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Database: UniProt
Entry: A0A024UVP3_9STRA
LinkDB: A0A024UVP3_9STRA
Original site: A0A024UVP3_9STRA 
ID   A0A024UVP3_9STRA        Unreviewed;       855 AA.
AC   A0A024UVP3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   11-DEC-2019, entry version 31.
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=H310_00423 {ECO:0000313|EMBL:ETW10020.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Stramenopiles; Oomycetes; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW10020.1, ECO:0000313|Proteomes:UP000024375};
RN   [1] {ECO:0000313|EMBL:ETW10020.1, ECO:0000313|Proteomes:UP000024375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETW10020.1,
RC   ECO:0000313|Proteomes:UP000024375};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) 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|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. {ECO:0000256|PIRNR:PIRNR001222,
CC       ECO:0000256|PIRSR:PIRSR001222-51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {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|PIRNR:PIRNR001222}.
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DR   EMBL; KI913952; ETW10020.1; -; Genomic_DNA.
DR   RefSeq; XP_008861431.1; XM_008863209.1.
DR   STRING; 157072.XP_008861431.1; -.
DR   EnsemblProtists; ETW10020; ETW10020; H310_00423.
DR   GeneID; 20077473; -.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000024375; 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   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:PIRSR001222-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024375}.
FT   DOMAIN          416..855
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        607
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   METAL           421
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           423
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           504
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           504
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           533
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           559
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           647
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         506
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         504
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ   SEQUENCE   855 AA;  92449 MW;  F40B3A2D5F53E248 CRC64;
     MRLSPREVEH LQLHQAGVVA QKRLARSLRL NYVETVALIA SQCLELIRDG RSVAEIMSLG
     KAMLGLRQVM DGVSAMLHDV QVEGTFPDGT KLVTVHNPIC RVDGDMSLAL YGSFFPVPSL
     ESFGPAEPSV DLNKQIIVVD DENGIELNGG RVPQRLVVKN MGDRPIQVGS HFHLIETNPI
     LDMDRRRAYG HRLNIPAGTA VRFEPGDVKT VSIVPIGGHR VISGGNNVAT GPVDQASIDG
     IVSTLVGRGF LHTPIDPTDE ELQSRPPPCI MSRQTYARTY GPTTGDRIRL GDTSLVVHVE
     MDFTVYGDEC TVLQTTRMRW HFYLSVGKFG GGKVLREGMG QATGCHADQV LDTVITNAVI
     VDYTGVYKAD IGIKHGVIWA IGKAGNPDVM DGVQDDMVVG VNTEVIAGEG LVVTAGGVDT
     HVHFICPQLF DEAISSGLTT LVGGGTGPAT GTKATTCTPH PDHVKRMLQA TDACSLNIGF
     TGKGNTASPI GLQDVVNAGV VGLKLHEDWG TTPSSIHVAL DVADANDIQV TIHTDTLNES
     SCVEQTIAAF GNRTIHTYHS EGAGGGHAPD IITVCGELHV LPSSTNPTRP FTVNTIEEHV
     DMLMVCHHLD KSIAEDVAFA ESRIREETIA AEDILHDIGA ISIISSDSQA MGRIGEVITR
     TWQTADKMKR QRGFLPEDAE TETDNLRVKR YIAKYTINPA IAHGMADWIG SVEVRKLADL
     VLWQPDHFGA KPELVLKGGS IVYSQMGDPN ASIPTPQPVR MRPMFGANGR AVGGTSIAFV
     SRACKEKQIA KGYGLGKRIE AVTKCRNLTK KHMKWNDALP KIEVDPETYQ VTVDGEVLTC
     LPSTWLPLSQ KYFLF
//
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