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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.

Pathwayi: 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 gamma (ureA), Urease subunit beta (ureB), Urease subunit alpha (ureC), Urease (ureC), Urease subunit beta (ureB), Urease subunit alpha (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)DescriptionActionsGraphical viewLength
Metal bindingi136Nickel 1; via tele nitrogenUniRule annotation2 Publications1
Metal bindingi138Nickel 1; via tele nitrogenUniRule annotation2 Publications1
Metal bindingi219Nickel 1; via carbamate groupUniRule annotation2 Publications1
Metal bindingi219Nickel 2; via carbamate groupUniRule annotation2 Publications1
Binding sitei221SubstrateCurated1
Metal bindingi248Nickel 2; via pros nitrogenUniRule annotation2 Publications1
Metal bindingi274Nickel 2; via tele nitrogenUniRule annotation2 Publications1
Active sitei322Proton donorCurated1
Metal bindingi362Nickel 1UniRule annotation2 Publications1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000675361 – 569Urease subunit alphaAdd BLAST569

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei219N6-carboxylysineUniRule annotation5 Publications1

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

Chemistry databases

BindingDBiP41020.

Structurei

Secondary structure

1569
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Helixi5 – 12Combined sources8
Beta strandi19 – 21Combined sources3
Beta strandi47 – 51Combined sources5
Turni52 – 54Combined sources3
Turni61 – 64Combined sources4
Beta strandi67 – 77Combined sources11
Beta strandi80 – 89Combined sources10
Beta strandi92 – 97Combined sources6
Turni102 – 104Combined sources3
Beta strandi119 – 122Combined sources4
Beta strandi127 – 130Combined sources4
Beta strandi132 – 138Combined sources7
Helixi144 – 150Combined sources7
Beta strandi153 – 159Combined sources7
Beta strandi161 – 163Combined sources3
Helixi165 – 169Combined sources5
Helixi175 – 186Combined sources12
Beta strandi190 – 198Combined sources9
Helixi204 – 213Combined sources10
Beta strandi217 – 221Combined sources5
Helixi222 – 224Combined sources3
Helixi228 – 241Combined sources14
Beta strandi244 – 248Combined sources5
Helixi258 – 265Combined sources8
Beta strandi270 – 272Combined sources3
Turni273 – 276Combined sources4
Beta strandi280 – 282Combined sources3
Turni283 – 285Combined sources3
Helixi286 – 291Combined sources6
Beta strandi295 – 298Combined sources4
Helixi301 – 303Combined sources3
Helixi310 – 321Combined sources12
Helixi329 – 338Combined sources10
Helixi341 – 352Combined sources12
Beta strandi365 – 367Combined sources3
Helixi372 – 387Combined sources16
Helixi399 – 409Combined sources11
Helixi411 – 416Combined sources6
Turni420 – 422Combined sources3
Beta strandi423 – 425Combined sources3
Beta strandi434 – 437Combined sources4
Helixi439 – 441Combined sources3
Turni442 – 444Combined sources3
Beta strandi447 – 451Combined sources5
Beta strandi454 – 460Combined sources7
Beta strandi465 – 468Combined sources4
Beta strandi474 – 477Combined sources4
Helixi479 – 481Combined sources3
Helixi485 – 488Combined sources4
Beta strandi491 – 494Combined sources4
Helixi496 – 500Combined sources5
Helixi503 – 507Combined sources5
Beta strandi511 – 515Combined sources5
Helixi524 – 526Combined sources3
Beta strandi536 – 538Combined sources3
Turni540 – 542Combined sources3
Beta strandi545 – 547Combined sources3
Beta strandi550 – 552Combined sources3
Beta strandi561 – 563Combined sources3
Turni564 – 566Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5A6TX-ray1.65C1-569[»]
5FSDX-ray1.75C1-569[»]
5FSEX-ray2.07C1-569[»]
ProteinModelPortaliP41020.
SMRiP41020.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41020.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini131 – 569UreaseUniRule annotationAdd BLAST439

Sequence similaritiesi

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

Family and domain databases

CDDicd00375. Urease_alpha. 1 hit.
Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
InterProiIPR006680. Amidohydro-rel.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
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.
SSF51556. SSF51556. 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)DescriptionActionsGraphical viewLength
Sequence conflicti497 – 501SSIQQ → ELNSE (Ref. 2) Curated5

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
PDB 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[»]
5A6TX-ray1.65C1-569[»]
5FSDX-ray1.75C1-569[»]
5FSEX-ray2.07C1-569[»]
ProteinModelPortaliP41020.
SMRiP41020.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

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

CDDicd00375. Urease_alpha. 1 hit.
Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
InterProiIPR006680. Amidohydro-rel.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
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.
SSF51556. SSF51556. 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...

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: November 2, 2016
This is version 115 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

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.