ID A0A3B4WMH1_SERLL Unreviewed; 830 AA.
AC A0A3B4WMH1;
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=AMPD2 {ECO:0000313|Ensembl:ENSSLDP00000002603.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000002603.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000002603.1}
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; A0A3B4WMH1; -.
DR STRING; 1841481.ENSSLDP00000002603; -.
DR Ensembl; ENSSLDT00000002712.1; ENSSLDP00000002603.1; ENSSLDG00000002040.1.
DR GeneTree; ENSGT00950000183011; -.
DR OrthoDB; 20951at2759; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000261360; Unplaced.
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}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 95953 MW; B683D2CB2A2AA7D2 CRC64;
MSSNLPPGTT AGAAGAKNKP LSPFRKRGSL QYTASTVDLR GARHLLTSQH SLPGIPVALK
QSIDLRTSMD GKYKEIAEEL FSRSLAESEM RSAPYEFPED SPIEQLEERR QRLERQISQD
VKFEPDILLR AKQEFMKTDS ATDLEYMKEQ SQAPDLQERE PVPEREYQRV TISGEEKCGV
PFTDLLDAAK CVVKALFIRQ KYMGLSLQSF CRTTSRYLQE LSERPLDLDL YEEEIPETTG
TADATVHPPV SQTHPYENQD PASMPPDMGY GCKMVDGVMH VYTTRSIMEK STELDLPYPD
LQEYIADMNV MMALIINGPV KSFCYRRLQY LSSKFQMHIL LNEMKELAAQ KKVPHRDFYN
IRKVDTHIHA SSCMNQKHLL RFIKRAMKKY PKEIVHVERG NGQTLMEVFE SMNLTAFDLS
VDTLDMHADR NTFHRFDKFN AKYNPIGESI LREIFIKTDN HIEGKYFGHI IKEVMADLEE
SKYQNVELRL SIYGRSRDEW DKLAKWAVKH QVYSTNVRWL VQVPRLFDVY HTKKQLCNFQ
EMLENVFMPL FEVTVNPGSH PELHLFLQHV VGFDSVDDES KPEQHIFNLD SPLPVNWTEE
DNPPYSYYLY YMYANMTVLN HLRRQRGFHT FVLRPHCGEA GPIHHLVSGF MLSENISHGL
LLRKAPVLQY LYYLAQIGIA MSPLSNNSLF LSYHRNPLPE YLSRGLMVSL STDDPLQFHF
TKEPLMEEYS IAAQVWKLSS CDMCELARNS VLMSGFSNKV KSYWLGPNYI KEGQESNDIR
RTNVPDIRVA YRYETMCEEL NLITQAIRTD ELETIEEEGS LCMAAVQAEK
//