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Database: UniProt
Entry: UREA_SCHPO
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Original site: UREA_SCHPO 
ID   UREA_SCHPO              Reviewed;         835 AA.
AC   O00084; Q9URH4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-OCT-2019, entry version 144.
DE   RecName: Full=Urease;
DE            EC=3.5.1.5;
DE   AltName: Full=Urea amidohydrolase;
GN   Name=ure1; ORFNames=SPAC1952.11c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9339351; DOI=10.1007/s002940050273;
RA   Tange Y., Niwa O.;
RT   "Identification of the ure1+ gene encoding urease in fission yeast.";
RL   Curr. Genet. 32:244-246(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-18 AND 129-153, AND CHARACTERIZATION.
RX   PubMed=8742356; DOI=10.1139/m96-021;
RA   Lubbers M.W., Rodriguez S.B., Honey N.K., Thornton R.J.;
RT   "Purification and characterization of urease from Schizosaccharomyces
RT   pombe.";
RL   Can. J. Microbiol. 42:132-140(1996).
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: Homodimer. {ECO:0000305}.
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}.
DR   EMBL; AB002590; BAA19550.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB52575.1; -; Genomic_DNA.
DR   PIR; T37939; T37939.
DR   RefSeq; NP_594813.1; NM_001020242.2.
DR   SMR; O00084; -.
DR   BioGrid; 279019; 6.
DR   STRING; 4896.SPAC1952.11c.1; -.
DR   MEROPS; M38.982; -.
DR   MaxQB; O00084; -.
DR   PaxDb; O00084; -.
DR   PRIDE; O00084; -.
DR   EnsemblFungi; SPAC1952.11c.1; SPAC1952.11c.1:pep; SPAC1952.11c.
DR   GeneID; 2542563; -.
DR   KEGG; spo:SPAC1952.11c; -.
DR   EuPathDB; FungiDB:SPAC1952.11c; -.
DR   PomBase; SPAC1952.11c; -.
DR   HOGENOM; HOG000075064; -.
DR   InParanoid; O00084; -.
DR   KO; K01427; -.
DR   OMA; GFDSHIH; -.
DR   PhylomeDB; O00084; -.
DR   UniPathway; UPA00258; UER00370.
DR   PRO; PR:O00084; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IDA:PomBase.
DR   GO; GO:0043419; P:urea catabolic process; IDA:PomBase.
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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Nickel; Reference proteome.
FT   CHAIN         1    835       Urease.
FT                                /FTId=PRO_0000067529.
FT   DOMAIN      399    835       Urease.
FT   ACT_SITE    590    590       Proton donor. {ECO:0000250}.
FT   METAL       404    404       Nickel 1; via tele nitrogen.
FT                                {ECO:0000250}.
FT   METAL       406    406       Nickel 1; via tele nitrogen.
FT                                {ECO:0000250}.
FT   METAL       487    487       Nickel 1; via carbamate group.
FT                                {ECO:0000250}.
FT   METAL       487    487       Nickel 2; via carbamate group.
FT                                {ECO:0000250}.
FT   METAL       516    516       Nickel 2; via pros nitrogen.
FT                                {ECO:0000250}.
FT   METAL       542    542       Nickel 2; via tele nitrogen.
FT                                {ECO:0000250}.
FT   METAL       630    630       Nickel 1. {ECO:0000250}.
FT   BINDING     489    489       Substrate. {ECO:0000250}.
FT   MOD_RES     487    487       N6-carboxylysine. {ECO:0000250}.
SQ   SEQUENCE   835 AA;  91182 MW;  AFB447F39DC4EF4C CRC64;
     MQPRELHKLT LHQLGSLAQK RLCRGVKLNK LEATSLIASQ IQEYVRDGNH SVADLMSLGK
     DMLGKRHVQP NVVHLLHEIM IEATFPDGTY LITIHDPICT TDGNLEHALY GSFLPTPSQE
     LFPLEEEKLY APENSPGFVE VLEGEIELLP NLPRTPIEVR NMGDRPIQVG SHYHFIETNE
     KLCFDRSKAY GKRLDIPSGT AIRFEPGVMK IVNLIPIGGA KLIQGGNSLS KGVFDDSRTR
     EIVDNLMKQG FMHQPESPLN MPLQSARPFV VPRKLYAVMY GPTTNDKIRL GDTNLIVRVE
     KDFTEYGNES VFGGGKVIRD GTGQSSSKSM DECLDTVITN AVIIDHTGIY KADIGIKNGY
     IVGIGKAGNP DTMDNIGENM VIGSSTDVIS AENKIVTYGG MDSHVHFICP QQIEEALASG
     ITTMYGGGTG PSTGTNATTC TPNKDLIRSM LRSTDSYPMN IGLTGKGNDS GSSSLKEQIE
     AGCSGLKLHE DWGSTPAAID SCLSVCDEYD VQCLIHTDTL NESSFVEGTF KAFKNRTIHT
     YHVEGAGGGH APDIISLVQN PNILPSSTNP TRPFTTNTLD EELDMLMVCH HLSRNVPEDV
     AFAESRIRAE TIAAEDILQD LGAISMISSD SQAMGRCGEV ISRTWKTAHK NKLQRGALPE
     DEGSGVDNFR VKRYVSKYTI NPAITHGISH IVGSVEIGKF ADLVLWDFAD FGARPSMVLK
     GGMIALASMG DPNGSIPTVS PLMSWQMFGA HDPERSIAFV SKASITSGVI ESYGLHKRVE
     AVKSTRNIGK KDMVYNSYMP KMTVDPEAYT VTADGKVMEC EPVDKLPLSQ SYFIF
//
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