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Database: UniProt
Entry: F9X890_ZYMTI
LinkDB: F9X890_ZYMTI
Original site: F9X890_ZYMTI 
ID   F9X890_ZYMTI            Unreviewed;       842 AA.
AC   F9X890;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   03-JUL-2019, entry version 50.
DE   RecName: Full=Urease {ECO:0000256|PIRNR:PIRNR001222};
DE            EC=3.5.1.5 {ECO:0000256|PIRNR:PIRNR001222};
DE   AltName: Full=Urea amidohydrolase {ECO:0000256|PIRNR:PIRNR001222};
GN   ORFNames=MYCGRDRAFT_85598 {ECO:0000313|EMBL:EGP87878.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf
OS   blotch fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP87878.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP87878.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J.,
RA   Crane C.F., Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J.,
RA   Aerts A., Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J.,
RA   van der Burgt A., Canto-Canche B., Churchill A.C.L., Conde-Ferraez L.,
RA   Cools H.J., Coutinho P.M., Csukai M., Dehal P., De Wit P.,
RA   Donzelli B., van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E.,
RA   Henrissat B., Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y.,
RA   Kuzniar A., Lindquist E., Lombard V., Maliepaard C., Martins N.,
RA   Mehrabi R., Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A.,
RA   Schmutz J., Schouten H.J., Shapiro H., Stergiopoulos I.,
RA   Torriani S.F.F., Tu H., de Vries R.P., Waalwijk C., Ware S.B.,
RA   Wiebenga A., Zwiers L.-H., Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella
RT   graminicola reveals dispensome structure, chromosome plasticity, and
RT   stealth pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
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; Evidence={ECO:0000256|PIRNR:PIRNR001222};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001222,
CC         ECO:0000256|PIRSR:PIRSR001222-51};
CC       Note=Binds 2 nickel ions per subunit.
CC       {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR001222}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR001222-50}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the metallo-
CC       dependent hydrolases superfamily. Urease alpha subunit family.
CC       {ECO:0000256|PIRNR:PIRNR001222}.
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DR   EMBL; CM001199; EGP87878.1; -; Genomic_DNA.
DR   RefSeq; XP_003852902.1; XM_003852854.1.
DR   STRING; 1047171.Mycgr3P85598; -.
DR   EnsemblFungi; Mycgr3T85598; Mycgr3P85598; Mycgr3G85598.
DR   GeneID; 13397223; -.
DR   KEGG; ztr:MYCGRDRAFT_85598; -.
DR   InParanoid; F9X890; -.
DR   KO; K01427; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000008062; Chromosome 4.
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   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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008062};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PROSITE-
KW   ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001222,
KW   ECO:0000256|PIRSR:PIRSR001222-51};
KW   Nickel {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-
KW   51}; Reference proteome {ECO:0000313|Proteomes:UP000008062}.
FT   DOMAIN      406    842       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    597    597       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       411    411       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       413    413       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       494    494       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       494    494       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       523    523       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       549    549       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       637    637       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     496    496       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     494    494       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   842 AA;  91590 MW;  0CA25589813CEA2C CRC64;
     MQLAPKEIDK LLITQTGFLA QRRLARGVRL NHTEALALIA SVIQELICDG NHTVADLMSL
     GTTLLGRRHV LPSVPHTLSE MMVEGTFVNG TYLVTIHNPI ATDEGNLERA LYGSFLPVPD
     QDKFPWPPVE GLEAWEEEKM PGAVVAVKGD RGRIKLSEGR KRIKLKVTSK GDRPIQVGSH
     YHFIETNPKL EFDRLKARGM RLDIAAGTSI RFEPGDSRTV TLVEIAGNQV IRGGNDLAPG
     HIHDASITDD ILQRLQAGGF LHVEQNPMAD QALEPFSMDR ESYISMFGPT VGDKIRLGPT
     DLWIQIEHDM TDHGDECTFG GGKTIRDGMG QASGRADSEC LDTVITNAVI VDWSGIYKAD
     IGIKNGLIAG IGKAGNPDVM ANVDPNMIVG VATDVIAGEH KIVTAGGFDS HIHLICPQQA
     YEAIASGITT FLGGGTGPST STNATTCTPS TNMIKWMLQA CDELPMNIGI TGKGNDADPK
     GLREQAEAGV CGLKLHEDWG TTPKAIDTCL TVCDEHDIQC LIHTDTLNES GFVETTVASF
     KDRTIHTYHT EGAGGGHAPD IISVVEHNNV LPSSTNPTRP FTNNTLDEHL DMLMVCHHLS
     RNIPEDVAFA ESRIRAETIA AEDVLHDLGA ISMMSSDSQA MGRCGEVILR TWNTAHKNKV
     QRGFLPEDQG TGVDNFRVKR YISKYTINPS ITQGMGHLIG SVEVGKLADL VLWNPANFGA
     KPAQVVKGGM ISWSQMGDPN ASIPTVEPVI MRPMFGAMNP NRSVMWVSKA SVENGKVEGY
     GLKKRIEAVK GCRRIGKKDM KWNDAMPRMK VDPERYTVEA DGMVCKAEPA DTLPLSQAYF
     MY
//
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