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P41020

- URE1_SPOPA

UniProt

P41020 - URE1_SPOPA

Protein

Urease subunit alpha

Gene

ureC

Organism
Sporosarcina pasteurii (Bacillus pasteurii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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

    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-SubCell

    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[»]
    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.
    [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

    MKINRQQYAE SYGPTVGDRV RLADTDLGEV EKDYYYLGDE VNFGGGKVLR    50
    EGMGENGTYT RTENVLDLLL TNALILDYTG IYKADIGVKD GYIVGIGKGG 100
    NPDIMDGVTP NMIVGTATEV IAAEGKIVTA GGIDTHVHFI NPDQVDVALA 150
    NGITTLFGGG TGPAEGSKAT TVTPGPWNIE KMLKSTEGLP INVGILGKGH 200
    GSSIAPIMEQ IDAGAAGLKI HEDWGATPAS IDRSLTVADE ADVQVAIHSD 250
    TLNEAGFLED TVRAINGRVI HSFHVEGAGG GHAPDIMAMA GHPNVLPSST 300
    NPTRPFTVNT IDEHLDMLMV CHHLKQNIPE DVAFADSRIR PETIAAEDIL 350
    HDLGIISMMS TDALAMGRAG EMVLRTWQTA DKMKKQRGPL AEEKNGSDNF 400
    RLKRYVSKYT INPAIAQGMA HEVGSIEEGK FADLVLWEPK FFGVKADRVI 450
    KGGIIAYAQI GDPSASIPTP QPVMGRRMYG TVGDLIHDTN ITFMSKSSIQ 500
    QGVPAKLGLK RRIGTVKNCR NIGKKDMKWN DVTTDIDINP ETYEVKVDGE 550
    VLTCEPVKEL PMAQRYFLF 569
    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 [» ]
    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.
    [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 1, 2014
    This is version 103 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