ID A0A2C5YCR5_9HYPO Unreviewed; 796 AA.
AC A0A2C5YCR5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=Urease {ECO:0000256|ARBA:ARBA00013883, ECO:0000256|PIRNR:PIRNR001222};
DE EC=3.5.1.5 {ECO:0000256|ARBA:ARBA00012934, ECO:0000256|PIRNR:PIRNR001222};
DE AltName: Full=Urea amidohydrolase {ECO:0000256|ARBA:ARBA00030395, ECO:0000256|PIRNR:PIRNR001222};
GN ORFNames=CDD81_2 {ECO:0000313|EMBL:PHH67305.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH67305.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH67305.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH67305.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000242,
CC ECO:0000256|PIRNR:PIRNR001222};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000256|PIRSR:PIRSR001222-51};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000256|PIRSR:PIRSR001222-
CC 51};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000256|ARBA:ARBA00004897,
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-dependent
CC hydrolases superfamily. Urease alpha subunit family.
CC {ECO:0000256|ARBA:ARBA00007966}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHH67305.1}.
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DR EMBL; NJET01000001; PHH67305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5YCR5; -.
DR STRING; 1399860.A0A2C5YCR5; -.
DR OrthoDB; 1408002at2759; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000226192; Unassembled WGS sequence.
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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.10.150.10; Urease, beta subunit; 1.
DR Gene3D; 3.30.280.10; Urease, gamma-like subunit; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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-like.
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 NCBIfam; TIGR01792; urease_alph; 1.
DR PANTHER; PTHR43440; UREASE; 1.
DR PANTHER; PTHR43440:SF1; UREASE; 1.
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; 2.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51278; Urease, beta-subunit; 1.
DR SUPFAM; SSF54111; Urease, gamma-subunit; 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001222};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR001222};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRNR:PIRNR001222};
KW Reference proteome {ECO:0000313|Proteomes:UP000226192}.
FT DOMAIN 360..796
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT ACT_SITE 551
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 365
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 367
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 448
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 448
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 477
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 503
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 591
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT MOD_RES 448
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ SEQUENCE 796 AA; 85110 MW; 790EAC15EE7A083E CRC64;
MHLVPKELDK LVLAQLGLLA QRRLARGVRL NHSEATALIA NNLHELIRDG NHSVEGTFPM
GTYLVTVHNP ISTDDGDLRR ALYGSFLPIP DNDAFPLFPD MDYDLLQQPG VVVAVKGKII
LNQGRRRVGS HFHFVEANPE LLFDRALAYG CRLDIAAGTS VRFEPGDTKT VTLVEIGGSR
VIRGGNNLAC GPVDLMRVDS LVTSLQAAGF AHAPEPLADA GLFPEIPEVF DMDRSAYANM
FGPTTGDCVR LGSTDLWICV ERDMTTYGDE CKFGGGKTLR EGMGQATGRT ADESLDLVVT
NALIVDWSGI YKADIGVKDG IIVGIGKAGS PDVMDGVSAN MVVGSCTDVI AAEGKIVTAG
GIDTHVHFIC PQQAEESLAS GITTMLGGGT GPSAGSNATT CTPGRNNLRN MLQASDSLPV
NVGITGKGCD SAPQALREQI AAGACGLKVH EDWGATPAAI DACLTVCDEL DVQCCIHTDT
LNESGYVEST LAAFKGRTVH TYHTEGAGGG HAPDIISVVE HSNVLPASTN PTRPFTRNTL
DEHLDMLMVC HHLSKNIPED VAFAESRIRA ETIAAEDVLQ DMGAISIMSS DSQAMGRCGE
VIVRTWNTAH KNKQQRGALE QDEGSRADNW RVRRYIAKYT INPAVAQGFA HAIGSIEPGK
LADLVLWDPA WFGTKPTTVV KGGIIAWSQM GDANASIPTV QPVIGRPMYA PLIPSCKMLF
VSQASVDSGA IASYGLRSRI EPVRNCRGIS KADMRLNDAR PRMRVDAESY AVEANGEVLR
AEPAELLPLA QAYYVF
//
