP, EDTA and
CC inorganic phosphate. {ECO:0000269|PubMed:1916064}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for AMP {ECO:0000269|PubMed:1916064};
CC Vmax=1.0 umol/min/mg enzyme {ECO:0000269|PubMed:1916064};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from AMP: step 1/1. {ECO:0000305|PubMed:11784104,
CC ECO:0000305|PubMed:1916064}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1916064}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1916064}.
CC -!- DEVELOPMENTAL STAGE: Expressed during normal growth and slightly more
CC for the first 4 hours of development. Enzymatic activity increases for
CC the first 5 hours of development and then tapers off.
CC {ECO:0000269|PubMed:11784104, ECO:0000269|PubMed:1916064}.
CC -!- DISRUPTION PHENOTYPE: Cells grow normally until development occurs.
CC Then they make a significantly increased proportion of prestalk cells,
CC and develop fruiting bodies with short thick stalks and glassy sori
CC with less than 5% normal spores. They have an increased content of
CC pstA-type prestalk cells. Intracellular levels of inosine increase
CC dramatically during development. This is cell autonomous, as the
CC presence of equal numbers of wild-type cells does not alter the cell
CC type proportion nor improve sporulation. Overexpression of the gene has
CC no apparent effect on development (PubMed:11784104). Mutants lacking
CC amdA form aspidocytes (a cell type able to resist detergent lysis and
CC which are also resistant to some antibiotics) more readily than wild-
CC type cells; their induction may involve AMP or other purine metabolites
CC (PubMed:17259634). {ECO:0000269|PubMed:11784104,
CC ECO:0000269|PubMed:17259634}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
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DR EMBL; AAFI02000189; EAL61257.1; -; Genomic_DNA.
DR EMBL; AF238311; AAF65407.1; -; Genomic_DNA.
DR RefSeq; XP_629711.1; XM_629709.1.
DR AlphaFoldDB; Q54DD0; -.
DR SMR; Q54DD0; -.
DR STRING; 44689.DDB0191089; -.
DR PaxDb; Q54DD0; -.
DR PRIDE; Q54DD0; -.
DR EnsemblProtists; EAL61257; EAL61257; DDB_G0292266.
DR GeneID; 8628625; -.
DR KEGG; ddi:DDB_G0292266; -.
DR dictyBase; DDB_G0292266; amdA.
DR eggNOG; KOG1096; Eukaryota.
DR HOGENOM; CLU_003782_4_2_1; -.
DR InParanoid; Q54DD0; -.
DR OMA; RKERGMC; -.
DR PhylomeDB; Q54DD0; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-74217; Purine salvage.
DR SABIO-RK; Q54DD0; -.
DR UniPathway; UPA00591; UER00663.
DR PRO; PR:Q54DD0; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IC:dictyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003876; F:AMP deaminase activity; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IMP:dictyBase.
DR GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0032264; P:IMP salvage; IDA:dictyBase.
DR GO; GO:0009167; P:purine ribonucleoside monophosphate metabolic process; IDA:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR CDD; cd01319; AMPD; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Hydrolase;
KW Metal-binding; Nucleotide metabolism; Reference proteome; Sporulation;
KW Zinc.
FT CHAIN 1..790
FT /note="AMP deaminase"
FT /id="PRO_0000327654"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 510
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 292..297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 566..569
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 790 AA; 90954 MW; 51ECE82FAA5C6C18 CRC64;
MSTPLRGSSP QVSFYESELD QEGGSDASHF TYRNYMEDDK INSFTFNMAR KDQTQLFQRI
ILTNESESEI EEYAEVAEQL LDAINLREKY VFHPKIWKAD APVGEKPPYS PFESDESTNC
ATEHMFKEVN GVYFVYSNET DMKSNKALFS VPHTLASYYK DINNLMMLSS YGPAKTFTFK
RLQLLESKFN MHTLLNDSLE LFQQKTAPHR DFYNVRKVDT HVHHSSSMNQ KHLLKFIKRK
LKENPNEIVI FRDDKYLTLA EVFKSLNLDV DELSVDTLDV HADNNTFHRF DKFNLKYNPC
GQSRLREIFL KTDNLIKGKY LAEISKEVFT DLESSKYQCA EYRLSIYGRK MSEWDTLASW
IVDNDLFSTK VRWLIQVPRL YDVYRETSTT TFQDFLNNVF HPLFEVTKDP SSHPKLHLFL
QQVVGIDCVD DESKFEKKFT EKFPVPGEWS SEHNPPYTYY LYYLYANLYT LNQFREEKGL
NILTLRPHSG EAGEVDHMGA AFYLAHGINH GINLRKTPVL QYLYYLTQIG IAMSPLSNNS
LFLTYNRNPF PAFFARGLNV SISTDDPLQF HYTKEPLMEE YSIATQVWRL SVCDICEIAR
NSVLQSGFEH NVKSHWLGPD YANSGGNDIK KTNISDIRVC FRNETLIEEL HLILKSLQTL
PNFKNLNINF LLDKLPSEIT TGNDYKLKKA QLKLNGANKL RNSSVGSTPN NGTPSSSGTP
SLSSPGAIVH LMKTKPYIPP PLSLNIKQEN NNNNNNNNNN NNNNNNNNTN TNTNSNSTTT
NQDDNSKSDK
