Group 1 truncated hemoglobin GlbN

Details

Name
Group 1 truncated hemoglobin GlbN
Synonyms
  • Hemoglobin-like protein HbN
  • Truncated hemoglobin
Gene Name
glbN
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051144|Group 1 truncated hemoglobin GlbN
MGLLSRLRKREPISIYDKIGGHEAIEVVVEDFYVRVLADDQLSAFFSGTNMSRLKGKQVE
FFAAALGGPEPYTGAPMKQVHQGRGITMHHFSLVAGHLADALTAAGVPSETITEILGVIA
PLAVDVTSGESTTAPV
Number of residues
136
Molecular Weight
14448.445
Theoretical pI
Not Available
GO Classification
Functions
heme binding / metal ion binding / nitric oxide dioxygenase activity / oxygen binding / oxygen transporter activity
Processes
detoxification of nitrogen compound / evasion or tolerance by symbiont of host-produced nitric oxide / nitric oxide catabolic process
Components
cytosol
General 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.
Specific Function
Heme binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0051145|Group 1 truncated hemoglobin GlbN (glbN)
ATGGGACTACTGTCACGCTTGCGCAAACGTGAGCCGATCAGCATCTACGACAAGATCGGC
GGGCATGAGGCCATCGAAGTCGTCGTCGAGGACTTCTATGTTCGTGTGCTTGCCGATGAC
CAACTATCGGCCTTCTTCAGCGGTACGAACATGAGCCGCCTCAAGGGCAAGCAGGTGGAG
TTTTTCGCGGCCGCGCTTGGCGGGCCCGAGCCCTATACCGGTGCGCCGATGAAGCAAGTC
CATCAGGGGCGCGGAATTACCATGCACCACTTCAGCCTGGTCGCCGGACACTTGGCCGAC
GCGCTGACCGCAGCCGGCGTGCCCTCCGAAACGATCACGGAAATCCTCGGCGTCATCGCG
CCGCTGGCGGTCGACGTCACATCGGGCGAGAGCACCACGGCACCAGTCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WN25
UniProtKB Entry NameTRHBN_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Yeh SR, Couture M, Ouellet Y, Guertin M, Rousseau DL: 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. [Article]
  3. Raman K, Yeturu K, Chandra N: 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. [Article]
  4. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: 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. [Article]
  5. Milani M, Pesce A, Ouellet Y, Ascenzi P, Guertin M, Bolognesi M: Mycobacterium tuberculosis hemoglobin N displays a protein tunnel suited for O2 diffusion to the heme. EMBO J. 2001 Aug 1;20(15):3902-9. [Article]
  6. Milani M, Ouellet Y, Ouellet H, Guertin M, Boffi A, Antonini G, Bocedi A, Mattu M, Bolognesi M, Ascenzi P: Cyanide binding to truncated hemoglobins: a crystallographic and kinetic study. Biochemistry. 2004 May 11;43(18):5213-21. [Article]
  7. Milani M, Pesce A, Ouellet Y, Dewilde S, Friedman J, Ascenzi P, Guertin M, Bolognesi M: Heme-ligand tunneling in group I truncated hemoglobins. J Biol Chem. 2004 May 14;279(20):21520-5. Epub 2004 Mar 11. [Article]
  8. Ouellet Y, Milani M, Couture M, Bolognesi M, Guertin M: 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. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01826N-Butyl IsocyanideexperimentalunknownDetails
DB03317Ferroheme CexperimentalunknownDetails