(data stored in ACNUC30567 zone)

HOGENOM: MOUSE3_PE1548

ID   MOUSE3_PE1548                        STANDARD;      PRT;   745 AA.
AC   MOUSE3_PE1548; Q3V1D3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=AMP deaminase 1; EC=3.5.4 6;AltName: Full=AMP deaminase
DE   isoform M;AltName: Full=Myoadenylate deaminase; (MOUSE3.PE1548).
GN   Name=Ampd1;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE3.PE1548.
CC       Mus musculus chromosome 3 NCBIM37  sequence 1..159599783 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:AMPD1_MOUSE
CC   -!- FUNCTION: AMP deaminase plays a critical role in energy
CC       metabolism.
CC   -!- CATALYTIC ACTIVITY: AMP + H(2)O = IMP + NH(3).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC       IMP from AMP: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the adenosine and AMP deaminases family.
CC   -!- GENE_FAMILY: HOG000092200 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000070385;ENSMUST00000090715;ENSMUSP00000088217.
DR   EMBL; AK132524; - ;
DR   UniProtKB/Swiss-Prot; Q3V1D3; -.
DR   EMBL; AK132524; BAE21218.1; -; mRNA.
DR   IPI; IPI00625079; -.
DR   UniGene; Mm.331272; -.
DR   ProteinModelPortal; Q3V1D3; -.
DR   SMR; Q3V1D3; 111-745.
DR   STRING; Q3V1D3; -.
DR   PRIDE; Q3V1D3; -.
DR   UCSC; uc008qso.1; mouse.
DR   MGI; MGI:88015; Ampd1.
DR   eggNOG; roNOG04969; -.
DR   GeneTree; ENSGT00390000008190; -.
DR   InParanoid; Q3V1D3; -.
DR   OrthoDB; EOG402WRH; -.
DR   PhylomeDB; Q3V1D3; -.
DR   ArrayExpress; Q3V1D3; -.
DR   Bgee; Q3V1D3; -.
DR   CleanEx; MM_AMPD1; -.
DR   Genevestigator; Q3V1D3; -.
DR   GO; GO:0003876; F:AMP deaminase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006144; P:purine base metabolic process; IEA:InterPro.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A/AMP_deaminase.
DR   InterPro; IPR006329; AMP_deaminase.
DR   InterPro; IPR016297; AMP_deaminase_met.
DR   Pfam; PF00962; A_deaminase; 1.
DR   PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR   TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
DR   HOGENOMDNA; MOUSE3.PE1548; -.
KW   ENSMUSG000000703855old_1320000031; ENSMUSP000000882171old_1320000031;
KW   AK132524;
KW   Complete proteome; Hydrolase; Metal-binding; Nucleotide metabolism;
KW   Reference proteome; Zinc.
SQ   SEQUENCE   745 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS LHEMQAHIFH
     MENLSMDGRR KRRFQGRKTV NLSIPQSETS STKLSHIEEF ISSSPTYESV PDFQRVQITG
     DYASGVTVED FEVVCKGLYR ALCIREKYMQ KSFQRFPKTP SKYLRNIDGE ALVGNESFYP
     VFTPPPKKGE DPFRTEDLPA NLGYHLKMKA GVIYIYPDEA AANRDEPKPY PYPNLDDFLD
     DMNFLLALIA QGPVKTYAHR RLKFLSSKFQ VHQMLNEMDE LKELKNNPHR DFYNCRKVDT
     HIHAAACMNQ KHLLRFIKKS YHIDADRVVY STKEKSLTLK ELFAKLNMHP YDLTVDSLDV
     HAGRQTFQRF DKFNDKYNPV GASELRDLYL KTDNYINGEY FATIIKEVGA DLVEAKYQHA
     EPRLSIYGRS PDEWNKLSSW FVCNRIYCPN MTWMIQVPRI YDVFRSKNFL PHFGKMLENI
     FLPVFEATIN PQAHPDLSVF LKHITGFDSV DDESKHSGHM FSSKSPKPEE WTMENNPSYT
     YYAYYMYANI TVLNSLRKER GMNTFLFRPH CGEAGALTHL MTAFMIADNI SHGLNLKKSP
     VLQYLFFLAQ IPIAMSPLSN NSLFLEYAKN PFLDFLQKGL MISLSTDDPM QFHFTKEPLM
     EEYAIAAQVF KLSTCDMCEV ARNSVLQCGI SHEEKAKFLG NNYLEEGPVG NDIRRTNVAQ
     IRMAYRYETW CYELNLIAEG LKATE
//

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