ID   A0A401SUE0_CHIPU        Unreviewed;       928 AA.
AC   A0A401SUE0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, 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=chiPu_0012484 {ECO:0000313|EMBL:GCC34011.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC34011.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC34011.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(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:GCC34011.1}.
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DR   EMBL; BEZZ01000560; GCC34011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401SUE0; -.
DR   STRING; 137246.A0A401SUE0; -.
DR   OMA; FHRKFPY; -.
DR   UniPathway; UPA00591; UER00663.
DR   Proteomes; UP000287033; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001251};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001251};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT   REGION          77..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          202..263
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        77..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   928 AA;  106817 MW;  C5CCBB75C38BD5A0 CRC64;
     MSWLQRRVYA WAPLLGAASR RSCLQSLGLD RSVLPAVSPQ SRAPLSASGG NLRGSYFILG
     WSIDSRQRAA AAAVPTSYSS SSSSSPCCCR HFSSQSSRSS GRDKMSDPIP ITGKKLRPRL
     QGRSSLQNAE PPDVHNKTGT LKQIHCSQSL PGTPLSLKSF PIHLPTSMDG KYKEIAEELF
     TRSLTESDMR TAPYEFPEES PIEQLEERRQ RLERQISQDV RLEPEILLRA KQDFMKIDSA
     TDLQHYKDQI DATTEKYPEE KENEIEQEFQ RVRIFGEEKC GVPFTDLLDA AKCVVKSLFV
     REKYMALSLQ SFGKTTKRFL EQLGDRQCQA NMHDETLEAP ISPDTTIHSP FAEEHPYENC
     DPSIMPEDTG FGCKMIDGVT HVYSESNIMD KTTELNLPRP DLQEFTADMN VLMALIINGP
     VKSFCYRRLQ YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL
     LRFIKRSMKK NPDEIIHVEN GKGQTLKDVF ESMNLTAYDL SVDTLDMHAD RNTFHRFDKF
     NAKYNPIGES ILREIFIKTD NYIEGKYFGH IIKEVMEDLE ESKYQNAELR LSIYGRSRDE
     WDRLAKWAVK HKVYSNNVCW LVQVPRLFDV FRTKKQLNNF QDMLENIFIP VFEATINPRN
     HPELHLFLQH VVGFDSVDDE SKPEHHIFNA DSPLPVNWTE DDNPPYAYYL YYMYANMTVL
     NHLRKKRGFN TFVLRPHCGE AGPIHHLISG FMLSQNISHG LLLRKAPVLQ YLYYLDQIGI
     AMSPLSNNSL FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY SIAAQVWKLS
     SCDMCELARN SVLMSGFSYK VKGYWLGPHY QKESIEGNDI RRTNVPDIRV AYRHETLCEE
     LNLITQALIT AEQLENDSIN MTPVSESR
//