ID A0A369RTA2_9METZ Unreviewed; 757 AA.
AC A0A369RTA2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 13-SEP-2023, entry version 16.
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=TrispH2_011052 {ECO:0000313|EMBL:RDD37531.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD37531.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD37531.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD37531.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD37531.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDD37531.1}.
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DR EMBL; NOWV01000235; RDD37531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369RTA2; -.
DR STRING; 287889.A0A369RTA2; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000253843; Unassembled WGS sequence.
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 PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR Pfam; PF19326; AMP_deaminase; 2.
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:UP000253843}.
SQ SEQUENCE 757 AA; 87913 MW; F1DEC151FAF687F3 CRC64;
MTELNRELLF SDHSMYGQDR SSSTPDASLF EMPDDDIAQR QIHEDALQTT MLQAGIKELE
FKNAKDEDLA SRYRSQCNRE RFLDSTKFHR IHVDEDECSH SGILLGNLEE ASSFFVKALL
IRQKYMKISR QSFCRTTEKA LKTYVDKSLE CIDHEDVARS ICAGLPTESF EDVNPFDIEF
LPDNGNVCKI KNGIVMVYED KDALEREKPL DLKHPDVQEF VSDRNVLLAL CSHGPIKSFA
YRRMSFLESR FNLHVLLNET NEIAAQKRVS HRDFYNVRKV DTHVHAASCM NQKHLLRFIK
NKMKNCPNEE VLFRNGNVMT LEKVFRSLNL TSYDLSVDKL DVHADRNTFH RFDKFNLKYN
PIGELVTNVS LRLKSARLKM NNFATFTGES RLREIFLKTD NYVDGRYFGE LIKEVAYELE
DSKYQMAEPR LSIYGKSKIE WDKLARWAVN NSVYSDNVRW LIQIPRLYNI YKSNNLLNNF
QEMLDNIFTP LFEVTCNPSS HPELHRFLPQ LIGFDSVDDE SKAENHLFHE DSPLPNEWDL
PENPPYSYYC FYMFANITAL NNLRKQRGLN CFMFRPHCGE AGSVEHLMAA FILAQNISHG
LLLRKVPALQ YLYYLAQVGI AMSPLSNNSL FLNYHRNPLP SYHARGLIVS ISSDDPLQFH
FTKEPLMEEY SIAAQVWKLN PCDMCELARN SVWMSGFEHN LKKHWLGENY LKEGIESNSI
SCTNVPGIRV AYRHETLEEE LCTICDPQIK DHIPPHS
//