Glucan 1,4-alpha-maltotetraohydrolase
Details
- Name
- Glucan 1,4-alpha-maltotetraohydrolase
- Synonyms
- 3.2.1.60
- Exo-maltotetraohydrolase
- G4-amylase
- Maltotetraose-forming amylase
- Maltotetraose-forming exo-amylase
- Gene Name
- amyP
- Organism
- Pseudomonas stutzeri
- Amino acid sequence
>lcl|BSEQ0011061|Glucan 1,4-alpha-maltotetraohydrolase MSHILRAAVLAAMLLPLPSMADQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNIL RQQAATIAADGFSAIWMPVPWRDFSSWSDGSKSGGGEGYFWHDFNKNGRYGSDAQLRQAA SALGGAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDCDDGDRFIGG DADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFDFVRGYAPERVNSWMTDSADNSFCVGE LWKGPSEYPNWDWRNTASWQQIIKDWSDRAKCPVFDFALKERMQNGSIADWKHGLNGNPD PRWREVAVTFVDNHDTGYSPGQNGGQHHWALQDGLIRQAYAYILTSPGTPVVYWSHMYDW GYGDFIRQLIQVRRAAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVAS GSFSEAVNASNGQVRVWRSGTGSGGGEPGALVSVSFRCDNGATQMGDSVYAVGNVSQLGN WSPAAALRLTDTSGYPTWKGSIALPAGQNEEWKCLIRNEANATQVRQWQGGANNSLTPSE GATTVGRL
- Number of residues
- 548
- Molecular Weight
- 59875.725
- Theoretical pI
- 5.93
- GO Classification
- Functionsglucan 1,4-alpha-maltotetraohydrolase activity / metal ion binding / starch bindingProcessesstarch catabolic processComponentsextracellular region
- General Function
- Starch binding
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0002977|1644 bp ATGAGCCACATCCTGCGAGCCGCCGTATTGGCGGCGATGCTGTTGCCGTTGCCGTCCATG GCCGATCAGGCCGGCAAGAGCCCCAACGCTGTGCGCTACCACGGCGGCGACGAAATCATT CTCCAGGGCTTTCACTGGAACGTCGTCCGCGAAGCGCCCAACGACTGGTACAACATCCTG CGCCAGCAGGCCGCGACCATCGCCGCCGACGGCTTCTCGGCGATCTGGATGCCGGTGCCC TGGCGCGACTTCTCCAGCTGGAGCGACGGCAGCAAGTCCGGCGGCGGTGAAGGCTACTTC TGGCACGACTTCAACAAGAACGGCCGCTATGGCAGTGACGCCCAGCTGCGTCAGGCCGCC AGCGCGCTCGGTGGCGCCGGCGTGAAAGTGCTTTACGACGTGGTGCCCAACCACATGAAC CGTGGCTATCCGGACAAGGAGATCAACCTCCCGGCCGGCCAGGGCTTCTGGCGCAACGAC TGCGCCGACCCGGGCAACTACCCCAATGATTGCGACGACGGCGACCGCTTCATCGGCGGC GATGCGGACCTCAACACCGGCCACCCGCAGGTCTACGGCATGTTCCGCGATGAATTCACC AACCTGCGCAGTCAGTACGGTGCCGGCGGCTTCCGCTTCGACTTTGTTCGGGGCTATGCG CCGGAGCGGGTCAACAGCTGGATGACCGATAGCGCCGACAACAGCTTCTGCGTCGGCGAA CTGTGGAAAGGCCCCTCTGAGTACCCGAACTGGGACTGGCGCAACACCGCCAGCTGGCAG CAGATCATCAAGGACTGGTCCGACCGGGCCAAGTGCCCGGTGTTCGACTTCGCCCTCAAG GAACGCATGCAGAACGCTCGATCGCCGACTGGAAGCACGCCTGAACGGCAATCCCGACCC GCGTGGCGCGAGGTGGCGGTGACCTTCGTCGACAACCACGACACCGGCTACTCGCCCGGG CAGAACGGTGGGCAGCACCACTGGGCTCTGCAGGACGGGCTGATCCGCCAGGCCTACGCC TACATCCTCACCAGCCCCGGTACGCCGGTGGTGTACTGGTCGCACATGTACGACTGGGGT TACGGCGACTTCATCCGTCAGCTGATCCAGGTGCGTCGCGCCGCCGGCGTGCGCGCCGAT TCGGCGATCAGCTTCCACAGCGGCTACAGCGGTCTGGTCGCCACCGTCAGCGGCAGCCAG CAGACCCTGGTGGTGGCGCTCAACTCCGACCTGGGCAATCCCGGCCAGGTGGCCAGCGGC AGCTTCAGCGAGGCGGTCAACGCCAGCAACGGCCAGGTGCGCGTGTGGCGTAGCGGCACG GGCAGCGGTGGCGGTGAACCCGGCGCTCTGGTCAGTGTGAGTTTCCGCTGCGACAACGGC GCGACGCAGATGGGCGACAGCGTCTACGCGGTCGGCAACGTCAGCCAGCTCGGTAACTGG AGCCCGGCCGCGGCGTTGCGCCTGACCGACACCAGCGGCTACCCGACCTGGAAGGGCAGC ATTGCCTTGCCTGCCGGCCAGAACGAGGAATGGAAATGCCTGATCCGCAACGAGGCCAAC GCCACCCAGGTGCGGCAATGGCAGGGCGGGGCAAACAACAGCCTGACGCCGAGCGAGGGC GCCACCACCGTCGGCCGGCTCTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P13507 UniProtKB Entry Name AMT4_PSEST GenBank Protein ID 151013 GenBank Gene ID M24516 - General References
- Fujita M, Torigoe K, Nakada T, Tsusaki K, Kubota M, Sakai S, Tsujisaka Y: Cloning and nucleotide sequence of the gene (amyP) for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19. J Bacteriol. 1989 Mar;171(3):1333-9. [Article]
- Morishita Y, Hasegawa K, Matsuura Y, Katsube Y, Kubota M, Sakai S: Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri. J Mol Biol. 1997 Apr 4;267(3):661-72. [Article]
- Yoshioka Y, Hasegawa K, Matsuura Y, Katsube Y, Kubota M: Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose. J Mol Biol. 1997 Aug 29;271(4):619-28. [Article]
- Hasegawa K, Kubota M, Matsuura Y: Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase. Protein Eng. 1999 Oct;12(10):819-24. [Article]