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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)DescriptionActionsGraphical viewLength
Metal bindingi407Nickel 1; via tele nitrogen1
Metal bindingi409Nickel 1; via tele nitrogen1
Metal bindingi490Nickel 1; via carbamate group1
Metal bindingi490Nickel 2; via carbamate group1
Binding sitei492SubstrateBy similarity1
Metal bindingi519Nickel 2; via pros nitrogen1
Metal bindingi545Nickel 2; via tele nitrogen1
Active sitei593Proton donorBy similarity1
Metal bindingi633Nickel 11

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 databases

ChEMBLiCHEMBL4161.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000675241 – 840UreaseAdd BLAST840

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei490N6-carboxylysine1 Publication1

Post-translational modificationi

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

Interactioni

Subunit structurei

Homohexamer.By similarity

Chemistry databases

BindingDBiP07374.

Structurei

Secondary structure

1840
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 25Combined sources21
Helixi32 – 49Combined sources18
Helixi54 – 60Combined sources7
Helixi61 – 63Combined sources3
Helixi67 – 69Combined sources3
Helixi74 – 77Combined sources4
Beta strandi79 – 87Combined sources9
Beta strandi90 – 98Combined sources9
Beta strandi102 – 104Combined sources3
Helixi107 – 110Combined sources4
Turni111 – 113Combined sources3
Helixi121 – 123Combined sources3
Beta strandi143 – 145Combined sources3
Beta strandi151 – 159Combined sources9
Beta strandi165 – 168Combined sources4
Helixi173 – 175Combined sources3
Beta strandi180 – 182Combined sources3
Helixi184 – 187Combined sources4
Beta strandi190 – 192Combined sources3
Beta strandi199 – 202Combined sources4
Beta strandi207 – 214Combined sources8
Beta strandi226 – 228Combined sources3
Beta strandi230 – 233Combined sources4
Helixi234 – 247Combined sources14
Beta strandi259 – 261Combined sources3
Beta strandi273 – 275Combined sources3
Helixi276 – 283Combined sources8
Beta strandi290 – 292Combined sources3
Beta strandi299 – 301Combined sources3
Beta strandi319 – 323Combined sources5
Turni324 – 326Combined sources3
Beta strandi329 – 331Combined sources3
Helixi333 – 335Combined sources3
Beta strandi338 – 348Combined sources11
Beta strandi351 – 360Combined sources10
Beta strandi363 – 368Combined sources6
Turni373 – 375Combined sources3
Beta strandi390 – 393Combined sources4
Beta strandi398 – 401Combined sources4
Beta strandi403 – 409Combined sources7
Helixi414 – 421Combined sources8
Beta strandi424 – 430Combined sources7
Beta strandi432 – 434Combined sources3
Helixi436 – 440Combined sources5
Helixi447 – 456Combined sources10
Turni457 – 459Combined sources3
Beta strandi460 – 469Combined sources10
Beta strandi473 – 475Combined sources3
Helixi476 – 484Combined sources9
Beta strandi487 – 492Combined sources6
Turni493 – 495Combined sources3
Helixi499 – 512Combined sources14
Beta strandi515 – 519Combined sources5
Helixi529 – 536Combined sources8
Beta strandi541 – 543Combined sources3
Turni544 – 547Combined sources4
Turni554 – 556Combined sources3
Helixi557 – 562Combined sources6
Beta strandi566 – 572Combined sources7
Helixi581 – 592Combined sources12
Helixi600 – 609Combined sources10
Helixi612 – 623Combined sources12
Beta strandi629 – 631Combined sources3
Turni635 – 637Combined sources3
Helixi640 – 642Combined sources3
Helixi643 – 658Combined sources16
Helixi670 – 678Combined sources9
Turni679 – 681Combined sources3
Helixi682 – 688Combined sources7
Turni691 – 693Combined sources3
Beta strandi694 – 697Combined sources4
Beta strandi705 – 708Combined sources4
Helixi710 – 712Combined sources3
Turni713 – 715Combined sources3
Beta strandi718 – 722Combined sources5
Beta strandi725 – 731Combined sources7
Beta strandi736 – 739Combined sources4
Beta strandi745 – 748Combined sources4
Helixi750 – 752Combined sources3
Helixi756 – 759Combined sources4
Beta strandi762 – 765Combined sources4
Helixi767 – 771Combined sources5
Helixi774 – 778Combined sources5
Beta strandi782 – 786Combined sources5
Helixi795 – 797Combined sources3
Beta strandi807 – 809Combined sources3
Turni811 – 813Combined sources3
Beta strandi816 – 818Combined sources3
Beta strandi832 – 834Combined sources3
Turni835 – 837Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP07374.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini402 – 840UreaseAdd BLAST439

Sequence similaritiesi

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

Family and domain databases

CDDicd00375. Urease_alpha. 1 hit.
cd00407. Urease_beta. 1 hit.
cd00390. Urease_gamma. 1 hit.
Gene3Di2.10.150.10. 1 hit.
2.30.40.10. 1 hit.
3.30.280.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti247K → R AA sequence (PubMed:3402446).Curated1
Sequence conflicti247K → R AA sequence (Ref. 3) Curated1
Sequence conflicti258S → P AA sequence (PubMed:3402446).Curated1
Sequence conflicti258S → P AA sequence (Ref. 3) Curated1
Sequence conflicti269P → S AA sequence (PubMed:3402446).Curated1
Sequence conflicti269P → S AA sequence (Ref. 3) Curated1
Sequence conflicti459D → Y in AAA83831 (PubMed:1721034).Curated1
Sequence conflicti653K → P in AAA83831 (PubMed:1721034).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LA4X-ray2.05A1-840[»]
4GOAX-ray2.20A1-840[»]
4GY7X-ray1.49A1-840[»]
4H9MX-ray1.52A1-840[»]
ProteinModelPortaliP07374.
SMRiP07374.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

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

CDDicd00375. Urease_alpha. 1 hit.
cd00407. Urease_beta. 1 hit.
cd00390. Urease_gamma. 1 hit.
Gene3Di2.10.150.10. 1 hit.
2.30.40.10. 1 hit.
3.30.280.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
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...

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 2, 2016
This is version 121 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.