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P18314

- URE1_ENTAE

UniProt

P18314 - URE1_ENTAE

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Protein
Urease subunit alpha
Gene
ureC
Organism
Enterobacter aerogenes (Aerobacter aerogenes)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.9 Publications

Cofactori

Binds 2 nickel ions per subunit.3 Publications

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 enzyme

pH dependencei

Optimum pH is 7.75.

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
Complete GO annotation...

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

SABIO-RKP18314.
UniPathwayiUPA00258; UER00370.

Protein family/group databases

MEROPSiM38.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Urease subunit alpha (EC:3.5.1.5)
Alternative name(s):
Urea amidohydrolase subunit alpha
Gene namesi
Name:ureC
OrganismiEnterobacter aerogenes (Aerobacter aerogenes)
Taxonomic identifieri548 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

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

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 alphaUniRule annotation
PRO_0000067543Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two nickel ions.UniRule 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.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

IntActiP18314. 3 interactions.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP18314.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 567439Urease
Add
BLAST

Sequence similaritiesi

Belongs to the urease family.
Contains 1 urease domain.

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...

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: September 3, 2014
This is version 125 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

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