3-methyl-2-oxobutanoate hydroxymethyltransferase

Details

Name
3-methyl-2-oxobutanoate hydroxymethyltransferase
Synonyms
  • 2.1.2.11
  • Ketopantoate hydroxymethyltransferase
  • KPHMT
Gene Name
panB
Organism
Neisseria meningitidis serogroup B (strain MC58)
Amino acid sequence
>lcl|BSEQ0011305|3-methyl-2-oxobutanoate hydroxymethyltransferase
MITVNTLQKMKAAGEKIAMLTAYESSFAALMDDAGVEMLLVGDSLGMAVQGRKSTLPVSL
RDMCYHTECVARGAKNAMIVSDLPFGAYQQSKEQAFAAAAELMAAGAHMVKLEGGVWMAE
TTEFLQMRGIPVCAHIGLTPQSVFAFGGYKVQGRGGKAQALLNDAKAHDDAGAAVVLMEC
VLAELAKKVTETVSCPTIGIGAGADCDGQVLVMHDMLGIFPGKTAKFVKNFMQGHDSVQA
AVRAYVAEVKAKTFPAAEHIFAD
Number of residues
263
Molecular Weight
27739.07
Theoretical pI
6.39
GO Classification
Functions
3-methyl-2-oxobutanoate hydroxymethyltransferase activity / metal ion binding
Processes
pantothenate biosynthetic process
Components
cytoplasm
General Function
Metal ion binding
Specific Function
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011306|3-methyl-2-oxobutanoate hydroxymethyltransferase (panB)
ATGATTACTGTGAACACACTGCAAAAAATGAAGGCGGCGGGCGAAAAAATCGCTATGCTG
ACCGCTTACGAATCCAGTTTTGCCGCGCTGATGGACGATGCCGGCGTGGAAATGCTGCTG
GTCGGCGATTCTTTGGGGATGGCGGTTCAGGGGCGGAAATCGACGCTGCCCGTCAGCCTG
CGCGATATGTGTTATCACACCGAATGTGTAGCACGCGGTGCAAAAAATGCGATGATTGTC
AGCGATTTGCCGTTTGGTGCATATCAGCAGAGTAAGGAGCAGGCGTTTGCCGCCGCCGCC
GAACTGATGGCTGCCGGCGCGCATATGGTTAAACTCGAAGGCGGCGTGTGGATGGCGGAA
ACGACTGAATTTTTGCAAATGCGCGGTATTCCGGTTTGTGCGCACATCGGTCTGACCCCG
CAATCCGTGTTTGCCTTCGGCGGATATAAAGTTCAGGGGCGCGGCGGCAAGGCGCAGGCG
TTGCTTAACGATGCCAAGGCGCATGACGATGCGGGGGCGGCGGTCGTGCTGATGGAGTGC
GTACTGGCGGAACTGGCAAAAAAGGTAACTGAAACTGTTTCCTGTCCGACCATCGGCATC
GGCGCGGGTGCGGATTGCGACGGGCAGGTTTTGGTGATGCACGATATGCTCGGCATTTTC
CCGGGTAAGACGGCGAAATTCGTCAAAAACTTTATGCAGGGGCATGATAGTGTTCAAGCG
GCGGTTCGGGCGTATGTTGCCGAAGTCAAAGCCAAAACCTTCCCTGCTGCGGAACATATT
TTTGCAGATTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ9JZW6
UniProtKB Entry NamePANB_NEIMB
GenBank Protein ID7226107
GenBank Gene IDAE002098
General References
  1. Tettelin H, Saunders NJ, Heidelberg J, Jeffries AC, Nelson KE, Eisen JA, Ketchum KA, Hood DW, Peden JF, Dodson RJ, Nelson WC, Gwinn ML, DeBoy R, Peterson JD, Hickey EK, Haft DH, Salzberg SL, White O, Fleischmann RD, Dougherty BA, Mason T, Ciecko A, Parksey DS, Blair E, Cittone H, Clark EB, Cotton MD, Utterback TR, Khouri H, Qin H, Vamathevan J, Gill J, Scarlato V, Masignani V, Pizza M, Grandi G, Sun L, Smith HO, Fraser CM, Moxon ER, Rappuoli R, Venter JC: Complete genome sequence of Neisseria meningitidis serogroup B strain MC58. Science. 2000 Mar 10;287(5459):1809-15. [Article]
  2. Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ: Structural analysis of a set of proteins resulting from a bacterial genomics project. Proteins. 2005 Sep 1;60(4):787-96. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04074alpha-KetoisovalerateexperimentalunknownDetails