Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P41020

- URE1_SPOPA

UniProt

P41020 - URE1_SPOPA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Urease subunit alpha

Gene

ureC

Organism
Sporosarcina pasteurii (Bacillus pasteurii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.UniRule annotation

Cofactori

Binds 2 nickel ions per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi136 – 1361Nickel 1; via tele nitrogen2 PublicationsUniRule annotation
Metal bindingi138 – 1381Nickel 1; via tele nitrogen2 PublicationsUniRule annotation
Metal bindingi219 – 2191Nickel 1; via carbamate group2 PublicationsUniRule annotation
Metal bindingi219 – 2191Nickel 2; via carbamate group2 PublicationsUniRule annotation
Binding sitei221 – 2211SubstrateCurated
Metal bindingi248 – 2481Nickel 2; via pros nitrogen2 PublicationsUniRule annotation
Metal bindingi274 – 2741Nickel 2; via tele nitrogen2 PublicationsUniRule annotation
Active sitei322 – 3221Proton donorCurated
Metal bindingi362 – 3621Nickel 12 PublicationsUniRule annotation

GO - Molecular functioni

  1. nickel cation binding Source: UniProtKB-HAMAP
  2. urease activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. urea catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.

Protein family/group databases

MEROPSiM38.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Urease subunit alphaUniRule annotation (EC:3.5.1.5UniRule annotation)
Alternative name(s):
Urea amidohydrolase subunit alphaUniRule annotation
Gene namesi
Name:ureCUniRule annotation
OrganismiSporosarcina pasteurii (Bacillus pasteurii)
Taxonomic identifieri1474 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPlanococcaceaeSporosarcina

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 569569Urease subunit alphaPRO_0000067536Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191N6-carboxylysine5 PublicationsUniRule annotation

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two nickel ions.5 PublicationsUniRule annotation

Interactioni

Subunit structurei

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.5 PublicationsUniRule annotation

Structurei

Secondary structure

1
569
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43
Helixi5 – 128
Beta strandi19 – 213
Beta strandi47 – 515
Turni52 – 543
Turni61 – 644
Beta strandi67 – 7711
Beta strandi80 – 8910
Beta strandi92 – 976
Turni102 – 1043
Beta strandi119 – 1224
Beta strandi127 – 1304
Beta strandi132 – 1387
Helixi144 – 1507
Beta strandi153 – 1597
Beta strandi161 – 1633
Helixi165 – 1695
Helixi175 – 18612
Beta strandi190 – 1989
Helixi204 – 21310
Beta strandi217 – 2215
Helixi222 – 2243
Helixi228 – 24114
Beta strandi244 – 2485
Helixi258 – 2658
Beta strandi270 – 2723
Turni273 – 2764
Beta strandi280 – 2823
Turni283 – 2853
Helixi286 – 2916
Beta strandi295 – 2984
Helixi301 – 3033
Helixi310 – 32112
Helixi329 – 33810
Helixi341 – 35212
Beta strandi365 – 3673
Helixi372 – 38716
Helixi399 – 40911
Helixi411 – 4166
Turni420 – 4223
Beta strandi423 – 4253
Beta strandi434 – 4374
Helixi439 – 4413
Turni442 – 4443
Beta strandi447 – 4515
Beta strandi454 – 4607
Beta strandi465 – 4684
Beta strandi474 – 4774
Helixi479 – 4813
Helixi485 – 4884
Beta strandi491 – 4944
Helixi496 – 5005
Helixi503 – 5075
Beta strandi511 – 5155
Helixi524 – 5263
Beta strandi536 – 5383
Turni540 – 5423
Beta strandi545 – 5473
Beta strandi561 – 5633
Turni564 – 5663

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IE7X-ray1.85C1-569[»]
1S3TX-ray2.10C1-569[»]
1UBPX-ray1.65C1-569[»]
2UBPX-ray2.00C1-569[»]
3UBPX-ray2.00C1-569[»]
4AC7X-ray1.50C1-569[»]
4CEUX-ray1.58C1-569[»]
4CEXX-ray1.59C1-569[»]
4UBPX-ray1.55C1-569[»]
ProteinModelPortaliP41020.
SMRiP41020. Positions 1-569.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41020.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini131 – 569439UreaseUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the urease family.UniRule annotation
Contains 1 urease domain.UniRule annotation

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01953. Urease_alpha.
InterProiIPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
IPR011612. Urease_alpha_N_dom.
IPR017950. Urease_AS.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR029754. Urease_Ni-bd.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSiPR01752. UREASE.
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR01792. urease_alph. 1 hit.
PROSITEiPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41020-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKINRQQYAE SYGPTVGDRV RLADTDLGEV EKDYYYLGDE VNFGGGKVLR
60 70 80 90 100
EGMGENGTYT RTENVLDLLL TNALILDYTG IYKADIGVKD GYIVGIGKGG
110 120 130 140 150
NPDIMDGVTP NMIVGTATEV IAAEGKIVTA GGIDTHVHFI NPDQVDVALA
160 170 180 190 200
NGITTLFGGG TGPAEGSKAT TVTPGPWNIE KMLKSTEGLP INVGILGKGH
210 220 230 240 250
GSSIAPIMEQ IDAGAAGLKI HEDWGATPAS IDRSLTVADE ADVQVAIHSD
260 270 280 290 300
TLNEAGFLED TVRAINGRVI HSFHVEGAGG GHAPDIMAMA GHPNVLPSST
310 320 330 340 350
NPTRPFTVNT IDEHLDMLMV CHHLKQNIPE DVAFADSRIR PETIAAEDIL
360 370 380 390 400
HDLGIISMMS TDALAMGRAG EMVLRTWQTA DKMKKQRGPL AEEKNGSDNF
410 420 430 440 450
RLKRYVSKYT INPAIAQGMA HEVGSIEEGK FADLVLWEPK FFGVKADRVI
460 470 480 490 500
KGGIIAYAQI GDPSASIPTP QPVMGRRMYG TVGDLIHDTN ITFMSKSSIQ
510 520 530 540 550
QGVPAKLGLK RRIGTVKNCR NIGKKDMKWN DVTTDIDINP ETYEVKVDGE
560
VLTCEPVKEL PMAQRYFLF
Length:569
Mass (Da):61,398
Last modified:February 1, 1995 - v1
Checksum:iEC55A5C4293F2E5C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti497 – 5015SSIQQ → ELNSE1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78411 Genomic DNA. Translation: CAA55175.1.
U29368 Genomic DNA. Translation: AAA73986.1.
PIRiS47104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78411 Genomic DNA. Translation: CAA55175.1 .
U29368 Genomic DNA. Translation: AAA73986.1 .
PIRi S47104.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IE7 X-ray 1.85 C 1-569 [» ]
1S3T X-ray 2.10 C 1-569 [» ]
1UBP X-ray 1.65 C 1-569 [» ]
2UBP X-ray 2.00 C 1-569 [» ]
3UBP X-ray 2.00 C 1-569 [» ]
4AC7 X-ray 1.50 C 1-569 [» ]
4CEU X-ray 1.58 C 1-569 [» ]
4CEX X-ray 1.59 C 1-569 [» ]
4UBP X-ray 1.55 C 1-569 [» ]
ProteinModelPortali P41020.
SMRi P41020. Positions 1-569.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P41020.

Protein family/group databases

MEROPSi M38.982.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00258 ; UER00370 .

Miscellaneous databases

EvolutionaryTracei P41020.

Family and domain databases

Gene3Di 2.30.40.10. 1 hit.
HAMAPi MF_01953. Urease_alpha.
InterProi IPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
IPR011612. Urease_alpha_N_dom.
IPR017950. Urease_AS.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR029754. Urease_Ni-bd.
[Graphical view ]
Pfami PF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view ]
PRINTSi PR01752. UREASE.
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR01792. urease_alph. 1 hit.
PROSITEi PS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of three genes on a urease encoding DNA-fragment from Bacillus pasteurii."
    Moersdorf G., Weinmann P., Kaltwasser H.
    Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
  2. "Genetic organization and nucleotide sequence of the ure gene cluster in Bacillus pasteurii."
    You J.-H., Kim J.-G., Song B.-H., Lee M.-H., Kim S.-D.
    Mol. Cells 5:359-369(1995)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 497-569.
    Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
  3. "Crystallization and preliminary high-resolution X-ray diffraction analysis of native and beta-mercaptoethanol-inhibited urease from Bacillus pasteurii."
    Benini S., Ciurli S., Rypniewski W.R., Wilson K.S., Mangani S.
    Acta Crystallogr. D 54:409-412(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL IONS AND BETA-MERCAPTOETHANOL, CARBAMYLATION AT LYS-219.
  4. "A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels."
    Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.
    Structure 7:205-216(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL IONS AND DIAMIDOPHOSPHATE, CARBAMYLATION AT LYS-219.
  5. "The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution."
    Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.
    J. Biol. Inorg. Chem. 5:110-118(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL IONS AND ACETOHYDROXAMIC ACID, CARBAMYLATION AT LYS-219.
  6. "Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism."
    Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S.
    J. Biol. Inorg. Chem. 6:778-790(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL AND PHOSPHATE IONS, CARBAMYLATION AT LYS-219.
  7. "Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism."
    Benini S., Rypniewski W.R., Wilson K.S., Mangani S., Ciurli S.
    J. Am. Chem. Soc. 126:3714-3715(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UREA; UREB; NICKEL AND BORATE IONS, CARBAMYLATION AT LYS-219.

Entry informationi

Entry nameiURE1_SPOPA
AccessioniPrimary (citable) accession number: P41020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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

External Data

Dasty 3