Urease subunit alpha
Details
- Name
- Urease subunit alpha
- Synonyms
- 3.5.1.5
- Urea amidohydrolase subunit alpha
- Gene Name
- ureC
- Organism
- Sporosarcina pasteurii
- Amino acid sequence
>lcl|BSEQ0019506|Urease subunit alpha MKINRQQYAESYGPTVGDRVRLADTDLGEVEKDYYYLGDEVNFGGGKVLREGMGENGTYT RTENVLDLLLTNALILDYTGIYKADIGVKDGYIVGIGKGGNPDIMDGVTPNMIVGTATEV IAAEGKIVTAGGIDTHVHFINPDQVDVALANGITTLFGGGTGPAEGSKATTVTPGPWNIE KMLKSTEGLPINVGILGKGHGSSIAPIMEQIDAGAAGLKIHEDWGATPASIDRSLTVADE ADVQVAIHSDTLNEAGFLEDTVRAINGRVIHSFHVEGAGGGHAPDIMAMAGHPNVLPSST NPTRPFTVNTIDEHLDMLMVCHHLKQNIPEDVAFADSRIRPETIAAEDILHDLGIISMMS TDALAMGRAGEMVLRTWQTADKMKKQRGPLAEEKNGSDNFRLKRYVSKYTINPAIAQGMA HEVGSIEEGKFADLVLWEPKFFGVKADRVIKGGIIAYAQIGDPSASIPTPQPVMGRRMYG TVGDLIHDTNITFMSKSSIQQGVPAKLGLKRRIGTVKNCRNIGKKDMKWNDVTTDIDINP ETYEVKVDGEVLTCEPVKELPMAQRYFLF
- Number of residues
- 569
- Molecular Weight
- 61397.44
- Theoretical pI
- 5.1
- GO Classification
- Functionsnickel cation binding / urease activityProcessesurea catabolic processComponentscytoplasm
- General Function
- Urease activity
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0007662|303 bp ATGCATTTAAATCCAGCAGAGAAAGAAAAATTACAAATTTTTCTAGCGAGCGAATTACTC TTAAGGCGTAAAGCAAGAGGTCTTAAGTTGAACTATCCGGAAGCAGTTGCGATCATCACA AGTTTCATTATGGAGGGTGCGCGTGACGGAAAGACGGTAGCGATGCTAATGGAAGAAGGA AAACACGTTCTTACGAGGGACGATGTTATGGAAGGTGTACCAGAAATGATTGATGATATT CAAGCAGAAGCTACTTTCCCGGATGGAACTAAACTCGTAACTGTTCACAATCCAATTTCT TAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P41020 UniProtKB Entry Name URE1_SPOPA GenBank Protein ID 498709 GenBank Gene ID X78411 - General References
- Benini S, Ciurli S, Rypniewski WR, Wilson KS, Mangani S: Crystallization and preliminary high-resolution X-ray diffraction analysis of native and beta-mercaptoethanol-inhibited urease from Bacillus pasteurii. Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):409-12. [Article]
- Benini S, Rypniewski WR, Wilson KS, Miletti S, Ciurli S, Mangani S: 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. Structure. 1999 Feb 15;7(2):205-16. [Article]
- Benini S, Rypniewski WR, Wilson KS, Miletti S, Ciurli S, Mangani S: The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution. J Biol Inorg Chem. 2000 Feb;5(1):110-8. [Article]
- Benini S, Rypniewski WR, Wilson KS, Ciurli S, Mangani S: Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism. J Biol Inorg Chem. 2001 Oct;6(8):778-90. [Article]
- Benini S, Rypniewski WR, Wilson KS, Mangani S, Ciurli S: Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism. J Am Chem Soc. 2004 Mar 31;126(12):3714-5. [Article]