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P18314

- URE1_ENTAE

UniProt

P18314 - URE1_ENTAE

Protein

Urease subunit alpha

Gene

ureC

Organism
Enterobacter aerogenes (Aerobacter aerogenes)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Urea + H2O = CO2 + 2 NH3.9 PublicationsUniRule annotation

    Cofactori

    Binds 2 nickel ions per subunit.3 PublicationsUniRule annotation

    Enzyme regulationi

    The apoenzyme can be activated in vitro in the presence of nickel ions and carbon dioxide, which promotes carbamylation of Lys-217.4 Publications

    Kineticsi

    1. KM=2.3 mM for urea4 Publications

    Vmax=1.9 mmol/min/mg enzyme4 Publications

    pH dependencei

    Optimum pH is 7.75.4 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi134 – 1341Nickel 1; via tele nitrogen
    Metal bindingi136 – 1361Nickel 1; via tele nitrogen
    Metal bindingi217 – 2171Nickel 1; via carbamate group
    Metal bindingi217 – 2171Nickel 2; via carbamate group
    Binding sitei219 – 2191Substrate
    Metal bindingi246 – 2461Nickel 2; via pros nitrogen
    Metal bindingi272 – 2721Nickel 2; via tele nitrogen
    Active sitei320 – 3201Proton donor
    Metal bindingi360 – 3601Nickel 1

    GO - Molecular functioni

    1. nickel cation binding Source: UniProtKB-HAMAP
    2. protein binding Source: IntAct
    3. 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

    SABIO-RKP18314.
    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
    OrganismiEnterobacter aerogenes (Aerobacter aerogenes)
    Taxonomic identifieri548 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi134 – 1341H → A: Abrogates activity and reduces binding to nickel ions. 1 Publication
    Mutagenesisi136 – 1361H → A: Abrogates activity and reduces binding to nickel ions. 1 Publication
    Mutagenesisi217 – 2171K → A, C or E: Reduces activity 8000-fold and abrogates binding to nickel ions. 1 Publication
    Mutagenesisi219 – 2191H → A: Reduces activity 500-fold and increases KM 1000-fold. Resistant to inactivation by diethylpyrocarbonate and iodoacetamide. 2 Publications
    Mutagenesisi219 – 2191H → N or Q: Increases KM 100-fold; optimum pH is 6. 2 Publications
    Mutagenesisi221 – 2211D → A: Reduces activity 1000-fold and increases KM 10-fold. 1 Publication
    Mutagenesisi221 – 2211D → N: Reduces activity 50-fold. 1 Publication
    Mutagenesisi246 – 2461H → A: Abrogates activity and reduces binding to nickel ions. 1 Publication
    Mutagenesisi312 – 3121H → A: Enhances thermal stability above 50 degrees Celsius.
    Mutagenesisi319 – 3191C → A: Reduces activity 2-fold, but increases KM only 1.7-fold; optimum pH is 6.7. Reduces binding of nickel ions. Resistant to inactivation by iodoacetamide. 2 Publications
    Mutagenesisi319 – 3191C → D: Reduces activity 20-fold, but increases KM only 1.9-fold; optimum pH is 5.2. Reduces binding of nickel ions. Resistant to inactivation by iodoacetamide. 2 Publications
    Mutagenesisi319 – 3191C → S: Reduces activity 3000-fold, but increases KM only 3.9-fold; optimum pH is 5.2. Reduces binding of nickel ions. Resistant to inactivation by iodoacetamide. 2 Publications
    Mutagenesisi319 – 3191C → Y: Abrogates activity. 2 Publications
    Mutagenesisi320 – 3201H → A: Reduces activity 100000-fold, but increases KM only 3-fold; optimum pH is 6.75. Resistant to inactivation by diethylpyrocarbonate and iodoacetamide. 2 Publications
    Mutagenesisi320 – 3201H → N or Q: Reduces activity 100000-fold, but increases KM only 3-fold. 2 Publications
    Mutagenesisi336 – 3361R → Q: Reduces activity 10000-fold, but has no effect on KM. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 567567Urease subunit alphaPRO_0000067543Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei217 – 2171N6-carboxylysine4 PublicationsUniRule annotation

    Post-translational modificationi

    Carbamylation allows a single lysine to coordinate two nickel ions.4 PublicationsUniRule annotation

    Interactioni

    Subunit structurei

    Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme. The apoenzyme interacts with an accessory complex composed of UreD, UreF and UreG, which is required for the assembly of the nickel containing metallocenter of UreC. The UreE protein may also play a direct role as a metallochaperone in nickel transfer to the urease apoprotein.12 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ureAP1831611EBI-1028571,EBI-1028581

    Protein-protein interaction databases

    IntActiP18314. 3 interactions.

    Structurei

    Secondary structure

    1
    567
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Helixi6 – 138
    Beta strandi20 – 223
    Beta strandi29 – 313
    Beta strandi50 – 534
    Turni54 – 563
    Helixi62 – 643
    Beta strandi67 – 7711
    Beta strandi80 – 8910
    Beta strandi92 – 976
    Turni102 – 1043
    Beta strandi105 – 1073
    Beta strandi109 – 1113
    Beta strandi117 – 1204
    Beta strandi125 – 1284
    Beta strandi130 – 1367
    Helixi142 – 1498
    Beta strandi151 – 1577
    Beta strandi159 – 1624
    Helixi163 – 1675
    Helixi173 – 18412
    Beta strandi187 – 19610
    Helixi202 – 21110
    Beta strandi214 – 2196
    Helixi220 – 2223
    Helixi226 – 23914
    Beta strandi242 – 2465
    Helixi256 – 2638
    Beta strandi268 – 2703
    Turni271 – 2744
    Beta strandi278 – 2803
    Turni281 – 2833
    Helixi284 – 2896
    Beta strandi293 – 2975
    Helixi299 – 3013
    Beta strandi305 – 3073
    Helixi308 – 32013
    Beta strandi324 – 3263
    Helixi327 – 33610
    Helixi339 – 35012
    Beta strandi356 – 3583
    Beta strandi363 – 3653
    Helixi370 – 38516
    Beta strandi393 – 3953
    Helixi397 – 4048
    Helixi405 – 4073
    Helixi409 – 4146
    Turni418 – 4203
    Beta strandi421 – 4244
    Beta strandi432 – 4354
    Helixi437 – 4393
    Turni440 – 4423
    Beta strandi445 – 4495
    Beta strandi452 – 4587
    Beta strandi463 – 4664
    Beta strandi472 – 4754
    Helixi477 – 4793
    Helixi481 – 4877
    Beta strandi489 – 4924
    Helixi494 – 4985
    Helixi501 – 5044
    Beta strandi509 – 5135
    Turni517 – 5193
    Helixi522 – 5243
    Beta strandi534 – 5363
    Turni538 – 5403
    Beta strandi543 – 5453
    Beta strandi548 – 5503
    Beta strandi555 – 5573
    Beta strandi559 – 5613
    Turni562 – 5643

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A5KX-ray2.20C2-567[»]
    1A5LX-ray2.20C2-567[»]
    1A5MX-ray2.00C2-567[»]
    1A5NX-ray2.40C2-567[»]
    1A5OX-ray2.50C2-567[»]
    1EF2X-ray2.50A2-567[»]
    1EJRX-ray2.00C1-567[»]
    1EJSX-ray2.00C1-567[»]
    1EJTX-ray2.00C1-567[»]
    1EJUX-ray2.00C1-567[»]
    1EJVX-ray2.40C1-567[»]
    1EJWX-ray1.90C1-567[»]
    1EJXX-ray1.60C1-567[»]
    1FWAX-ray2.00C1-567[»]
    1FWBX-ray2.00C1-567[»]
    1FWCX-ray2.00C1-567[»]
    1FWDX-ray2.00C1-567[»]
    1FWEX-ray2.00C1-567[»]
    1FWFX-ray2.00C1-567[»]
    1FWGX-ray2.00C1-567[»]
    1FWHX-ray2.00C1-567[»]
    1FWIX-ray2.00C1-567[»]
    1FWJX-ray2.20C1-567[»]
    1KRAX-ray2.30C1-567[»]
    1KRBX-ray2.50C1-567[»]
    1KRCX-ray2.50C1-567[»]
    2KAUX-ray2.00C1-567[»]
    4EP8X-ray1.55C2-567[»]
    4EPBX-ray1.75C2-567[»]
    4EPDX-ray1.70C2-567[»]
    4EPEX-ray2.05C2-567[»]
    ProteinModelPortaliP18314.
    SMRiP18314. Positions 2-567.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18314.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini129 – 567439UreaseUniRule 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.

    P18314-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNISRQAYA DMFGPTVGDK VRLADTELWI EVEDDLTTYG EEVKFGGGKV    50
    IRDGMGQGQM LAADCVDLVL TNALIVDHWG IVKADIGVKD GRIFAIGKAG 100
    NPDIQPNVTI PIGAATEVIA AEGKIVTAGG IDTHIHWICP QQAEEALVSG 150
    VTTMVGGGTG PAAGTHATTC TPGPWYISRM LQAADSLPVN IGLLGKGNVS 200
    QPDALREQVA AGVIGLKIHE DWGATPAAID CALTVADEMD IQVALHSDTL 250
    NESGFVEDTL AAIGGRTIHT FHTEGAGGGH APDIITACAH PNILPSSTNP 300
    TLPYTLNTID EHLDMLMVCH HLDPDIAEDV AFAESRIRRE TIAAEDVLHD 350
    LGAFSLTSSD SQAMGRVGEV ILRTWQVAHR MKVQRGALAE ETGDNDNFRV 400
    KRYIAKYTIN PALTHGIAHE VGSIEVGKLA DLVVWSPAFF GVKPATVIKG 450
    GMIAIAPMGD INASIPTPQP VHYRPMFGAL GSARHHCRLT FLSQAAAANG 500
    VAERLNLRSA IAVVKGCRTV QKADMVHNSL QPNITVDAQT YEVRVDGELI 550
    TSEPADVLPM AQRYFLF 567
    Length:567
    Mass (Da):60,305
    Last modified:November 1, 1990 - v1
    Checksum:i2ECF3C4268A2E2C7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36068 Genomic DNA. Translation: AAA25151.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36068 Genomic DNA. Translation: AAA25151.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A5K X-ray 2.20 C 2-567 [» ]
    1A5L X-ray 2.20 C 2-567 [» ]
    1A5M X-ray 2.00 C 2-567 [» ]
    1A5N X-ray 2.40 C 2-567 [» ]
    1A5O X-ray 2.50 C 2-567 [» ]
    1EF2 X-ray 2.50 A 2-567 [» ]
    1EJR X-ray 2.00 C 1-567 [» ]
    1EJS X-ray 2.00 C 1-567 [» ]
    1EJT X-ray 2.00 C 1-567 [» ]
    1EJU X-ray 2.00 C 1-567 [» ]
    1EJV X-ray 2.40 C 1-567 [» ]
    1EJW X-ray 1.90 C 1-567 [» ]
    1EJX X-ray 1.60 C 1-567 [» ]
    1FWA X-ray 2.00 C 1-567 [» ]
    1FWB X-ray 2.00 C 1-567 [» ]
    1FWC X-ray 2.00 C 1-567 [» ]
    1FWD X-ray 2.00 C 1-567 [» ]
    1FWE X-ray 2.00 C 1-567 [» ]
    1FWF X-ray 2.00 C 1-567 [» ]
    1FWG X-ray 2.00 C 1-567 [» ]
    1FWH X-ray 2.00 C 1-567 [» ]
    1FWI X-ray 2.00 C 1-567 [» ]
    1FWJ X-ray 2.20 C 1-567 [» ]
    1KRA X-ray 2.30 C 1-567 [» ]
    1KRB X-ray 2.50 C 1-567 [» ]
    1KRC X-ray 2.50 C 1-567 [» ]
    2KAU X-ray 2.00 C 1-567 [» ]
    4EP8 X-ray 1.55 C 2-567 [» ]
    4EPB X-ray 1.75 C 2-567 [» ]
    4EPD X-ray 1.70 C 2-567 [» ]
    4EPE X-ray 2.05 C 2-567 [» ]
    ProteinModelPortali P18314.
    SMRi P18314. Positions 2-567.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P18314. 3 interactions.

    Chemistry

    DrugBanki DB00551. Acetohydroxamic Acid.

    Protein family/group databases

    MEROPSi M38.982.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00258 ; UER00370 .
    SABIO-RK P18314.

    Miscellaneous databases

    EvolutionaryTracei P18314.

    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. "Sequence of the Klebsiella aerogenes urease genes and evidence for accessory proteins facilitating nickel incorporation."
      Mulrooney S.B., Hausinger R.P.
      J. Bacteriol. 172:5837-5843(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY.
      Strain: CG253.
    2. "Klebsiella aerogenes urease gene cluster: sequence of ureD and demonstration that four accessory genes (ureD, ureE, ureF, and ureG) are involved in nickel metallocenter biosynthesis."
      Lee M.H., Mulrooney S.B., Renner M.J., Markowicz Y., Hausinger R.P.
      J. Bacteriol. 174:4324-4330(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    3. "Site-directed mutagenesis of the active site cysteine in Klebsiella aerogenes urease."
      Martin P.R., Hausinger R.P.
      J. Biol. Chem. 267:20024-20027(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-319.
    4. "Site-directed mutagenesis of Klebsiella aerogenes urease: identification of histidine residues that appear to function in nickel ligation, substrate binding, and catalysis."
      Park I.-S., Hausinger R.P.
      Protein Sci. 2:1034-1041(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-134; HIS-136; HIS-219; HIS-246; HIS-320 AND HIS-320.
    5. "In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly."
      Park I.-S., Carr M.B., Hausinger R.P.
      Proc. Natl. Acad. Sci. U.S.A. 91:3233-3237(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREA; UREB AND URED.
    6. "Evidence for the presence of urease apoprotein complexes containing UreD, UreF, and UreG in cells that are competent for in vivo enzyme activation."
      Park I.-S., Hausinger R.P.
      J. Bacteriol. 177:1947-1951(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREA; UREB; URED; UREF AND UREG.
    7. "Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter."
      Park I.-S., Hausinger R.P.
      Science 267:1156-1158(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
    8. "Purification and activation properties of UreD-UreF-urease apoprotein complexes."
      Moncrief M.B.C., Hausinger R.P.
      J. Bacteriol. 178:5417-5421(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREA; UREB; URED AND UREF.
    9. "GTP-dependent activation of urease apoprotein in complex with the UreD, UreF, and UreG accessory proteins."
      Soriano A., Hausinger R.P.
      Proc. Natl. Acad. Sci. U.S.A. 96:11140-11144(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREA; UREB; URED; UREF AND UREG.
    10. "UreE stimulation of GTP-dependent urease activation in the UreD-UreF-UreG-urease apoprotein complex."
      Soriano A., Colpas G.J., Hausinger R.P.
      Biochemistry 39:12435-12440(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, ACTIVATION OF THE APOPROTEIN BY UREE.
    11. "Dual effects of ionic strength on Klebsiella aerogenes urease: pH-dependent activation and inhibition."
      Mulrooney S.B., Zakharian T., Schaller R.A., Hausinger R.P.
      Arch. Biochem. Biophys. 394:280-282(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    12. "Chemical cross-linking and mass spectrometric identification of sites of interaction for UreD, UreF, and urease."
      Chang Z., Kuchar J., Hausinger R.P.
      J. Biol. Chem. 279:15305-15313(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UREA; UREB; URED AND UREF, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "The crystal structure of urease from Klebsiella aerogenes."
      Jabri E., Carr M.B., Hausinger R.P., Karplus P.A.
      Science 268:998-1004(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UREA; UREB AND NICKEL IONS, CARBAMYLATION AT LYS-217.
    14. "Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants."
      Jabri E., Karplus P.A.
      Biochemistry 35:10616-10626(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-219 AND ALA-320 IN COMPLEX WITH UREA; UREB AND NICKEL IONS, CARBAMYLATION AT LYS-217.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ALA-134 IN COMPLEX WITH UREA; UREB AND NICKEL IONS, MAGNETIC CIRCULAR DICHROISM, ABSORPTION SPECTROSCOPY, CARBAMYLATION AT LYS-217.
    16. "Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease."
      Pearson M.A., Michel L.O., Hausinger R.P., Karplus P.A.
      Biochemistry 36:8164-8172(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA/ASP/SER/TYR-319 IN COMPLEX WITH UREA; UREB; NICKEL IONS AND ACETOHYDROXAMIC ACID.
    17. "Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand."
      Pearson M.A., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P.
      Biochemistry 37:6214-6220(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA/CYS/GLU-217 IN COMPLEX WITH UREA; UREB AND FORMATE, MUTAGENESIS OF LYS-217.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH UREA; UREB AND MANGANESE IONS, ABSORPTION SPECTROSCOPY, MUTAGENESIS OF CYS-319.
    19. "Kinetic and structural characterization of urease active site variants."
      Pearson M.A., Park I.-S., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P.
      Biochemistry 39:8575-8584(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF WILD-TYPE AND MUTANTS ASN/GLN-219; ALA-221 AND ASN/GLN-320 IN COMPLEX WITH UREA; UREB AND NICKEL IONS, CARBAMYLATION AT LYS-217, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-219; ASP-221; HIS-320 AND ARG-336.

    Entry informationi

    Entry nameiURE1_ENTAE
    AccessioniPrimary (citable) accession number: P18314
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 126 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