Aminopeptidase S
Details
- Name
- Aminopeptidase S
- Synonyms
- 3.4.11.24
- API
- SGAP
- Gene Name
- Not Available
- Organism
- Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
- Amino acid sequence
>lcl|BSEQ0016877|Aminopeptidase S MRPNRFSLRRSPTAVAAVALAAVLAAGAPAAQAAGAAAPTAAAAAAPDIPLANVKAHLTQ LSTIAANNGGNRAHGRPGYKASVDYVKAKLDAAGYTTTLQQFTSGGATGYNLIADWPGGD PNKVLMAGAHLDSVSSGAGINDNGSGSAAVLETALAVSRAGYQPDKHLRFAWWGAEELGL IGSKYYVNNLPSADRSKLAGYLNFDMIGSPNPGYFVYDDDPVIEKTFKDYFAGLNVPTEI ETEGDGRSDHAPFKNVGVPVGGLFTGAGYTKSAAQAQKWGGTAGQAFDRCYHSSCDSLSN INDTALDRNSDAAAHAIWTLSSGTGEPPTGEGVFSNTTDVAIPDAGAAVTSSVAVTGRTG NAPAALQVGVDIKHTYRGDLVVDLLAPDGTAYRLKNSSSGDSADNVIATYTVNASSEVAN GSWKLRVQDIARQDTGYIDSWKLTF
- Number of residues
- 445
- Molecular Weight
- 45939.31
- Theoretical pI
- 5.87
- GO Classification
- Functionsaminopeptidase activity / metal ion binding / serine-type endopeptidase activityComponentsextracellular region
- General Function
- Serine-type endopeptidase activity
- Specific Function
- An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0016878|Aminopeptidase S ATGAGACCGAACCGCTTCTCCCTGCGCAGATCCCCGACGGCCGTCGCCGCCGTGGCCCTC GCCGCCGTCCTCGCGGCCGGTGCCCCGGCCGCCCAGGCCGCCGGCGCCGCGGCCCCGACG GCAGCCGCCGCGGCCGCGCCCGACATCCCCCTGGCCAACGTCAAGGCCCACCTCACGCAG CTCTCGACGATCGCCGCGAACAACGGCGGCAACCGCGCCCACGGCCGCCCCGGCTACAAG GCGTCCGTCGACTACGTGAAGGCCAAGCTCGACGCGGCCGGATACACCACCACGCTCCAG CAGTTCACCTCGGGCGGGGCCACCGGCTACAACCTGATAGCCGACTGGCCCGGCGGCGAC CCCAACAAGGTCCTGATGGCCGGGGCCCACCTCGACTCGGTCTCCTCCGGCGCCGGGATC AACGACAACGGCTCCGGCTCGGCCGCCGTGCTGGAGACCGCGCTCGCCGTCTCCCGCGCC GGGTACCAGCCCGACAAGCACCTGCGGTTCGCCTGGTGGGGCGCGGAGGAGCTGGGCCTG ATCGGCTCGAAGTACTACGTCAACAACCTGCCGTCCGCCGACCGCTCCAAGCTCGCCGGA TATCTCAACTTCGACATGATCGGCTCGCCCAACCCCGGTTACTTCGTCTACGACGACGAC CCGGTCATCGAGAAGACCTTCAAGGACTACTTCGCCGGCCTGAACGTCCCGACCGAGATC GAGACCGAGGGCGACGGCCGCTCCGACCACGCCCCGTTCAAGAACGTCGGCGTCCCCGTC GGCGGACTCTTCACCGGCGCCGGCTACACCAAGTCCGCCGCCCAGGCGCAGAAGTGGGGC GGGACGGCCGGGCAGGCCTTCGACCGCTGCTACCACTCCTCGTGCGACAGCCTGAGCAAC ATCAACGACACCGCCCTGGACCGCAACAGCGACGCCGCCGCCCACGCGATCTGGACCCTG TCCTCCGGCACCGGCGAACCGCCCACCGGCGAGGGCGTCTTCAGCAACACCACGGACGTG GCCATCCCGGACGCCGGGGCCGCGGTCACCTCGTCGGTCGCCGTCACCGGACGCACGGGC AACGCCCCGGCCGCCCTCCAGGTCGGCGTCGACATCAAGCACACCTACCGCGGCGACCTC GTCGTGGACCTGCTCGCCCCGGACGGCACCGCGTACCGGCTGAAGAACTCCAGCAGCGGC GACTCGGCCGACAACGTCATCGCGACGTACACGGTCAACGCCTCCAGCGAGGTGGCCAAC GGGTCCTGGAAGCTCCGTGTCCAGGACATCGCCCGCCAGGACACCGGATACATCGACAGC TGGAAGCTCACCTTCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P80561 UniProtKB Entry Name APX_STRGG - General References
- Ohnishi Y, Ishikawa J, Hara H, Suzuki H, Ikenoya M, Ikeda H, Yamashita A, Hattori M, Horinouchi S: Genome sequence of the streptomycin-producing microorganism Streptomyces griseus IFO 13350. J Bacteriol. 2008 Jun;190(11):4050-60. doi: 10.1128/JB.00204-08. Epub 2008 Mar 28. [Article]
- Maras B, Greenblatt HM, Shoham G, Spungin-Bialik A, Blumberg S, Barra D: Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases. Eur J Biochem. 1996 Mar 15;236(3):843-6. [Article]
- Spungin A, Blumberg S: Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme. Eur J Biochem. 1989 Aug 1;183(2):471-7. [Article]
- Ben-Meir D, Spungin A, Ashkenazi R, Blumberg S: Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution. Eur J Biochem. 1993 Feb 15;212(1):107-12. [Article]
- Fundoiano-Hershcovitz Y, Rabinovitch L, Langut Y, Reiland V, Shoham G, Shoham Y: Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus. FEBS Lett. 2004 Jul 30;571(1-3):192-6. [Article]
- Hershcovitz YF, Gilboa R, Reiland V, Shoham G, Shoham Y: Catalytic mechanism of SGAP, a double-zinc aminopeptidase from Streptomyces griseus. FEBS J. 2007 Aug;274(15):3864-76. Epub 2007 Jul 2. [Article]
- Greenblatt HM, Almog O, Maras B, Spungin-Bialik A, Barra D, Blumberg S, Shoham G: Streptomyces griseus aminopeptidase: X-ray crystallographic structure at 1.75 A resolution. J Mol Biol. 1997 Feb 7;265(5):620-36. [Article]
- Reiland V, Gilboa R, Spungin-Bialik A, Schomburg D, Shoham Y, Blumberg S, Shoham G: Binding of inhibitory aromatic amino acids to Streptomyces griseus aminopeptidase. Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1738-46. Epub 2004 Sep 23. [Article]