Neopullulanase 2

Details

Name
Neopullulanase 2
Synonyms
  • 3.2.1.135
  • Alpha-amylase II
  • TVA II
Gene Name
tvaII
Organism
Thermoactinomyces vulgaris
Amino acid sequence
>lcl|BSEQ0011001|Neopullulanase 2
MLLEAIFHEAKGSYAYPISETQLRVRLRAKKGDVVRCEVLYADRYASPEEELAHALAGKA
GSDERFDYFEALLECSTKRVKYVFLLTGPQGEAVYFGETGFSAERSKAGVFQYAYIHRSE
VFTTPEWAKEAVIYQIFPERFANGDPSNDPPGTEQWAKDARPRHDSFYGGDLKGVIDRLP
YLEELGVTALYFTPIFASPSHHKYDTADYLAIDPQFGDLPTFRRLVDEAHRRGIKIILDA
VFNHAGDQFFAFRDVLQKGEQSRYKDWFFIEDFPVSKTSRTNYETFAVQVPAMPKLRTEN
PEVKEYLFDVARFWMEQGIDGWRLDVANEVDHAFWREFRRLVKSLNPDALIVGEIWHDAS
GWLMGDQFDSVMNYLFRESVIRFFATGEIHAERFDAELTRARMLYPEQAAQGLWNLLDSH
DTERFLTSCGGNEAKFRLAVLFQMTYLGTPLIYYGDEIGMAGATDPDCRRPMIWEEKEQN
RGLFEFYKELIRLRHRLASLTRGNVRSWHADKQANLYAFVRTVQDQHVGVVLNNRGEKQT
VLLQVPESGGKTWLDCLTGEEVHGKQGQLKLTLRPYQGMILWNGR
Number of residues
585
Molecular Weight
67466.71
Theoretical pI
5.89
GO Classification
Functions
metal ion binding / neopullulanase activity
Processes
carbohydrate metabolic process
General Function
Neopullulanase activity
Specific Function
Hydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0002832|1758 bp
ATGCTGTTGGAAGCGATTTTTCATGAAGCGAAAGGAAGCTATGCTTACCCGATTTCGGAA
ACGCAACTGCGGGTGAGATTGCGGGCGAAAAAAGGGGACGTGGTGAGATGCGAGGTGCTC
TATGCGGACCGCTATGCTTCGCCGGAGGAAGAACTGGCACATGCACTTGCGGGCAAAGCA
GGGTCCGATGAGCGATTTGATTATTTTGAGGCTTTACTGGAATGTTCCACCAAACGGGTG
AAATACGTGTTTTTGTTGACAGGCCCACAAGGGGAGGCTGTTTATTTTGGCGAGACCGGT
TTTTCCGCCGAACGGTCTAAAGCGGGGGTGTTCCAATATGCTTACATCCACCGGAGCGAA
GTGTTTACGACACCGGAATGGGCAAAGGAGGCGGTGATCTACCAGATCTTTCCCGAACGT
TTTGCCAATGGGGATCCCAGCAATGATCCGCCGGGAACGGAACAATGGGCCAAAGACGCC
AGACCTCGGCACGACAGTTTTTACGGCGGAGATTTAAAGGGGGTGATCGACCGTTTGCCA
TATTTGGAGGAGTTGGGAGTGACGGCGCTTTATTTTACTCCCATTTTTGCTTCGCCGTCC
CATCACAAATATGATACAGCTGATTATTTGGCGATTGATCCGCAATTTGGGGATTTGCCC
ACCTTTCGGCGTTTGGTGGATGAAGCTCACCGGCGCGGGATCAAAATCATTTTGGATGCC
GTGTTTAACCATGCCGGAGATCAGTTTTTTGCGTTTCGGGATGTTCTGCAAAAGGGAGAA
CAGTCGCGATATAAGGATTGGTTTTTCATCGAGGATTTTCCCGTTTCCAAGACGTCAAGA
ACCAATTATGAAACCTTTGCCGTCCAAGTGCCGGCCATGCCCAAATTGCGGACGGAAAAT
CCGGAAGTGAAGGAATATTTGTTTGATGTCGCGCGATTTTGGATGGAGCAGGGGATCGAC
GGATGGAGACTGGATGTGGCCAATGAGGTGGATCACGCCTTTTGGCGCGAGTTTCGCCGC
CTTGTCAAATCCCTCAATCCCGACGCCTTGATTGTCGGAGAGATTTGGCATGACGCTTCC
GGCTGGCTGATGGGAGACCAATTTGATTCGGTGATGAATTATTTGTTTCGCGAGAGTGTG
ATCCGTTTTTTTGCCACGGGGGAGATCCATGCCGAAAGATTTGACGCCGAACTTACCCGG
GCCAGGATGCTTTATCCGGAACAGGCGGCACAAGGGTTATGGAACCTCCTCGACTCACAC
GATACGGAACGTTTTTTGACATCGTGTGGGGGGAATGAGGCGAAATTCCGCCTGGCTGTT
TTGTTTCAGATGACATACCTGGGGACGCCGCTGATTTATTACGGTGATGAGATCGGGATG
GCCGGAGCGACGGACCCGGATTGCCGGCGCCCGATGATATGGGAGGAAAAAGAGCAGAAC
CGCGGCTTGTTTGAGTTTTATAAGGAATTGATTCGCTTGCGCCATCGGCTGGCATCGCTC
ACCAGGGGAAATGTCCGGTCTTGGCATGCCGACAAACAAGCCAATCTTTATGCTTTTGTG
CGCACGGTTCAAGACCAACATGTCGGTGTGGTTCTCAATAATCGTGGCGAGAAGCAAACC
GTTTTGCTACAGGTGCCGGAATCGGGCGGAAAAACTTGGCTGGATTGTTTGACCGGAGAA
GAAGTGCATGGCAAACAAGGGCAACTGAAGCTGACACTTCGCCCTTACCAGGGAATGATT
CTCTGGAATGGCCGGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ08751
UniProtKB Entry NameNEPU2_THEVU
GenBank Protein ID398125
GenBank Gene IDD13178
General References
  1. Tonozuka T, Ohtsuka M, Mogi S, Sakai H, Ohta T, Sakano Y: A neopullulanase-type alpha-amylase gene from Thermoactinomyces vulgaris R-47. Biosci Biotechnol Biochem. 1993 Mar;57(3):395-401. [Article]
  2. Kamitori S, Kondo S, Okuyama K, Yokota T, Shimura Y, Tonozuka T, Sakano Y: Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution. J Mol Biol. 1999 Apr 16;287(5):907-21. [Article]
  3. Kamitori S, Abe A, Ohtaki A, Kaji A, Tonozuka T, Sakano Y: Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution. J Mol Biol. 2002 Apr 26;318(2):443-53. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02237MaltotetraoseexperimentalunknownDetails
DB03995BetadexexperimentalunknownDetails
DB02379Beta-D-GlucoseexperimentalunknownDetails