ID   A0A3B4T8B0_SERDU        Unreviewed;       765 AA.
AC   A0A3B4T8B0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   Name=AMPD3 {ECO:0000313|Ensembl:ENSSDUP00000002334.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000002334.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000002334.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   AlphaFoldDB; A0A3B4T8B0; -.
DR   Ensembl; ENSSDUT00000002399.1; ENSSDUP00000002334.1; ENSSDUG00000001715.1.
DR   GeneTree; ENSGT00950000183011; -.
DR   UniPathway; UPA00591; UER00663.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; IPR001079; Galectin_CRD.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01429; AMP_deaminase; 1.
DR   PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR   PANTHER; PTHR11359:SF2; AMP DEAMINASE 3; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   PIRSF; PIRSF001251; AMP_deaminase_met; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
DR   PROSITE; PS51304; GALECTIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001251};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001251}.
FT   DOMAIN          110..269
FT                   /note="Galectin"
FT                   /evidence="ECO:0000259|PROSITE:PS51304"
SQ   SEQUENCE   765 AA;  88435 MW;  EE470D6EA5DF1344 CRC64;
     MPRLFPRISM SEVDERVRLI AEKVYASALK EEDTKDAMAL FSVPEDCPIG LHEDRERALQ
     KELAEQQSQE SAKKKKSFML KRSQSVSLQI PVSGDWALSV VSPMLSPTTP EPHLPESFPD
     FQRVTISGDY CAGITVEDYE QAAKSLLTAL LIREKYSRLA YHRFPRTTAQ FLRNAENEKW
     REEDEILPDI WPFPHEGEDP YSMEGIPENL NYELQMKDGI VHVYNNEEAL KHEQPHSLPY
     PDLETFAIDL SHVLAMIADD CLVSRVVLKG SSVVRLNFLA SKFYLHEMLN EMAELKELKC
     VPHRDFYNVR KVDTHIHAAA CMNQKHLLKF IKTTYQTEAD RVVLERGCQK ITLKEVFNNL
     HMDPYDLTVD SLDVHAGRQT FHRFDKFNSK YNPVGASELR EIYLKSDNYI EGEYFARLIK
     EVAKELEDSK YQHAEPRLSI YGRSPSEWES LATWFIQHKV HSPNMRWMIQ VPRIYDIFRS
     KKLVPHFAKM LENIFLPLFE ATVNPQKHKA VHVFLKYVTG FDSVDDESKH SDHMFSYKSP
     KPEAWITDDN PPYTYYLFYM YANIMVLNNL RKERGLNTFQ FRPHCGEAGS ITHLVSAFLT
     ADNISHGLNL KKSPVLQYLY YLAQVPIAMS PLSNNSLFLQ YSKNPLREFL QKGLCVSLST
     DDPMQFHYTK EALMEEYAIA GQLWKLSTCD LCEIARNSVL QSGLSHQEKK HFIGSNYLQD
     GPDGNDIRRT NVAQIRMAYR HETLCNELSF LVDAVRTEVG TSPPE
//