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 03-AUG-2022, entry version 154.
DE RecName: Full=Urease;
DE EC=3.5.1.5 {ECO:0000269|PubMed:8742356};
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; Schizosaccharomycetaceae;
OC 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA 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, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, AND SUBCELLULAR LOCATION.
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(+); 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 Evidence={ECO:0000269|PubMed:8742356};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000250};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for urea (at pH 7.5) {ECO:0000269|PubMed:8742356};
CC Vmax=713 umol/min/mg enzyme {ECO:0000269|PubMed:8742356};
CC pH dependence:
CC Optimum pH is 4-10. {ECO:0000269|PubMed:8742356};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000305|PubMed:8742356}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:8742356}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:8742356}.
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}.
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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 AlphaFoldDB; O00084; -.
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 PomBase; SPAC1952.11c; -.
DR VEuPathDB; FungiDB:SPAC1952.11c; -.
DR eggNOG; ENOG502QPKB; Eukaryota.
DR HOGENOM; CLU_000980_0_0_1; -.
DR InParanoid; O00084; -.
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:0035550; C:urease complex; IEA:InterPro.
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 Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Nickel;
KW Reference proteome.
FT CHAIN 1..835
FT /note="Urease"
FT /id="PRO_0000067529"
FT DOMAIN 399..835
FT /note="Urease"
FT ACT_SITE 590
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 487
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 487
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 489
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 630
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 487
FT /note="N6-carboxylysine"
FT /evidence="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
