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   24-JAN-2024, entry version 108.
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 (Social amoeba).
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 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.Q54DD0; -.
DR   PaxDb; 44689-DDB0191089; -.
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   Gene3D; 4.10.800.20; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR006329; AMPD.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01429; AMP_deaminase; 1.
DR   PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR   PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 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
//