Gene - combatTB X

panB

Type: protein_coding
Name: panB
Locus Name: Rv2225
Product: 3-methyl-2-oxobutanoate hydroxymethyltransferase PanB
Functional Category: Intermediary metabolism and respiration
Location: 2497742..2498587 (+ strand)
Gene Length: 845 bp
Nucleotides: TGTCTGAGCAGACTATCTATGGGGCCAATACCCCCGGAGGCTCCGGGCCGCGGACCAAGATCCGCACCCACCACCTACAGAGATGGAAGGCCGACGGCCACAAGTGGGCCATGCTGACGGCCTACGACTATTCGACGGCCCGGATCTTCGACGAGGCCGGCATCCCGGTGCTGCTGGTCGGTGATTCGGCGGCCAACGTCGTGTACGGCTACGACACCACCGTGCCGATCTCCATCGACGAGCTGATCCCGCTGGTCCGTGGCGTGGTGCGGGGTGCCCCGCACGCACTGGTCGTCGCCGACCTGCCGTTCGGCAGCTACGAGGCGGGGCCCACCGCCGCGTTGGCCGCCGCCACCCGGTTCCTCAAGGACGGCGGCGCACATGCGGTCAAGCTCGAGGGCGGTGAGCGGGTGGCCGAGCAAATCGCCTGTCTGACCGCGGCGGGCATCCCGGTGATGGCACACATCGGCTTCACCCCGCAAAGCGTCAACACCTTGGGCGGCTTCCGGGTGCAGGGCCGCGGCGACGCCGCCGAACAAACCATCGCCGACGCGATCGCCGTCGCCGAAGCCGGAGCGTTTGCCGTCGTGATGGAGATGGTGCCCGCCGAGTTGGCCACCCAGATCACCGGCAAGCTTACCATTCCGACGGTCGGGATCGGCGCTGGGCCCAACTGCGACGGCCAGGTCCTGGTATGGCAGGACATGGCCGGGTTCAGCGGCGCCAAGACCGCCCGCTTCGTCAAACGGTATGCCGATGTCGGTGGTGAACTACGCCGTGCTGCAATGCAATACGCCCAAGAGGTGGCCGGCGGGGTATTCCCCGCTGACGAACACAGTTTCTGA
Drug Resistance: Check for drug resistance association at TBDREAMDB
Mutations: Check for mutants available at TARGET

Function

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000269|PubMed:12515554}.

Family

PanB family

GO

magnesium ion binding GO:0000287 molecular_function
pantothenate biosynthetic process GO:0015940 biological_process
3-methyl-2-oxobutanoate hydroxymethyltransferase activity GO:0003864 molecular_function
plasma membrane GO:0005886 cellular_component
cytoplasm GO:0005737 cellular_component

InterPro

UniProt: P9WIL7
GenBank: Rv2225
EnsemblBacteria: Rv2225
Mycobrowser: Rv2225

Summary

Name: 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) (Ketopantoate hydroxymethyltransferase) (KPHMT)
Family: PanB family
Protein Sequence: MSEQTIYGANTPGGSGPRTKIRTHHLQRWKADGHKWAMLTAYDYSTARIFDEAGIPVLLVGDSAANVVYGYDTTVPISIDELIPLVRGVVRGAPHALVVADLPFGSYEAGPTAALAAATRFLKDGGAHAVKLEGGERVAEQIACLTAAGIPVMAHIGFTPQSVNTLGGFRVQGRGDAAEQTIADAIAVAEAGAFAVVMEMVPAELATQITGKLTIPTVGIGAGPNCDGQVLVWQDMAGFSGAKTARFVKRYADVGGELRRAAMQYAQEVAGGVFPADEHSF
Mass: 29,336 Da
Length: 281 Aa

Rv2225 doesn't seem to be a targeted by any drug.

Pantothenate and CoA biosynthesis mtu00770
mtu00770
PATHWAY_MAP mtu00770 Pantothenate and CoA biosynthesis

The crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosis.: Structure. 2003 Jul;11(7):753-64.
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.: Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate.: J Am Chem Soc. 2010 Apr 28;132(16):5610-2. doi: 10.1021/ja910546x.
targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis.: BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109.
Identification of substrates of the Mycobacterium tuberculosis proteasome.: EMBO J. 2006 Nov 15;25(22):5423-32. doi: 10.1038/sj.emboj.7601405. Epub 2006 Nov 2.
Mycobacterium tuberculosis ketopantoate hydroxymethyltransferase: tetrahydrofolate-independent hydroxymethyltransferase and enolization reactions with alpha-keto acids.: Biochemistry. 2003 Jan 14;42(1):191-9. doi: 10.1021/bi020516q.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.: Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.