Acetolactate synthase, catabolic


NameAcetolactate synthase, catabolic
Synonyms
  • 2.2.1.6
  • ALS
  • ilvK
Gene NamebudB
OrganismKlebsiella pneumoniae
Amino acid sequence
>lcl|BSEQ0019135|Acetolactate synthase, catabolic
MDKQYPVRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPVRHEANA
AFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVALGGAVKRADKAKQVHQ
SMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAAEQGRPGSAFVSLPQDVVDGPVSGKV
LPASGAPQMGAAPDDAIDQVAKLIAQAKNPIFLLGLMASQPENSKALRRLLETSHIPVTS
TYQAAGAVNQDNFSRFAGRVGLFNNQAGDRLLQLADLVICIGYSPVEYEPAMWNSGNATL
VHIDVLPAYEERNYTPDVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQRELLD
RRGAQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYLYTFRARQVMISNGQQ
TMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSMELETAVRLKANVLHLIWVDNGYNMV
AIQEEKKYQRLSGVEFGPMDFKAYAESFGAKGFAVESAEALEPTLRAAMDVDGPAVVAIP
VDYRDNPLLMGQLHLSQIL
Number of residuesNone
Molecular Weight60337.52
Theoretical pI5.99
GO Classification
Functions
  • magnesium ion binding
  • thiamine pyrophosphate binding
  • acetolactate synthase activity
Processes
  • butanediol metabolic process
Components
General FunctionThiamine pyrophosphate binding
Specific FunctionNone
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP27696
UniProtKB Entry Name
Cellular LocationNone
Gene sequence
>lcl|BSEQ0003039|1680 bp
ATGGACAAACAGTATCCGGTACGCCAGTGGGCGCACGGCGCCGATCTCGTCGTCAGTCAG
CTGGAAGCTCAGGGAGTACGCCAGGTGTTCGGCATCCCCGGCGCCAAAATCGACAAGGTC
TTTGATTCACTGCTGGATTCCTCCATTCGCATTATTCCGGTACGCCACGAAGCCAACGCC
GCATTTATGGCCGCCGCCGTCGGACGCATTACCGGCAAAGCGGGCGTGGCGCTGGTCACC
TCCGGTCCGGGCTGTTCCAACCTGATCACCGGCATGGCCACCGCGAACAGCGAAGGCGAC
CCGGTGGTGGCCCTGGGCGGCGCGGTAAAACGCGCCGATAAAGCGAAGCAGGTCCACCAG
AGTATGGATACGGTGGCGATGTTCAGCCCGGTCACCAAATACGCCATCGAGGTGACGGCG
CCGGATGCGCTGGCGGAAGTGGTCTCCAACGCCTTCCGCGCCGCCGAGCAGGGCCGGCCG
GGCAGCGCGTTCGTTAGCCTGCCGCAGGATGTGGTCGATGGCCCGGTCAGCGGCAAAGTG
CTGCCGGCCAGCGGGGCCCCGCAGATGGGCGCCGCGCCGGATGATGCCATCGACCAGGTG
GCGAAGCTTATCGCCCAGGCGAAGAACCCGATCTTCCTGCTCGGCCTGATGGCCAGCCAG
CCGGAAAACAGCAAGGCGCTGCGCCGTTTGCTGGAGACCAGCCATATTCCAGTCACCAGC
ACCTATCAGGCCGCCGGAGCGGTGAATCAGGATAACTTCTCTCGCTTCGCCGGCCGGGTT
GGGCTGTTTAACAACCAGGCCGGGGACCGTCTGCTGCAGCTCGCCGACCTGGTGATCTGC
ATCGGCTACAGCCCGGTGGAATACGAACCGGCGATGTGGAACAGCGGCAACGCGACGCTG
GTGCACATCGACGTGCTGCCCGCCTATGAAGAGCGCAACTACACCCCGGATGTCGAGCTG
GTGGGCGATATCGCCGGCACTCTCAACAAGCTGGCGCAAAATATCGATCATCGGCTGGTG
CTCTCCCCGCAGGCGGCGGAGATCCTCCGCGACCGCCAGCACCAGCGCGAGCTGCTGGAC
CGCCGCGGCGCGCAGCTCAACCAGTTTGCCCTGCATCCCCTGCGCATCGTTCGCGCCATG
CAGGATATCGTCAACAGCGACGTCACGTTGACCGTGGACATGGGCAGCTTCCATATCTGG
ATTGCCCGCTACCTGTACACGTTCCGCGCCCGTCAGGTGATGATCTCCAACGGCCAGCAG
ACCATGGGCGTCGCCCTGCCCTGGGCTATCGGCGCCTGGCTGGTCAATCCTGAGCGCAAA
GTGGTCTCCGTCTCCGGCGACGGCGGCTTCCTGCAGTCGAGCATGGAGCTGGAGACCGCC
GTCCGCCTGAAAGCCAACGTGCTGCATCTTATCTGGGTCGATAACGGCTACAACATGGTC
GCTATCCAGGAAGAGAAAAAATATCAGCGCCTGTCCGGCGTCGAGTTTGGGCCGATGGAT
TTTAAAGCCTATGCCGAATCCTTCGGCGCGAAAGGGTTTGCCGTGGAAAGCGCCGAGGCG
CTGGAGCCGACCCTGCGCGCGGCGATGGACGTCGACGGCCCGGCGGTAGTGGCCATCCCG
GTGGATTATCGCGATAACCCGCTGCTGATGGGCCAGCTGCATCTGAGTCAGATTCTGTAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Peng HL, Wang PY, Wu CM, Hwang DC, Chang HY: Cloning, sequencing and heterologous expression of a Klebsiella pneumoniae gene encoding an FAD-independent acetolactate synthase. Gene. 1992 Aug 1;117(1):125-30. [1644303 ]
  2. Pang SS, Duggleby RG, Schowen RL, Guddat LW: The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate. J Biol Chem. 2004 Jan 16;279(3):2242-53. Epub 2003 Oct 13. [14557277 ]

From www.t3db.ca