UREA_CRYNJ
ID UREA_CRYNJ Reviewed; 833 AA.
AC P0CS22; Q55IZ5; Q5KCQ6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Urease;
DE EC=3.5.1.5;
DE AltName: Full=Urea amidohydrolase;
GN Name=URE1; OrderedLocusNames=CNH01900;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017348; AAW45058.1; -; Genomic_DNA.
DR RefSeq; XP_572365.1; XM_572365.1.
DR AlphaFoldDB; P0CS22; -.
DR SMR; P0CS22; -.
DR STRING; 5207.AAW45058; -.
DR MEROPS; M38.982; -.
DR PaxDb; P0CS22; -.
DR EnsemblFungi; AAW45058; AAW45058; CNH01900.
DR GeneID; 3259018; -.
DR KEGG; cne:CNH01900; -.
DR VEuPathDB; FungiDB:CNH01900; -.
DR eggNOG; ENOG502QPKB; Eukaryota.
DR HOGENOM; CLU_000980_0_0_1; -.
DR InParanoid; P0CS22; -.
DR OMA; GFDSHIH; -.
DR OrthoDB; 183108at2759; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000002149; Chromosome 8.
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 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; 2.
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 Hydrolase; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..833
FT /note="Urease"
FT /id="PRO_0000067527"
FT DOMAIN 395..833
FT /note="Urease"
FT ACT_SITE 586
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 483
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 483
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 485
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 626
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 483
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 833 AA; 90455 MW; E090343FE3252584 CRC64;
MHLLPRETDK LIVTTLGTLA QRRLARGLIL NRAETIALIS SQLQEFIRDG RHSVAELMDL
GKKMLGRRHV RKGVPESIHT IQVEGTFPDG VFLVTVDDPI SSDDGDLNNA FYGSFLPIPS
ADVFPAAPEP ADTLLGALIC RKEPIKINAS RRRFKLEVKN AGDRPIQVGS HYHFLETNPA
LIFDRLLSYG YHLDIPAGTA VRFEPGEKKT VTMVEFGGKK IFHGGSGLAS GSFDENLRET
KVKEMVEKGG FGHKDQEKVE EGPTTEMNRE VYASMFGPTT GDKIKLADMD LWIEVEKDYT
VYGEECKFGG GKVLRDGGGQ ASGRHEHEVL DLVITNALIV DWNGIYKADI GVKNGIIVGI
GKAGNPDMMD GVTDGMIVGS STEVIAGEKL IITAGALDVH VHYICPQLMT EALASGITTV
VGGGTGPADG SNATTCTSSS FYMQNMIKAT DTVPLNFGFT GKGNDSGTNA LRDVIEAGAC
GLKVHEDWGA TPEVIDRALS IADEYDVQVN LHSDTLNESG YVESTLAAIK GRTIHSYHTE
GAGGGHAPDI IVVCEYENVL PSSTNPTRPY AVNTLDEHLD MLMVCHHLDK SIPEDIAFAD
SRIRSETVAA EDVLQDTGAI SMISSDCQAM GRIGEVITRT WRTAAKMKQF RGPLEGDEPT
RDNNRVKRYV AKYTINPAIT HGMSHLIGQV AVGCLADLVF WTAESFGARP EMILKGGVIA
WAAMGDANAS IPTVQPVIGR PMWGSQPEAA ALNSIVWVSQ ASLDKDLVKR FNIKKRAEAV
KNCRAIGKKD MKWNDSMPKM TVDPETYDVH ADGVLCDVPP ADKLPLTKRY FVY
