(data stored in ACNUC7421 zone)

SWISSPROT: Q4W9T7_ASPFU

ID   Q4W9T7_ASPFU            Unreviewed;       543 AA.
AC   Q4W9T7;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 78.
DE   RecName: Full=Guanine deaminase {ECO:0000256|RuleBase:RU366009};
DE            Short=Guanase {ECO:0000256|RuleBase:RU366009};
DE            EC=3.5.4.3 {ECO:0000256|RuleBase:RU366009};
DE   AltName: Full=Guanine aminohydrolase {ECO:0000256|RuleBase:RU366009};
GN   ORFNames=AFUA_4G03770 {ECO:0000313|EMBL:EAL84526.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL84526.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84526.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC       xanthine and ammonia. {ECO:0000256|RuleBase:RU366009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanine + H(+) + H2O = NH4(+) + xanthine;
CC         Xref=Rhea:RHEA:14665, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16235, ChEBI:CHEBI:17712, ChEBI:CHEBI:28938; EC=3.5.4.3;
CC         Evidence={ECO:0000256|RuleBase:RU366009};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU366009};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU366009};
CC   -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC       step 1/1. {ECO:0000256|RuleBase:RU366009}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ATZ/TRZ family. {ECO:0000256|RuleBase:RU366009}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL84526.1}.
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DR   EMBL; AAHF01000016; EAL84526.1; -; Genomic_DNA.
DR   RefSeq; XP_746564.1; XM_741471.1.
DR   STRING; 746128.CADAFUBP00009645; -.
DR   MEROPS; M38.981; -.
DR   EnsemblFungi; EAL84526; EAL84526; AFUA_4G03770.
DR   GeneID; 3503938; -.
DR   KEGG; afm:AFUA_4G03770; -.
DR   EuPathDB; FungiDB:Afu4g03770; -.
DR   HOGENOM; HOG000257692; -.
DR   InParanoid; Q4W9T7; -.
DR   KO; K01487; -.
DR   OMA; ASYFATN; -.
DR   OrthoDB; 612054at2759; -.
DR   UniPathway; UPA00603; UER00660.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0008892; F:guanine deaminase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046098; P:guanine metabolic process; IBA:GO_Central.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR014311; Guanine_deaminase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02967; guan_deamin; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4W9T7.
DR   SWISS-2DPAGE; Q4W9T7.
KW   Hydrolase {ECO:0000256|RuleBase:RU366009, ECO:0000313|EMBL:EAL84526.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU366009};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Zinc {ECO:0000256|RuleBase:RU366009}.
FT   DOMAIN          93..489
FT                   /note="Amidohydro-rel"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   543 AA;  58819 MW;  114445B2E114034B CRC64;
     MATATAPTYT LFLGTFIHLP RKPTGADPGA KWRPALEINH GALWVSNSDG KIAGFDWSFS
     PADGDVNSLT EKLGLSGKVT EVVRAREERN EFFFPGFIAD RQDTHIHAPQ YPNSGIFGSS
     TLLDWLETYT FPLESSFGDA SKARAVYSRV IARTLANGTT CASYFATIHV PATNLLASLC
     HSRGQRALIG RVCMDNPSFC PDYYLDSSPE SSVSKSKETI AHIHSIDPAG TLIHPILTPR
     FAPTCSPPAL HGLAQLAQSY NPPLHIQTHL SENTGEISLV RELFPQSKDY TSVYDDFGLL
     TPRTILAHAV HLSPSERELI AARGAKVSHC PASNSALGSG LCAVRKLLEA GVEVGLGTDV
     SGGYNCSVLE AVRQGCLVSR LLRHSGTDDP GDGDDGEEVL SVEEGLYLAT RGGAAVVDLA
     GEIGGFEVGM SFDAQMVRLG HSHTSSSPTA EHGVVDVFGW ESWTEKVHKW VWTGDDRNVK
     AVWVRGRLVH SLDEGQSQSD VSIPEKGKPT WIWAGTGAAW ESKWWLCGLG FVSAWFIFDR
     VMR
//

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