UREA_ASPFU
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 03-AUG-2022, entry version 113.
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;
OC Aspergillus subgen. Fumigati.
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 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., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., 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., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA 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(+); Xref=Rhea:RHEA:20557,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; 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) from
CC 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-dependent
CC hydrolases superfamily. Urease alpha subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL88166.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ578495; CAE17672.1; -; mRNA.
DR EMBL; AAHF01000007; EAL88166.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_750204.1; XM_745111.1.
DR AlphaFoldDB; Q6A3P9; -.
DR SMR; Q6A3P9; -.
DR STRING; 746128.CADAFUBP00000484; -.
DR MEROPS; M38.982; -.
DR PRIDE; Q6A3P9; -.
DR GeneID; 3507289; -.
DR KEGG; afm:AFUA_1G04560; -.
DR eggNOG; ENOG502QPKB; Eukaryota.
DR HOGENOM; CLU_000980_0_0_1; -.
DR InParanoid; Q6A3P9; -.
DR OrthoDB; 183108at2759; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0035550; C:urease complex; IEA:InterPro.
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 Hydrolase; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..838
FT /note="Urease"
FT /id="PRO_0000067526"
FT DOMAIN 402..838
FT /note="Urease"
FT ACT_SITE 593
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 633
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 490
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT CONFLICT 159
FT /note="R -> P (in Ref. 1; CAE17672)"
FT /evidence="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
