ID   J4D910_THEOR            Unreviewed;       778 AA.
AC   J4D910;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775, ECO:0000256|PIRNR:PIRNR001251};
DE            EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775, ECO:0000256|PIRNR:PIRNR001251};
GN   ORFNames=TOT_030000388 {ECO:0000313|EMBL:BAM41125.1};
OS   Theileria orientalis strain Shintoku.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41125.1, ECO:0000313|Proteomes:UP000003786};
RN   [1] {ECO:0000313|EMBL:BAM41125.1, ECO:0000313|Proteomes:UP000003786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shintoku {ECO:0000313|EMBL:BAM41125.1,
RC   ECO:0000313|Proteomes:UP000003786};
RX   PubMed=22951932;
RA   Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA   Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA   Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA   Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA   Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT   "Comparative genome analysis of three eukaryotic parasites with differing
RT   abilities to transform leukocytes reveals key mediators of Theileria-
RT   induced leukocyte transformation.";
RL   MBio 3:e00204-e00212(2012).
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:0000256|PIRNR:PIRNR001251};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|PIRNR:PIRNR001251};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004955}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676,
CC       ECO:0000256|PIRNR:PIRNR001251}.
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DR   EMBL; AP011948; BAM41125.1; -; Genomic_DNA.
DR   RefSeq; XP_009691426.1; XM_009693131.1.
DR   AlphaFoldDB; J4D910; -.
DR   STRING; 869250.J4D910; -.
DR   EnsemblProtists; BAM41125; BAM41125; TOT_030000388.
DR   GeneID; 20715568; -.
DR   KEGG; tot:TOT_030000388; -.
DR   VEuPathDB; PiroplasmaDB:TOT_030000388; -.
DR   eggNOG; KOG1096; Eukaryota.
DR   OrthoDB; 20951at2759; -.
DR   UniPathway; UPA00591; UER00663.
DR   Proteomes; UP000003786; Chromosome 3.
DR   GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF3; AMP DEAMINASE 2; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001251};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001251};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003786}.
SQ   SEQUENCE   778 AA;  90430 MW;  CEC7B6CA2B3703BF CRC64;
     MNNYIPITDN PHSVERMPLD PRINDSHLDI IIPMDGNSKT ILGEQANYTV PENDLRSPSY
     QFPHESPIEQ LEERQKRLER QISQDVKHEP EIPPWTSQDF KSESDIDFQM YKERREGRGG
     FGTWDLDSSL EREFQRVTIS GDEKCGVPFT DLLDAAKYVV RALFIREKYI SMSLQTFCPT
     TLRYIQQLTD RPLELHTHDF DNLTPVAADA PVHPPLMEQH PYETCDPSTM PGDMGLGIRM
     IHGVVHLYSS REPGENCTEI DLPCPSLEEF VVDHNSLMPL IINGPMKSFC YRRLQYLSSK
     FQMHVLLNEM KELAAQKRAP HRDFYNIRKV DTHIHAASCM NQKHLLRFIK CAMKKHPDEI
     VHVEQGREQT LREVFESMNL TAYDLSVDTL DMHADRNTFH RFDKFNSKYN PIGESALREI
     FIKTDNRVSG KYFAHIIKEV MSDLEDSKYS NAELRLSIYG RSRDEWDKLA RWAIVNRVHS
     PSVLWLVQVP RLFDVYRTKR QLANFNEMLE NIFLPLFEVT INPQSHPELH LFLEHVHGFD
     SVDDESKPEN YLFNMETPLP DVWVMDDNPP YAYYLYYMFA NMTILNHLRK QRGFNTFVLR
     PHSGEAGPIH HMVTAFMISQ NISHGLLLRK SPVLQYLYYL AQVGIAMSPL SNNSLFLSYH
     RSPLPEFLSR GLMVSLSTDD PLHFHFTKEP LMEEYSIAAQ VWKLSSCDMC ELARNSVLMS
     GFSPKVKSHW LGPNYMKEGP EGNDIHRSNV PDIRISYRYE TLCQELALIT QAMPMYAP
//