Gene - combatTB X

glbN

Type: protein_coding
Name: glbN
Locus Name: Rv1542c
Product: Hemoglobin GlbN
Functional Category: Intermediary metabolism and respiration
Location: 1744426..1744836 (- strand)
Gene Length: 410 bp
Nucleotides: ATGGGACTACTGTCACGCTTGCGCAAACGTGAGCCGATCAGCATCTACGACAAGATCGGCGGGCATGAGGCCATCGAAGTCGTCGTCGAGGACTTCTATGTTCGTGTGCTTGCCGATGACCAACTATCGGCCTTCTTCAGCGGTACGAACATGAGCCGCCTCAAGGGCAAGCAGGTGGAGTTTTTCGCGGCCGCGCTTGGCGGGCCCGAGCCCTATACCGGTGCGCCGATGAAGCAAGTCCATCAGGGGCGCGGAATTACCATGCACCACTTCAGCCTGGTCGCCGGACACTTGGCCGACGCGCTGACCGCAGCCGGCGTGCCCTCCGAAACGATCACGGAAATCCTCGGCGTCATCGCGCCGCTGGCGGTCGACGTCACATCGGGCGAGAGCACCACGGCACCAGTCTG
Drug Resistance: Check for drug resistance association at TBDREAMDB
Mutations: Check for mutants available at TARGET

Function

Binds oxygen cooperatively with very high affinity (P(50) = 0.013 mmHg at 20 degrees Celsius) because of a fast combination (25 microM(-1).s(-1)) and a slow dissociation (0.2 s(-1)) rate.

Family

Truncated hemoglobin family, Group I subfamily

GO

metal ion binding GO:0046872 molecular_function
heme binding GO:0020037 molecular_function
nitric oxide catabolic process GO:0046210 biological_process
oxygen carrier activity GO:0005344 molecular_function
oxygen binding GO:0019825 molecular_function
cytosol GO:0005829 cellular_component
nitric oxide dioxygenase activity GO:0008941 molecular_function
evasion or tolerance by symbiont of host-produced nitric oxide GO:0052060 biological_process
detoxification of nitrogen compound GO:0051410 biological_process

InterPro

UniProt: P9WN25
GenBank: Rv1542c
EnsemblBacteria: Rv1542c
Mycobrowser: Rv1542c

PDB IDs:

Summary

Name: Group 1 truncated hemoglobin GlbN (Truncated hemoglobin) (trHbN) (Hemoglobin-like protein HbN)
Family: Truncated hemoglobin family, Group I subfamily
Protein Sequence: MGLLSRLRKREPISIYDKIGGHEAIEVVVEDFYVRVLADDQLSAFFSGTNMSRLKGKQVEFFAAALGGPEPYTGAPMKQVHQGRGITMHHFSLVAGHLADALTAAGVPSETITEILGVIAPLAVDVTSGESTTAPV
Mass: 14,449 Da
Length: 136 Aa

Rv1542c doesn't seem to be a targeted by any drug.

Tolerance by Mtb to nitric oxide produced by macrophages R-HSA-1222538
Homo sapiens
R-HSA-1222538

Ligand interactions in the distal heme pocket of Mycobacterium tuberculosis truncated hemoglobin N: roles of TyrB10 and GlnE11 residues.: Biochemistry. 2006 Jul 25;45(29):8770-81. doi: 10.1021/bi060112o.
Heme-ligand tunneling in group I truncated hemoglobins.: J Biol Chem. 2004 May 14;279(20):21520-5. doi: 10.1074/jbc.M401320200. Epub 2004 Mar 11.
Cyanide binding to truncated hemoglobins: a crystallographic and kinetic study.: Biochemistry. 2004 May 11;43(18):5213-21. doi: 10.1021/bi049870+.
Mycobacterium tuberculosis hemoglobin N displays a protein tunnel suited for O2 diffusion to the heme.: EMBO J. 2001 Aug 1;20(15):3902-9. doi: 10.1093/emboj/20.15.3902.
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.
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.
A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis. Stabilization of heme ligands by a distal tyrosine residue.: J Biol Chem. 2000 Jan 21;275(3):1679-84. doi: 10.1074/jbc.275.3.1679.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.: Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.