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ADEC_ARCFU
ID   ADEC_ARCFU              Reviewed;         556 AA.
AC   O29999;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=AF_0240;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+);
CC         Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR   EMBL; AE000782; AAB90993.1; -; Genomic_DNA.
DR   PIR; H69279; H69279.
DR   RefSeq; WP_010877751.1; NC_000917.1.
DR   AlphaFoldDB; O29999; -.
DR   SMR; O29999; -.
DR   STRING; 224325.AF_0240; -.
DR   PRIDE; O29999; -.
DR   DNASU; 1483451; -.
DR   EnsemblBacteria; AAB90993; AAB90993; AF_0240.
DR   GeneID; 1483451; -.
DR   KEGG; afu:AF_0240; -.
DR   eggNOG; arCOG00693; Archaea.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 12286at2157; -.
DR   PhylomeDB; O29999; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR   CDD; cd01295; AdeC; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01518; Adenine_deamin; 1.
DR   InterPro; IPR006679; Adenine_deam.
DR   InterPro; IPR026912; Adenine_deam_C.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11113:SF2; PTHR11113:SF2; 1.
DR   Pfam; PF13382; Adenine_deam_C; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..556
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142438"
SQ   SEQUENCE   556 AA;  60764 MW;  B3E3440A09F86A79 CRC64;
     MSSPTADVEK LRRIIEVARG DRRADFVVKN AQIVDLVNEE IFEGDIAVAE GFIAGIGSYS
     GVEECEASNL VAVPGLIDAH THIEMSMLTV SEFARLVVPR GTTGVVADPH EIANVLGKDG
     VMLMLEEARS TPLRFYCMVP SCVPSSPLET SGARIGVEEI RELLEEEEVL GLAEMMNFPG
     VVSADREVLE KIVLAGIVDG HAPGLRGKKL NAYIAAGASS DHETTSFEEG KEKLRLGMWV
     MIREGSAARN LVALKGLTGN RHTMLVTDGD RSVKDIIEEG YLDHVFRRAI EEGIDEIKAL
     QMLTLNPAEY FGINAGLIAP SRLADIVLLK NLRKFEVRDV FVGGRRPEFK RFNHPEWAKK
     TVKARKITPE SIQLKTGRVR VIEVYDGEIV TGEAIEEVQG VDVERDILKA VVVERHIRSG
     RVGKAYVRGF GLKRGAIAQS IAHDAHNIVC VGVDDGSICA AVNRVIELQG GIVVADAEVR
     AELPLPIAGI MSDERAERVL ERLSEIEEEV RKLGCRLKSP VITLSFIALP VIPKLKLTDL
     GLVDVEAFRV VDLQAD
 
 
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