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Database: UniProt
Entry: F7VXN7_SORMK
LinkDB: F7VXN7_SORMK
Original site: F7VXN7_SORMK 
ID   F7VXN7_SORMK            Unreviewed;       855 AA.
AC   F7VXN7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   03-JUL-2019, entry version 50.
DE   RecName: Full=Urease {ECO:0000256|PIRNR:PIRNR001222};
DE            EC=3.5.1.5 {ECO:0000256|PIRNR:PIRNR001222};
DE   AltName: Full=Urea amidohydrolase {ECO:0000256|PIRNR:PIRNR001222};
GN   ORFNames=SMAC_02858 {ECO:0000313|EMBL:CCC10281.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) /
OS   K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC10281.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC10281.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC10281.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D.,
RA   Poeggeler S., Read N., Seiler S., Smith K., Zickler D., Kueck U.,
RA   Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence
RT   reads: Sordaria macrospora, a model organism for fungal
RT   morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5; Evidence={ECO:0000256|PIRNR:PIRNR001222};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001222,
CC         ECO:0000256|PIRSR:PIRSR001222-51};
CC       Note=Binds 2 nickel ions per subunit.
CC       {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1.
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-
CC       dependent hydrolases superfamily. Urease alpha subunit family.
CC       {ECO:0000256|PIRNR:PIRNR001222}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCC10281.1}.
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DR   EMBL; CABT02000012; CCC10281.1; -; Genomic_DNA.
DR   RefSeq; XP_003348361.1; XM_003348313.1.
DR   STRING; 5147.XP_003348361.1; -.
DR   EnsemblFungi; CCC10281; CCC10281; SMAC_02858.
DR   GeneID; 10805819; -.
DR   KEGG; smp:SMAC_02858; -.
DR   EuPathDB; FungiDB:SMAC_02858; -.
DR   eggNOG; ENOG410IGM6; Eukaryota.
DR   eggNOG; COG0804; LUCA.
DR   eggNOG; COG0831; LUCA.
DR   eggNOG; COG0832; LUCA.
DR   InParanoid; F7VXN7; -.
DR   KO; K01427; -.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
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   HAMAP; MF_01954; Urease_beta; 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   Complete proteome {ECO:0000313|Proteomes:UP000001881};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PROSITE-
KW   ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001222,
KW   ECO:0000256|PIRSR:PIRSR001222-51};
KW   Nickel {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-
KW   51}; Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT   DOMAIN      403    855       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    594    594       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       408    408       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       410    410       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       491    491       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       491    491       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       520    520       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       546    546       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       634    634       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     493    493       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     491    491       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   855 AA;  91838 MW;  6759376426FA3CD5 CRC64;
     MHLIPKELDK LAISQLGFLA QRRLARGVKL NHSEATALIA NNLQELIRDG NHCVADLMAL
     GATMLGRRHV LPEVTSTLHE IQVEGTFPSG TYLVTVHNPI SSDDGDLARA LYGSFLPIPP
     NDDSVFPLPP AAAYEASKQP GAVVCVKDAK VKLNEGRNRI RLKITSKGDR PIQVGSHYHF
     IETNPQLSFD RLRAYGYRLD IPAGTSVRFE PGDTKTVTLV EIGGNKVIRG GNNLASGRLD
     LSRAEEIIAK LQAAGFAHAP EPAGDAAFIS EPFTMDRRAY AVMFGPTVGD MVRLGSTDLW
     IKVEKDYTVY GDECKFGGGK TLREGMGQAT GRSDEETLDM VVTNALVVDW TGIYKADIGI
     KAGVIVGIGK AGNPDVMDGV TPGMIVGSCT DVVAGEGKII TAGGIDTHIH FICPQQAAEA
     LAAGITTFLG GGTGPSAGTN ATTCTPGAHY MRQMLQACDS LPLNIGITGK GNDSDPSALR
     EQIRAGACGL KLHEDWGTTP AAIDSCLTVC DELDVQCLIH TDTLNESGFM ESTIAAFAGR
     TIHTYHTEGA GGGHAPDIIS VVEYPNVLPS STNPTRPYTR NTLDEHLDML MVCHHLSKNI
     PEDVAFAESR IRAETIAAED VLHDLGAISM MSSDSQAMGR CGEVILRTWN TAHKNKLQRG
     FLPEDLAEAA ANNGDGDSPE NETQKADNYR VKRYISKYTI NPALAQGMAH LIGSIEVGKL
     ADLVVWDPAW FGTKPSLVIK SGLIACAMMG DPNASIPTVQ PVISRQMFAP MVAQTKVLFV
     SQASIDSGAV PGYNLKSRVE AVRGCRTVSK RDMKFNEKTP RMKVDPERYT VEADGEVCEA
     EPSSELPLTQ SWFVY
//
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