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Entry: N4UNG9_COLOR
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ID   N4UNG9_COLOR            Unreviewed;       835 AA.
AC   N4UNG9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   03-JUL-2019, entry version 36.
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   Name=ure1 {ECO:0000313|EMBL:TDZ20498.1};
GN   ORFNames=Cob_13318 {ECO:0000313|EMBL:ENH77308.1}, Cob_v006655
GN   {ECO:0000313|EMBL:TDZ20498.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 /
OS   LARS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:ENH77308.1};
RN   [1] {ECO:0000313|EMBL:ENH77308.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MAFF 240422 {ECO:0000313|EMBL:ENH77308.1};
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT   gloeosporioides.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the
RT   hemibiotrophic stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
RN   [3] {ECO:0000313|EMBL:TDZ20498.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=104-T {ECO:0000313|EMBL:TDZ20498.1};
RA   Gan P., Shirasu K.;
RT   "Hybrid genome sequence and assembly of Colletotrichum orbiculare.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000014480}
RP   GENOME REANNOTATION.
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA   Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA   Shirasu K.;
RT   "Genome sequence resources for four phytopathogenic fungi from the
RT   Colletotrichum orbiculare species complex.";
RL   Mol. Plant Microbe Interact. 0:0-0(2019).
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}.
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DR   EMBL; KB726094; ENH77308.1; -; Genomic_DNA.
DR   EMBL; AMCV02000017; TDZ20498.1; -; Genomic_DNA.
DR   STRING; 5465.ENH77308; -.
DR   EnsemblFungi; ENH77308; ENH77308; Cob_13318.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000014480; 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   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:UP000014480};
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:UP000014480}.
FT   DOMAIN      399    835       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    590    590       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       404    404       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       406    406       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       487    487       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       487    487       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       516    516       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       542    542       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       630    630       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     489    489       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     487    487       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   835 AA;  89787 MW;  8F01C1494DCA4F56 CRC64;
     MHLVPKELDK LVISQLGSLA QRRLARGVKL NHSEAMALIA SNLQELIRDG NHTVADLMSL
     GATMLGRRHV LPAVCSTLHE IQVEGTFPSG TYLVTVHHPI STDDGDLARA LYGSFLPIPS
     NDIFSLPEVT AYEPKKQPGA VVVASKRVTL SQGRNRIRLK VTSRGDRPIQ VGSHYHFIET
     NPQLEFDREK SYGYRLDIPA GTSVRFEPGD EKTVTLVEIG GNKVIRGGNR LATGGVELWR
     AKEIVEKLQL AGFAHAPEPE AVLNHAELYQ MDRSAYATMF GPTTDDLVRL GGTDLWIRVE
     KDFTVYGDEC KFGGGKTLRE GMGQATGRPD SESLDMVVTN ALVVDWSGIY KADIGVKNGM
     IVGIGKAGNP DVMDGVAPNM VVGSCTDVVA GEGKIITAGG IDTHIHFICP QQADEAVASG
     ITTMLGGGTG PSAGTSATTC TPGKNYMREM LQACDSLPLN IGITGKGNDS SPEALRDQVN
     AGACGLKLHE DWGSTPAAID TCLSVCDELD VQCLIHTDTL NESGFVESTI NAFAGRTIHT
     YHTEGAGGGH APDIISVVEH PNVLPSSTNP TRPYTRNTLD EHLDMLMVCH HLSKNIPEDV
     AFAESRIRAE TIAAEDVLHD LGAISMMSSD SQAMGRCGEV VLRTWNTAHK NKVQRGALPE
     DEGTGADNFR VKRYVSKYTI NPALAQGFGH LVGSVEIGKL ADLVVWDPAW FGTKPTLVIK
     SGLIACAQMG DPNASIPTVQ PIIARPMFAP LVPPSSVLFV SQSSIDSGAI ASYGLKKRVE
     AVRNCRGVGK KDMRFNDSMP KMRVDPESYV VEADGEVCRA DPAEDLPLTQ AYYVY
//
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