ID A0A316YU41_9BASI Unreviewed; 841 AA.
AC A0A316YU41;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 13-SEP-2023, entry version 19.
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=FA10DRAFT_235889 {ECO:0000313|EMBL:PWN92751.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN92751.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN92751.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN92751.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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}.
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DR EMBL; KZ819634; PWN92751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YU41; -.
DR STRING; 215250.A0A316YU41; -.
DR InParanoid; A0A316YU41; -.
DR OrthoDB; 1408002at2759; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000245768; 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; 1.
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 NCBIfam; TIGR00192; urease_beta; 1.
DR NCBIfam; TIGR00193; urease_gam; 1.
DR PANTHER; PTHR33569; UREASE; 1.
DR PANTHER; PTHR33569: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; 1.
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:UP000245768}.
FT DOMAIN 403..841
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT ACT_SITE 594
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 408
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 410
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 491
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 491
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 493
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 520
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 546
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 634
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT MOD_RES 491
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ SEQUENCE 841 AA; 89332 MW; 32D7A8ECE6B5719A CRC64;
MHLLPREKDK IFLHQVGSLA QKRLARGVRL NQTEATALIA SVLQERIRDG NHSVAELMQH
GKTLLGRNHV LPGVESLLYE VMVEGTFHDG CFLVTVHDPI CTAKGNLKDA LYGSFLPVPN
DRLFGPAEED AEGLSGAVVV KQNADNIVLS PGRERLAMKV TNTGDRPIQV GSHYPFHETN
PALLFARLSA IGFRLDIAAG TAVRFEPGDV KTVPMVRIAG NQIVAGGNGI YNGPLSALAS
NAALLAEVKG RITSGRFQDE SESAEALAAP PPCSLSREAY AALYGPTVGD KVRLADSPLW
IEVERDMTAF GDECKFGGGK VLRDGMGQMT GKADAETLDT VVINALIVDW WGVVKADIGI
KNGHIVGIGK AGNPDVMDGV TEGMYVGSCT DVVAAEGLIV TAGAIDAHVH YICPDLCEEA
LASGITTVIG GGTGPSSGSS ATTCTPGKDH ARFMLRATDD IPLNFAFTGK GNDSNPGPLE
EQIRAGCAGL KLHEDWGTTP RAIDTCLSVC DQFDVQCNIH TDTLNESSFV EGTIAAFKGR
TIHTYHSEGA GGGHAPDIIT VCGESNVLPS STNPTRPYAK NTLDEHLDML MVCHHLSKNI
AEDVAFADSR IRAETVAAED VLQDQGAISI ISSDSQAMGR IGEVVSRTWR TAAKMRQVRG
PLDGDAAGND NNRVKRYVAK YTINPAIVHG MSHLIGSVEE GKLADLVLYK PSNFGTKPEM
IIKGGQIAWA QMGDANASIP TVQPIYGRPM YGAKPCAAPF NSIAFVSGVS ISTRTIAEYG
LRKRVEAVVG CRKVTKSDMK LNSALPKLTV DPESYDVLAD GELCTVPAAT ALPLTQAAHL
F
//
