ID V4ZET5_TOXGV Unreviewed; 1159 AA.
AC V4ZET5; A0A0F7V2T8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN ORFNames=BN1205_062920 {ECO:0000313|EMBL:CEL76800.1}, TGVEG_234280
GN {ECO:0000313|EMBL:ESS30887.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS30887.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|EMBL:ESS30887.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS30887.1};
RA Paulsen I.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ESS30887.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS30887.1};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CEL76800.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:CEL76800.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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DR EMBL; LN714500; CEL76800.1; -; Genomic_DNA.
DR EMBL; AAYL02000220; ESS30887.1; -; Genomic_DNA.
DR AlphaFoldDB; V4ZET5; -.
DR STRING; 432359.V4ZET5; -.
DR PaxDb; 5811-TGME49_034280; -.
DR EnsemblProtists; ESS30887; ESS30887; TGVEG_234280.
DR VEuPathDB; ToxoDB:TGVEG_234280; -.
DR eggNOG; KOG1096; Eukaryota.
DR OMA; VFWDPAN; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000002226; Partially assembled WGS sequence.
DR GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ESS30887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226}.
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 129107 MW; 796ADFF439DD2AEE CRC64;
MPLHRVEDRG DSCACSSLGG SSLPSRGTRK EAGEGSLSSS VETSVASLSR PSSAALHVHE
RAEEAESLFS PAFSAAGSTL SVGEEERRTA RFVAQNETVL NGEQQSDIPP PVPDEDDEEQ
VGWSYMFKQL LSLNHKDAGT VTYMEKLPSV PAKAGSAAAA APARLASPSL SAPSPFSPAA
AAVGYVRMVP SKDLAVASSV CDESVEAVRF LAHLLQLRQF WARAYEEPPS PGVRPLSEEE
KNKFRTKEPM YDPFNIPLKP PCNAVYKMHH GVYQVFWDPA NDVATKDAPL LWKANPLPDV
HQFLRGLKDV MTAVQNPACK SFCYKRLKYL EEKFNLHLMF NSPAEVTETK CNFHRDFYNV
RKVDTHIHHS ACMQQKHLLR FIRKKYRTEP ETVVAKTRDG NEQTLMELFH TEVGIGAHDA
SIDHLNVHAL GSCFQRFDLF NQKYNPFGQK TLRDVFLKTD NYIEGRFLAE ITREVISDLE
ERKYQHVEWR LSIYGRSRDE WTKLAKWVVK NKLSSKRVRW MVQVPRLYHV YRRLGMIRSF
GELLENIFEP LYDAVRNPEE HPEVFTFLHM LVGWDSVDDE SYASKYTMEG GELPKPAEWT
GENNPPYSYW GYYMYANIRA LNEFMVARGL RALAFRPHCG EAGSVSHLAT MFLLADAINH
GIMLKKCPVL QYLFYLAQIG LAVSPLSNNA LFMDIAKNPL CSFFKIGLNV SISTDDPLMF
HFTDEPLLEE YSVAAHTWKL SPVDLCELAR NSVLQSGFEA EFKRHWLGPK YKLGGRRGNC
MRQTNVSNIR LQYREDALRE ELSYMHDVLA LRIALSRPFS PAVHPAICPP SVSPRSALLP
EKSEPTFAAF EDAFEPGNEA DEPAQVLRVA APENFRAAER ETKGETKGGK PTAKDGRHER
EASTGRCGET GAGGGDNGAT EKTTRASLVF DREQEELHAS HSITVSPPDS AEGTEKDGEK
KARLGLRSPK TGSDSESPGT QTSPRMRPLL LRDAAMKKLL EVAEESAVMD LGEIPGGVSS
PMPRSESFEV LDGPSREALQ TLDAYTHLEA REENVDMGVL KVALTSQRSP ALLSGSGTGR
TLRRASMDES DGRRRSGAGL LQLLTSPLLQ QQLSHASSVI VGEYANSTAE GDEERRGDSE
GDPDDAKRSE NEKETEEAK
//
