ID   AMPD_ORYSJ              Reviewed;         815 AA.
AC   Q84NP7; Q0D3C9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Probable AMP deaminase;
DE            EC=3.5.4.6;
GN   Name=AMPD; OrderedLocusNames=Os07g0693500, LOC_Os07g49270;
GN   ORFNames=OsJ_25692 {ECO:0000312|EMBL:EAZ41190.1}, P0034A04.129;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism.
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from AMP: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC       Note=Might be associated with the inner mitochondrial membrane.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP004333; BAC75568.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF22644.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT03357.1; -; Genomic_DNA.
DR   EMBL; CM000144; EAZ41190.1; -; Genomic_DNA.
DR   EMBL; AK064333; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK102007; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015646516.1; XM_015791030.1.
DR   AlphaFoldDB; Q84NP7; -.
DR   SMR; Q84NP7; -.
DR   STRING; 39947.Q84NP7; -.
DR   PaxDb; 39947-Q84NP7; -.
DR   EnsemblPlants; Os07t0693500-01; Os07t0693500-01; Os07g0693500.
DR   GeneID; 4344386; -.
DR   Gramene; Os07t0693500-01; Os07t0693500-01; Os07g0693500.
DR   KEGG; osa:4344386; -.
DR   eggNOG; KOG1096; Eukaryota.
DR   HOGENOM; CLU_003782_3_0_1; -.
DR   InParanoid; Q84NP7; -.
DR   OMA; MICECLD; -.
DR   OrthoDB; 20951at2759; -.
DR   UniPathway; UPA00591; UER00663.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000007752; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   ExpressionAtlas; Q84NP7; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003876; F:AMP deaminase activity; IBA:GO_Central.
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:0006188; P:IMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
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:SF10; AMP DEAMINASE-RELATED; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
DR   Genevisible; Q84NP7; OS.
PE   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Metal-binding; Nucleotide metabolism;
KW   Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..815
FT                   /note="Probable AMP deaminase"
FT                   /id="PRO_0000238456"
FT   TRANSMEM        5..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          53..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        657
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT   BINDING         367
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         438..443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         635
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         638
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         712
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         713..716
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   815 AA;  93854 MW;  E9C9C55382961A7F CRC64;
     MDSTYALHLA VATLLGASFA AASAYYMHRK TLDQLLRFAR SLDRDHRRRN RHLLDADDDD
     DDDPPRDHDR RTTLPIPPGL PPLHTGREGK PIISPASTKR VGPLVRPTTP RSPVPTVSAF
     ETIEDSDDDD ENIAPDAKNN AVSLLTNGTI GSDPLPGKAS QNGDTKPVPS TNMIRSQSAT
     GSLHGAQHNP VAADILRKEP EHETFSRINI TAVETPSPDE IEAYKVLQKC LELREKYMFR
     EEVAPWEKEI ITDPSTPKPN PNPFYYEQQT KTEHHFEMVD GVIHVYPNKD AKERIYPVAD
     ATTFFTDMHY ILRVLAAGDI RTVCYKRLNL LEQKFNLHLM VNADRELLAQ KAAPHRDFYN
     VRKVDTHVHH SACMNQKHLL RFIKSKLRKE PDEVVIFRDG TYLTLKEVFE SLDLTGYDLN
     VDLLDVHADK STFHRFDKFN LKYNPCGQSR LREIFLKQDN LIQGRFLAEL TKEVFSDLEA
     SKYQMAEYRI SIYGRKKSEW DQMASWIVNN ELYSENVVWL IQIPRIYNVY REMGTINSFQ
     NLLDNIFLPL FEVTVDPASH PQLHVFLQQV VGLDLVDDES KPERRPTKHM PTPEQWTNVF
     NPAYAYYVYY CYANLYTLNK LRESKGMTTI KLRPHCGEAG DIDHLAAAFL TSHNIAHGVN
     LKKSPVLQYL YYLAQIGLAM SPLSNNSLFI DYHRNPFPTF FLRGLNVSLS TDDPLQIHLT
     KEPLVEEYSI AASLWKLSSC DLCEIARNSV YQSGFSHRLK SHWIGRNYYK RGHDGNDIHQ
     TNVPHIRIEF RHTIWKEEME LIHLRNVDIP EEIDR
//