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Database: UniProt
Entry: UREA_ASPFU
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ID   UREA_ASPFU              Reviewed;         838 AA.
AC   Q6A3P9; Q4WJW6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   16-OCT-2019, entry version 103.
DE   RecName: Full=Urease;
DE            EC=3.5.1.5;
DE   AltName: Full=Urea amidohydrolase;
GN   Name=ure1; ORFNames=AFUA_1G04560;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D141;
RA   Eglins M., Reichard U.;
RT   "Molecular cloning and sequencing of urease from Aspergillus
RT   fumigatus.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5;
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000250};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the metallo-
CC       dependent hydrolases superfamily. Urease alpha subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL88166.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AJ578495; CAE17672.1; -; mRNA.
DR   EMBL; AAHF01000007; EAL88166.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_750204.1; XM_745111.1.
DR   SMR; Q6A3P9; -.
DR   STRING; 746128.CADAFUBP00000484; -.
DR   MEROPS; M38.982; -.
DR   PRIDE; Q6A3P9; -.
DR   GeneID; 3507289; -.
DR   KEGG; afm:AFUA_1G04560; -.
DR   EuPathDB; FungiDB:Afu1g04560; -.
DR   HOGENOM; HOG000075064; -.
DR   InParanoid; Q6A3P9; -.
DR   KO; K01427; -.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002530; Chromosome 1.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00375; Urease_alpha; 1.
DR   CDD; cd00407; Urease_beta; 1.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   Gene3D; 3.30.280.10; -; 1.
DR   HAMAP; MF_01953; Urease_alpha; 1.
DR   HAMAP; MF_01954; Urease_beta; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008221; Urease.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   InterPro; IPR017950; Urease_AS.
DR   InterPro; IPR005848; Urease_asu.
DR   InterPro; IPR017951; Urease_asu_c.
DR   InterPro; IPR002019; Urease_beta.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR   InterPro; IPR036463; Urease_gamma_sf.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   Pfam; PF00699; Urease_beta; 1.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   PIRSF; PIRSF001222; Urease; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF54111; SSF54111; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 1.
DR   TIGRFAMs; TIGR00193; urease_gam; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Hydrolase; Metal-binding; Nickel;
KW   Reference proteome.
FT   CHAIN         1    838       Urease.
FT                                /FTId=PRO_0000067526.
FT   DOMAIN      402    838       Urease.
FT   ACT_SITE    593    593       Proton donor. {ECO:0000250}.
FT   METAL       407    407       Nickel 1; via tele nitrogen.
FT                                {ECO:0000250}.
FT   METAL       409    409       Nickel 1; via tele nitrogen.
FT                                {ECO:0000250}.
FT   METAL       490    490       Nickel 1; via carbamate group.
FT                                {ECO:0000250}.
FT   METAL       490    490       Nickel 2; via carbamate group.
FT                                {ECO:0000250}.
FT   METAL       519    519       Nickel 2; via pros nitrogen.
FT                                {ECO:0000250}.
FT   METAL       545    545       Nickel 2; via tele nitrogen.
FT                                {ECO:0000250}.
FT   METAL       633    633       Nickel 1. {ECO:0000250}.
FT   BINDING     492    492       Substrate. {ECO:0000250}.
FT   MOD_RES     490    490       N6-carboxylysine. {ECO:0000250}.
FT   CONFLICT    159    159       R -> P (in Ref. 1; CAE17672).
FT                                {ECO:0000305}.
SQ   SEQUENCE   838 AA;  90912 MW;  63EBF567ACB73B9E CRC64;
     MHLIPKELDK LVISQLGFLA QRRLARGVRL NHAEAAALIS SNLQELIRDG HYSVADLMSI
     GKTMLGRRHV LPSVVHTLVE LQVEGTFPTG TYLVTVHHPI SSDDGDLEKA LYGSFLPIPP
     ADTFPDPNPD DYLPEKMPGA VLPVKNERIT LNDGRKRIRL KVMSKGDRPI QVGSHYHFIE
     TNPQLHFDRL RAYGYRLDIP AGTSVRFEPG DTKTVTLVEI AGNRIIKGGN SIASGKVDIS
     RAEEILQRLQ VEGFAHVPEP APTADSALIA PFTMDREAYA RMFGPTTGDL VRLGLTNLWV
     RVEKDCTVYG DECAFGGGKT LREGMGQSSE RSATECLDTV ITNALIIDWS GIYKADIGIK
     NGLISAIGKA GNPDMMDGVH PDMIVGSSTD VIAGENKIVT AGGFDTHIHF ICPQQVDEAL
     ASGITTFLGG GTGPSTGTNA TTCTPGPTLM RQMIQACDGL PINVGITGKG NDSGGKSIEE
     QIRAGAAGLK LHEDWGSTPA AIDTCLDMCD KFDVQCMIHT DTLNESGFVE QTVKSFKNRT
     IHTYHTEGAG GGHAPDIISV VEHPNVLPSS TNPTRPFTMN TLDEHLDMLM VCHHLSKNIP
     EDVAFAESRI RAETIAAEDV LHDLGAISMM SSDSQAMGRC GEVILRTWNT AHKNKAQRGP
     LKEDEGTGAD NFRVKRYISK YTINPAIAQG MSHLIGSVEV GKLADLVIWH PSTFGTKPAQ
     VLKSGMIVAS QMGDPNGSIP TIEPVVMRRQ FGAFVPSTSI MWVSQASIDD GIVQSYGLKK
     RIEAVRNCRN IGKKDMKFND VMPKMRVDPE SYVVEADGVL CDAEPAEALP LTQDYFVY
//
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