UREA_CRYNH
ID UREA_CRYNH Reviewed; 833 AA.
AC O13465; J9VZV0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Urease;
DE EC=3.5.1.5;
DE AltName: Full=Urea amidohydrolase;
GN Name=URE1; ORFNames=CNAG_05540;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=10639402; DOI=10.1128/iai.68.2.443-448.2000;
RA Cox G.M., Mukherjee J., Cole G.T., Casadevall A., Perfect J.R.;
RT "Urease as a virulence factor in experimental cryptococcosis.";
RL Infect. Immun. 68:443-448(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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=AFR98966.2; Type=Erroneous gene model prediction; Evidence={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; AF006062; AAC62257.1; -; Genomic_DNA.
DR EMBL; CP003833; AFR98966.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_012053644.1; XM_012198254.1.
DR AlphaFoldDB; O13465; -.
DR SMR; O13465; -.
DR EnsemblFungi; AFR98966; AFR98966; CNAG_05540.
DR GeneID; 23888844; -.
DR HOGENOM; CLU_000980_0_0_1; -.
DR UniPathway; UPA00258; UER00370.
DR PHI-base; PHI:194; -.
DR Proteomes; UP000010091; Chromosome 14.
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; 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 Hydrolase; Metal-binding; Nickel.
FT CHAIN 1..833
FT /note="Urease"
FT /id="PRO_0000067528"
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"
FT CONFLICT 249
FT /note="G -> V (in Ref. 1; AAC62257)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="A -> R (in Ref. 1; AAC62257)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="P -> A (in Ref. 1; AAC62257)"
FT /evidence="ECO:0000305"
FT CONFLICT 700..703
FT /note="FWTA -> LLDG (in Ref. 1; AAC62257)"
FT /evidence="ECO:0000305"
FT CONFLICT 744..757
FT /note="GSQPEAAALNSIVW -> ALSLRPLHSIQLF (in Ref. 1;
FT AAC62257)"
FT /evidence="ECO:0000305"
FT CONFLICT 771..774
FT /note="FNIK -> YRLR (in Ref. 1; AAC62257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 833 AA; 90475 MW; 89E4D04C82FFE5ED CRC64;
MHLLPRETDK LILTTLGTLA QRRLARGLIL NRAETIALIS SQLQEFVRDG RHSVAELMDL
GKKMLGRRHV RKGVPESIHT IQVEGTFPDG VFLVTVDDPI SSDDGDLNNA FYGSFLPIPS
ADVFPAAPEP ADTLLGALIC RKETVKINAS RRRFRLEVKN AGDRPVQVGS HYHFLETNPA
LIFDRLLSYG YHLDIPAGTA VRFEPGEKKT VTMVEFGGKK IFHGGSGLGN GSFDENLRET
KVKEMVEKGG FGHKEQEKIE EGPVTEMNRE VYASMFGPTT GDKIKLADMD LWIEVEKDYT
VYGDECKFGG GKVIRDGGGQ ASGRHDHEVL DLVITNALIV DWTGIYKADI GVKNGIIVGI
GKAGNPDMMD GVTDGMIVGS STEVISGEKL ITTAGALDVH VHYISPQLMT EALASGITTV
IGGGTGPADG SNATTCTSSS FYMQNMIKAT DTIPLNFGFT GKGSDSGTNA MRDIIEAGAC
GLKVHEDWGA TPEVIDRALS MADEYDVQIN LHSDTLNESG YVESTLAAIK GRTIHSYHTE
GAGGGHAPDI IVVCEYENVL PSSTNPTRPY AVNTLDEHLD MLMICHGLDK SIPEDIAFAD
SRIRSETVAA EDVLQDTGAI SMISSDCQAM GRIGEVVTRT WRTAAKMKQF RGPLEGDEPT
RDNNRVKRYV AKYTINPAIT HGMSHLIGQV AVGCLADLVF WTAESFGARP EMILKGGVIA
WAAVGDANAS IPTVQPVLGR PMWGSQPEAA ALNSIVWVSQ ASLDKDLVKR FNIKKRAEAV
KNCRSIGKKD MKWNDTMPKM TVDPETYDVR ADGVLCDVPP ADKLPLTRRY FVY
