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Protein

Urease subunit alpha

Gene

ureC

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

Functioni

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.UniRule annotation

Cofactori

Ni cationNote: Binds 2 nickel ions per subunit.

Pathway: urea degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and NH(3) from urea (urease route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Urease subunit gamma (ureA), Urease subunit beta (ureB), Urease subunit alpha (ureC), Urease (ureC)
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 bindingi136 – 1361Nickel 1; via tele nitrogenUniRule annotation2 Publications
Metal bindingi138 – 1381Nickel 1; via tele nitrogenUniRule annotation2 Publications
Metal bindingi219 – 2191Nickel 1; via carbamate groupUniRule annotation2 Publications
Metal bindingi219 – 2191Nickel 2; via carbamate groupUniRule annotation2 Publications
Binding sitei221 – 2211SubstrateCurated
Metal bindingi248 – 2481Nickel 2; via pros nitrogenUniRule annotation2 Publications
Metal bindingi274 – 2741Nickel 2; via tele nitrogenUniRule annotation2 Publications
Active sitei322 – 3221Proton donorCurated
Metal bindingi362 – 3621Nickel 1UniRule annotation2 Publications

GO - Molecular functioni

GO - Biological processi

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

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-carboxylysineUniRule annotation5 Publications

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two nickel ions.UniRule annotation5 Publications

Interactioni

Subunit structurei

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.UniRule annotation5 Publications

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 → ELNSE (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78411 Genomic DNA. Translation: CAA55175.1.
U29368 Genomic DNA. Translation: AAA73986.1.
PIRiS47104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78411 Genomic DNA. Translation: CAA55175.1.
U29368 Genomic DNA. Translation: AAA73986.1.
PIRiS47104.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Chemistry

BindingDBiP41020.

Protein family/group databases

MEROPSiM38.982.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.

Miscellaneous databases

EvolutionaryTraceiP41020.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 106 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

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 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.