UREA_ARATH
ID UREA_ARATH Reviewed; 838 AA.
AC Q9SR52;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Urease {ECO:0000303|PubMed:16244137};
DE EC=3.5.1.5 {ECO:0000269|PubMed:16244137};
DE AltName: Full=Urea amidohydrolase {ECO:0000305};
GN Name=URE {ECO:0000305};
GN OrderedLocusNames=At1g67550 {ECO:0000312|Araport:AT1G67550};
GN ORFNames=F12B7.10 {ECO:0000312|EMBL:AAG52306.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16244137; DOI=10.1104/pp.105.070292;
RA Witte C.P., Rosso M.G., Romeis T.;
RT "Identification of three urease accessory proteins that are required for
RT urease activation in Arabidopsis.";
RL Plant Physiol. 139:1155-1162(2005).
CC -!- FUNCTION: Urea hydrolase involved in nitrogen recycling from ureide,
CC purine, and arginine catabolism. {ECO:0000269|PubMed:16244137}.
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:0000269|PubMed:16244137};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20558;
CC Evidence={ECO:0000269|PubMed:16244137};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000250|UniProtKB:P07374};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000250|UniProtKB:P07374};
CC -!- ACTIVITY REGULATION: Requires the three urease accessory proteins URED,
CC UREF AND UREG for its activation. {ECO:0000269|PubMed:16244137}.
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P07374}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000250|UniProtKB:P07374}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants cannot grow on medium with urea as the
CC sole source of nitrogen. {ECO:0000269|PubMed:16244137}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the metallo-dependent
CC hydrolases superfamily. Urease alpha subunit family. {ECO:0000305}.
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DR EMBL; AC011020; AAG52306.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34663.1; -; Genomic_DNA.
DR PIR; A96699; A96699.
DR RefSeq; NP_176922.1; NM_105422.4.
DR AlphaFoldDB; Q9SR52; -.
DR SMR; Q9SR52; -.
DR ComplexPortal; CPX-1296; Urease activation complex.
DR STRING; 3702.AT1G67550.1; -.
DR MEROPS; M38.982; -.
DR iPTMnet; Q9SR52; -.
DR PaxDb; Q9SR52; -.
DR PRIDE; Q9SR52; -.
DR ProteomicsDB; 228661; -.
DR EnsemblPlants; AT1G67550.1; AT1G67550.1; AT1G67550.
DR GeneID; 843076; -.
DR Gramene; AT1G67550.1; AT1G67550.1; AT1G67550.
DR KEGG; ath:AT1G67550; -.
DR Araport; AT1G67550; -.
DR TAIR; locus:2008798; AT1G67550.
DR eggNOG; ENOG502QPKB; Eukaryota.
DR HOGENOM; CLU_000980_0_0_1; -.
DR InParanoid; Q9SR52; -.
DR OMA; GFDSHIH; -.
DR OrthoDB; 183108at2759; -.
DR PhylomeDB; Q9SR52; -.
DR BioCyc; ARA:AT1G67550-MON; -.
DR UniPathway; UPA00258; UER00370.
DR PRO; PR:Q9SR52; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SR52; baseline and differential.
DR Genevisible; Q9SR52; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0150006; C:urease activator complex; IPI:ComplexPortal.
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; IDA:TAIR.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IDA:TAIR.
DR GO; GO:0043419; P:urea catabolic process; IDA:ComplexPortal.
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; IPR040881; Urease_linker.
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 Pfam; PF18473; Urease_linker; 1.
DR PIRSF; PIRSF001222; Urease; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51278; SSF51278; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..838
FT /note="Urease"
FT /id="PRO_0000424246"
FT DOMAIN 400..838
FT /note="Urease"
FT ACT_SITE 591
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 405
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 407
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 488
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 488
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 490
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 517
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 543
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 631
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT MOD_RES 488
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P07374"
SQ SEQUENCE 838 AA; 91024 MW; E60C9DD1B07FE754 CRC64;
MKLLPREIEK LELHQAGFLA QKRLARGIRL NYTEAVALIA TQILEFIRDG DKSVAELMDI
GRQLLGRRQV LPAVLHLLYT VQVEGTFRDG TKLVTVHEPI SLENGNLELA LHGSFLPVPS
LDKFPEVHEG VIIPGDMKYG DGSIIINHGR KAVVLKVVNT GDRPVQVGSH YHFIEVNPLL
VFDRRKALGM RLNIPAGTAV RFEPGERKSV VLVNIGGNKV IRGGNGIVDG LVDDVNWTVL
METMERRGFK HLEDIDASEG IAGEDPRFTT MISREKYANM YGPTTGDKLR LGDTNLYARI
EKDYTVYGDE CVFGGGKVLR EGMGQGIEQA EALSLDTVIT NSVIIDYSGI YKADIGIKNG
HIVGIGKAGN PDTMHGVQNN MLIGNKTEVI AGEGMIVTAG AIDCHVHFIC PQLVYEAVSS
GITTMVGGGT GPAYGTRATT CTPSPFDMKL MLQSTDSLPL NFGFTGKGNT AKPLELRHIV
EAGAMGLKLH EDWGTTPAAI DNCLAVAEEY DIQVNIHTDT LNESGFVEHT INAFRGRTIH
TYHSEGAGGG HAPDIIRVCG VKNVLPSSTN PTRPYTKNTV DEHLDMLMVC HHLDKNIPED
VAFAESRIRA ETIAAEDILH DMGAISIISS DSQAMGRIGE VISRTWQTAD KMKAQRGAID
PNMADDDNSR IKRYIAKYTI NPAIANGFAD LIGSVEVKKL ADLVIWQPAF FGAKPEMIIK
GGNIAWANMG DANASIPTPE PVISRPMFGA FGKAGSENSV AFVSKAALRK GVKELYGLKK
RVVAVSNVRQ LTKLDMKLND ALPEITVDPE TYVVTANGEV LTCAPADSVP LSRNYFLF
