ID A0A3Q3BQH6_KRYMA Unreviewed; 986 AA.
AC A0A3Q3BQH6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN Name=AMPD2 {ECO:0000313|Ensembl:ENSKMAP00000028669.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000028669.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000028669.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q3BQH6; -.
DR STRING; 37003.ENSKMAP00000028669; -.
DR Ensembl; ENSKMAT00000029029.1; ENSKMAP00000028669.1; ENSKMAG00000021250.1.
DR GeneTree; ENSGT00950000183011; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
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 SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 112674 MW; C0FB0348E2A29EE4 CRC64;
MPSPAAVFCH AGYRKLVPWL LGQPGRLAPC RSRGGPGQHS GTSPVDPLWR AGRRRRRSRL
CRGALSSPVW VLLLHCPTAM RQSSNIRAGA PPSLCWSLRR SDSLCYCSNK NIKMSSSSST
SNSDRQRNVK LKSQFQKRGS LQSTPSPAGE GASAVPGLVS CPSIPQELKP GHGDRSGDCV
CRTRQADRDA GGGSGPKTLK AQRSLPGAPV SLSHYLVDLR TSMEEKYKEI AEELFTRSMA
ESEMRSAPYE FPEDSPIEQL EERRHRLERQ ISQDIKLEPE ILLRAKQDFM KIDSAADLEL
MKDRSVDVVD VGFKERAMPM EREYQRVSIS GEEKCGVPFT DLVDAAKCVV KALLIREKYI
NRSMQSFCKT TAHALQDLRT KPLDLEIYDD VPETPVDADA PVHPPVSETH PYDNQDPDNM
PADTGYGCKM VGGVVHVYTK KTNMDKSMEL DLPYPDLKEY IADMNVMMSL IINGPVKSFC
YRRLQYLSSK FQMHILLNEM KELAAQKKVP HRDFYNIRKV DTHIHASSCM NQKHLLRFIK
RAMKKYPGEI VHVERGRGQT LKDVFESMNL TAYDLSVDTL DMHADRNTFH RFDKFNSKYN
PIGESILREI FIKTDNHVEG KYFAHIVKEV MSDLEESKYQ NSELRLSIYG RSRDEWDKLA
QWAVQHRVYS DNVRWLIQVP RLFDVYHTKK QLANFQEMLE NIFMPLFEAT INPRSHPDLH
LLLEHVVGFD SVDDESKPEH HIFNLDSPLP PDWTEVDNPP YSYYLYYTYA NMTVLNHLRR
RRGFHTFVLR PHCGEAGPIH HLVSGFMLSE NISHGLLLRK APVLQYLYYL AQVGIAMSPL
SNNSLFLSYH RNPLPEYLSR GLMISLSTDD PLQFHFTKEP LMEEYSIAAQ VWKLSSCDMC
ELARNSVLMS GFSHKVKSYW LGPSYYLEGP ESNDIRRTNV PDIRVAYRFE TLTEELHLIT
HAVRTDEMDA IDEEDSLTMG PLPGQC
//