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ADD_MYCA1
ID   ADD_MYCA1               Reviewed;         366 AA.
AC   A0QKJ4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_00540};
DE            EC=3.5.4.4 {ECO:0000255|HAMAP-Rule:MF_00540};
DE   AltName: Full=Adenosine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00540};
GN   Name=add {ECO:0000255|HAMAP-Rule:MF_00540}; OrderedLocusNames=MAV_4294;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC       deoxyadenosine. {ECO:0000255|HAMAP-Rule:MF_00540}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC         Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+);
CC         Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00540};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. Adenosine deaminase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00540}.
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DR   EMBL; CP000479; ABK68515.1; -; Genomic_DNA.
DR   RefSeq; WP_009978822.1; NC_008595.1.
DR   AlphaFoldDB; A0QKJ4; -.
DR   SMR; A0QKJ4; -.
DR   PRIDE; A0QKJ4; -.
DR   EnsemblBacteria; ABK68515; ABK68515; MAV_4294.
DR   GeneID; 66695488; -.
DR   KEGG; mav:MAV_4294; -.
DR   HOGENOM; CLU_039228_0_0_11; -.
DR   OMA; NHFTIHA; -.
DR   OrthoDB; 554648at2; -.
DR   Proteomes; UP000001574; Chromosome.
DR   GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:RHEA.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00540; A_deaminase; 1.
DR   InterPro; IPR028893; A_deaminase.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11409; PTHR11409; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01430; aden_deam; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nucleotide metabolism; Zinc.
FT   CHAIN           1..366
FT                   /note="Adenosine deaminase"
FT                   /id="PRO_1000017667"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   SITE            232
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
SQ   SEQUENCE   366 AA;  40534 MW;  80EC045E97F13E55 CRC64;
     MTAPLELEQI RKAPKALLHD HLDGGLRPST VLDIAGQTGY DGLPATDVEE LATWFRTRSH
     SGSLERYLEP FSHTVAVMQT PEALHRVAYE CVEDLAEDSV VYAEIRFAPE LHINRGMSFD
     EIVDAVLAGF ADGEKACAAA GRPIVVRLLV TAMRHAAVSR EIAELAIRWR DKGVVGFDIA
     GAEAGNPPTR HLEAFDYMRD HNARFTIHAG EAFGLPSIHE AIAFCGADRL GHGVRIVDDI
     DVLADGPDKG KVRLGRLANI LRDKRIPLEL CPSSNVQTGA VKSIADHPFD LLARTRFRVT
     VNTDNRLMSD TYMSREMHRL VQAFGYGWSD LERFTINAMK SAFIPFDERL AIIDEVIKPR
     YAVLIG
 
 
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