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Protein

Urease

Gene
N/A
Organism
Canavalia ensiformis (Jack bean) (Dolichos ensiformis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Urea hydrolase involved in nitrogen recycling from ureide, purine, and arginine catabolism.By similarity

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.

Cofactori

Ni cationBy similarityNote: Binds 2 nickel ions per subunit.By similarity

Pathwayi: urea degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and NH(3) from urea (urease route).
Proteins known to be involved in this subpathway in this organism are:
  1. Urease, Urease
This subpathway is part of the pathway urea degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and NH(3) from urea (urease route), the pathway urea degradation and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi407 – 4071Nickel 1; via tele nitrogen
Metal bindingi409 – 4091Nickel 1; via tele nitrogen
Metal bindingi490 – 4901Nickel 1; via carbamate group
Metal bindingi490 – 4901Nickel 2; via carbamate group
Binding sitei492 – 4921SubstrateBy similarity
Metal bindingi519 – 5191Nickel 2; via pros nitrogen
Metal bindingi545 – 5451Nickel 2; via tele nitrogen
Active sitei593 – 5931Proton donorBy similarity
Metal bindingi633 – 6331Nickel 1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

BRENDAi3.5.1.5. 1091.
SABIO-RKP07374.
UniPathwayiUPA00258; UER00370.

Protein family/group databases

MEROPSiM38.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Urease (EC:3.5.1.5)
Alternative name(s):
Urea amidohydrolase
OrganismiCanavalia ensiformis (Jack bean) (Dolichos ensiformis)
Taxonomic identifieri3823 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4161.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 840840UreasePRO_0000067524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei490 – 4901N6-carboxylysine1 Publication

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two nickel ions.1 Publication

Interactioni

Subunit structurei

Homohexamer.By similarity

Chemistry

BindingDBiP07374.

Structurei

Secondary structure

1
840
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2521Combined sources
Helixi32 – 4918Combined sources
Helixi54 – 607Combined sources
Helixi61 – 633Combined sources
Helixi67 – 693Combined sources
Helixi74 – 774Combined sources
Beta strandi79 – 879Combined sources
Beta strandi90 – 989Combined sources
Beta strandi102 – 1043Combined sources
Helixi107 – 1104Combined sources
Turni111 – 1133Combined sources
Helixi121 – 1233Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi151 – 1599Combined sources
Beta strandi165 – 1684Combined sources
Helixi173 – 1753Combined sources
Beta strandi180 – 1823Combined sources
Helixi184 – 1874Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi207 – 2148Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi230 – 2334Combined sources
Helixi234 – 24714Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi273 – 2753Combined sources
Helixi276 – 2838Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi319 – 3235Combined sources
Turni324 – 3263Combined sources
Beta strandi329 – 3313Combined sources
Helixi333 – 3353Combined sources
Beta strandi338 – 34811Combined sources
Beta strandi351 – 36010Combined sources
Beta strandi363 – 3686Combined sources
Turni373 – 3753Combined sources
Beta strandi390 – 3934Combined sources
Beta strandi398 – 4014Combined sources
Beta strandi403 – 4097Combined sources
Helixi414 – 4218Combined sources
Beta strandi424 – 4307Combined sources
Beta strandi432 – 4343Combined sources
Helixi436 – 4405Combined sources
Helixi447 – 45610Combined sources
Turni457 – 4593Combined sources
Beta strandi460 – 46910Combined sources
Beta strandi473 – 4753Combined sources
Helixi476 – 4849Combined sources
Beta strandi487 – 4926Combined sources
Turni493 – 4953Combined sources
Helixi499 – 51214Combined sources
Beta strandi515 – 5195Combined sources
Helixi529 – 5368Combined sources
Beta strandi541 – 5433Combined sources
Turni544 – 5474Combined sources
Turni554 – 5563Combined sources
Helixi557 – 5626Combined sources
Beta strandi566 – 5727Combined sources
Helixi581 – 59212Combined sources
Helixi600 – 60910Combined sources
Helixi612 – 62312Combined sources
Beta strandi629 – 6313Combined sources
Turni635 – 6373Combined sources
Helixi640 – 6423Combined sources
Helixi643 – 65816Combined sources
Helixi670 – 6789Combined sources
Turni679 – 6813Combined sources
Helixi682 – 6887Combined sources
Turni691 – 6933Combined sources
Beta strandi694 – 6974Combined sources
Beta strandi705 – 7084Combined sources
Helixi710 – 7123Combined sources
Turni713 – 7153Combined sources
Beta strandi718 – 7225Combined sources
Beta strandi725 – 7317Combined sources
Beta strandi736 – 7394Combined sources
Beta strandi745 – 7484Combined sources
Helixi750 – 7523Combined sources
Helixi756 – 7594Combined sources
Beta strandi762 – 7654Combined sources
Helixi767 – 7715Combined sources
Helixi774 – 7785Combined sources
Beta strandi782 – 7865Combined sources
Helixi795 – 7973Combined sources
Beta strandi807 – 8093Combined sources
Turni811 – 8133Combined sources
Beta strandi816 – 8183Combined sources
Beta strandi832 – 8343Combined sources
Turni835 – 8373Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LA4X-ray2.05A1-840[»]
4GOAX-ray2.20A1-840[»]
4GY7X-ray1.49A1-840[»]
4H9MX-ray1.52A1-840[»]
ProteinModelPortaliP07374.
SMRiP07374. Positions 1-100, 274-840.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07374.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini402 – 840439UreaseAdd
BLAST

Sequence similaritiesi

Belongs to the urease family.Curated
Contains 1 urease domain.Curated

Family and domain databases

Gene3Di2.10.150.10. 1 hit.
2.30.40.10. 1 hit.
3.30.280.10. 1 hit.
HAMAPiMF_01953. Urease_alpha.
InterProiIPR006680. Amidohydro-rel.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
IPR008221. Urease.
IPR011612. Urease_alpha_N_dom.
IPR017950. Urease_AS.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR002019. Urease_beta.
IPR002026. Urease_gamma/gamma-beta_su.
IPR029754. Urease_Ni-bd.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
PF00699. Urease_beta. 1 hit.
PF00547. Urease_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF001222. Urease. 1 hit.
PRINTSiPR01752. UREASE.
ProDomiPD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51278. SSF51278. 1 hit.
SSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 2 hits.
SSF54111. SSF54111. 1 hit.
TIGRFAMsiTIGR01792. urease_alph. 1 hit.
TIGR00192. urease_beta. 1 hit.
TIGR00193. urease_gam. 1 hit.
PROSITEiPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSPREVEK LGLHNAGYLA QKRLARGVRL NYTEAVALIA SQIMEYARDG
60 70 80 90 100
EKTVAQLMCL GQHLLGRRQV LPAVPHLLNA VQVEATFPDG TKLVTVHDPI
110 120 130 140 150
SRENGELQEA LFGSLLPVPS LDKFAETKED NRIPGEILCE DECLTLNIGR
160 170 180 190 200
KAVILKVTSK GDRPIQVGSH YHFIEVNPYL TFDRRKAYGM RLNIAAGTAV
210 220 230 240 250
RFEPGDCKSV TLVSIEGNKV IRGGNAIADG PVNETNLEAA MHAVRSKGFG
260 270 280 290 300
HEEEKDASEG FTKEDPNCPF NTFIHRKEYA NKYGPTTGDK IRLGDTNLLA
310 320 330 340 350
EIEKDYALYG DECVFGGGKV IRDGMGQSCG HPPAISLDTV ITNAVIIDYT
360 370 380 390 400
GIIKADIGIK DGLIASIGKA GNPDIMNGVF SNMIIGANTE VIAGEGLIVT
410 420 430 440 450
AGAIDCHVHY ICPQLVYEAI SSGITTLVGG GTGPAAGTRA TTCTPSPTQM
460 470 480 490 500
RLMLQSTDDL PLNFGFTGKG SSSKPDELHE IIKAGAMGLK LHEDWGSTPA
510 520 530 540 550
AIDNCLTIAE HHDIQINIHT DTLNEAGFVE HSIAAFKGRT IHTYHSEGAG
560 570 580 590 600
GGHAPDIIKV CGIKNVLPSS TNPTRPLTSN TIDEHLDMLM VCHHLDREIP
610 620 630 640 650
EDLAFAHSRI RKKTIAAEDV LNDIGAISII SSDSQAMGRV GEVISRTWQT
660 670 680 690 700
ADKMKAQTGP LKCDSSDNDN FRIRRYIAKY TINPAIANGF SQYVGSVEVG
710 720 730 740 750
KLADLVMWKP SFFGTKPEMV IKGGMVAWAD IGDPNASIPT PEPVKMRPMY
760 770 780 790 800
GTLGKAGGAL SIAFVSKAAL DQRVNVLYGL NKRVEAVSNV RKLTKLDMKL
810 820 830 840
NDALPEITVD PESYTVKADG KLLCVSEATT VPLSRNYFLF
Length:840
Mass (Da):90,748
Last modified:February 1, 1994 - v3
Checksum:i1407E4ECCF00727F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti247 – 2471K → R AA sequence (PubMed:3402446).Curated
Sequence conflicti247 – 2471K → R AA sequence (Ref. 3) Curated
Sequence conflicti258 – 2581S → P AA sequence (PubMed:3402446).Curated
Sequence conflicti258 – 2581S → P AA sequence (Ref. 3) Curated
Sequence conflicti269 – 2691P → S AA sequence (PubMed:3402446).Curated
Sequence conflicti269 – 2691P → S AA sequence (Ref. 3) Curated
Sequence conflicti459 – 4591D → Y in AAA83831 (PubMed:1721034).Curated
Sequence conflicti653 – 6531K → P in AAA83831 (PubMed:1721034).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65260 mRNA. Translation: AAA83831.1.
PIRiJC1396. URJB.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65260 mRNA. Translation: AAA83831.1.
PIRiJC1396. URJB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LA4X-ray2.05A1-840[»]
4GOAX-ray2.20A1-840[»]
4GY7X-ray1.49A1-840[»]
4H9MX-ray1.52A1-840[»]
ProteinModelPortaliP07374.
SMRiP07374. Positions 1-100, 274-840.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP07374.
ChEMBLiCHEMBL4161.

Protein family/group databases

MEROPSiM38.982.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.
BRENDAi3.5.1.5. 1091.
SABIO-RKP07374.

Miscellaneous databases

EvolutionaryTraceiP07374.

Family and domain databases

Gene3Di2.10.150.10. 1 hit.
2.30.40.10. 1 hit.
3.30.280.10. 1 hit.
HAMAPiMF_01953. Urease_alpha.
InterProiIPR006680. Amidohydro-rel.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
IPR008221. Urease.
IPR011612. Urease_alpha_N_dom.
IPR017950. Urease_AS.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR002019. Urease_beta.
IPR002026. Urease_gamma/gamma-beta_su.
IPR029754. Urease_Ni-bd.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
PF00699. Urease_beta. 1 hit.
PF00547. Urease_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF001222. Urease. 1 hit.
PRINTSiPR01752. UREASE.
ProDomiPD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51278. SSF51278. 1 hit.
SSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 2 hits.
SSF54111. SSF54111. 1 hit.
TIGRFAMsiTIGR01792. urease_alph. 1 hit.
TIGR00192. urease_beta. 1 hit.
TIGR00193. urease_gam. 1 hit.
PROSITEiPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of a jack bean urease-encoding cDNA."
    Riddles P.W., Whan V., Blakeley R.L., Zerner B.
    Gene 108:265-267(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The structure of jack bean urease. The complete amino acid sequence, limited proteolysis and reactive cysteine residues."
    Takishima K., Suga T., Mamiya G.
    Eur. J. Biochem. 175:151-165(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  3. "Complete amino acid sequence of jack bean urease."
    Mamiya G., Takishima K., Masakuni M., Kayumi T., Ogawa K., Sekita T.
    Proc. Jpn. Acad., B, Phys. Biol. Sci. 61:395-398(1985)
    Cited for: PROTEIN SEQUENCE.
  4. "Location of the essential cysteine residue of jack bean urease."
    Takishima K., Mamiya G.
    Protein Seq. Data Anal. 1:103-106(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 591-637.
  5. "Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure."
    Balasubramanian A., Ponnuraj K.
    J. Mol. Biol. 400:274-283(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH NICKEL IONS, CARBAMYLATION AT LYS-490.

Entry informationi

Entry nameiUREA_CANEN
AccessioniPrimary (citable) accession number: P07374
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1994
Last modified: November 11, 2015
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.