ID M7THT7_EUTLA Unreviewed; 853 AA.
AC M7THT7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 55.
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=UCREL1_3475 {ECO:0000313|EMBL:EMR69506.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR69506.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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; KB706069; EMR69506.1; -; Genomic_DNA.
DR RefSeq; XP_007791405.1; XM_007793214.1.
DR AlphaFoldDB; M7THT7; -.
DR STRING; 1287681.M7THT7; -.
DR MEROPS; M38.982; -.
DR KEGG; ela:UCREL1_3475; -.
DR eggNOG; ENOG502QPKB; Eukaryota.
DR HOGENOM; CLU_000980_0_0_1; -.
DR OMA; DTMDGVH; -.
DR OrthoDB; 1408002at2759; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000012174; 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; 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; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
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:UP000012174}.
FT DOMAIN 417..853
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT ACT_SITE 608
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 422
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 424
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 505
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 505
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 507
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 534
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 560
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 648
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT MOD_RES 505
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ SEQUENCE 853 AA; 90728 MW; 9DEC403A26164BCB CRC64;
MHLVPKELDK LVISQLGSLA QKRLARGLKL NHTEATALIA NNLQELIRDG QHTVADLMSL
GTTMLGRRHV LASVPSTLHS VQVEGTFPTG TYLVTVTNPI ATDDGDLARA LYSSFLPIPS
ADLFPPSEPA AYDAAKQPGA VVVVVSSSKE GSDEDGEDPS ISARIALNAN RRRIRLKVTS
TGDRPIQIGS HYHFIEANPQ LSFDRARAYG FRLDVPAGTS VRFEPGDAKT VSLVEIGGRR
VIRGGNNLAS GVVDLSRTGD IVAKLQEAGF AHAPEEPVGD PFLVDPYTID RAAYAAMFGP
TTGDVVRLGS TDLWVKVERD LTVYGDECKF GGGKTLREGM GQMSGCPDAE SLDVVIVNAL
IVDYTGIYKA DIGVKDGVIV GIGKAGNPDV MDGVTDGMIV GSCTDVIAGE GKIITAGGFD
SHIHFICPQQ AYESISSGIT TMLGGGTGPS AGTAATTCTP GANLMRQMLQ ACDELPLNIG
ITGKGNDSAP QALREQVLAG ACGLKLHEDW GTTPAAIDAC LGVCDELDVQ CLIHTDTLNE
SGYVESTIAA FKNRTIHTYH TEGAGGGHAP DIISVVELDN VLPSSTNPTR PYTRNTLDEH
LDMLMVCHHL SKNIPEDVAF AESRIRAETI AAEDVLHDLG AISMMSSDSQ AMGRCGEVIL
RTWNTAHKNK VQRGFLGEDL GTGADNFRVK RYVSKYTINP ALTQGMSHLV GSVEVGKLAD
LVVWDPAWFG TKPSLVVKSG LIAYAQMGDP NASIPTVQPV ISRPMFAPLV PQTSVLFVSQ
ASIDSGATAS YGLKKRVEPV RGCRSVGKKD MRFNDATPGM RVDPERYTVE ADGMVCAAEP
AVELPLTQAF YAY
//
