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Group 1 truncated hemoglobin GlbN (Truncated hemoglobin) (trHbN) (Hemoglobin-like protein HbN)

 TRHBN_MYCTU             Reviewed;         136 AA.
P9WN25; L0T6Z0; P0A592; Q10784;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
22-NOV-2017, entry version 27.
RecName: Full=Group 1 truncated hemoglobin GlbN;
Short=Truncated hemoglobin;
Short=trHbN;
AltName: Full=Hemoglobin-like protein HbN;
Name=glbN; OrderedLocusNames=Rv1542c; ORFNames=MTCY48.23;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
CHARACTERIZATION.
PubMed=10636862; DOI=10.1074/jbc.275.3.1679;
Yeh S.R., Couture M., Ouellet Y., Guertin M., Rousseau D.L.;
"A cooperative oxygen binding hemoglobin from Mycobacterium
tuberculosis. Stabilization of heme ligands by a distal tyrosine
residue.";
J. Biol. Chem. 275:1679-1684(2000).
[3]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
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. 2:109-109(2008).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[5]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN THE OXY-FORM, SUBUNIT, AND
HEME COFACTOR.
PubMed=11483493; DOI=10.1093/emboj/20.15.3902;
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. 20:3902-3909(2001).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN THE FE(3+)-CYANIDE-DERIVATIVE
FORM.
PubMed=15122887; DOI=10.1021/bi049870+;
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 43:5213-5221(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN THE CYANO-MET FORM.
PubMed=15016811; DOI=10.1074/jbc.M401320200;
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. 279:21520-21525(2004).
[8]
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN THE CYANO-MET FORM.
PubMed=16846220; DOI=10.1021/bi060112o;
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 45:8770-8781(2006).
-!- 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.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Note=Binds 1 heme group per subunit.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11483493}.
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
-!- SIMILARITY: Belongs to the truncated hemoglobin family. Group I
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL123456; CCP44306.1; -; Genomic_DNA.
PIR; C70761; C70761.
RefSeq; NP_216058.1; NC_000962.3.
RefSeq; WP_003407730.1; NZ_KK339370.1.
PDB; 1IDR; X-ray; 1.90 A; A/B=1-136.
PDB; 1RTE; X-ray; 2.00 A; A/B=1-136.
PDB; 1S56; X-ray; 2.43 A; A/B=1-136.
PDB; 1S61; X-ray; 2.10 A; A/B=1-136.
PDB; 2GKM; X-ray; 1.73 A; A/B=1-136.
PDB; 2GKN; X-ray; 2.10 A; A/B=1-136.
PDB; 2GL3; X-ray; 1.92 A; A/B=1-136.
PDB; 2GLN; X-ray; 1.98 A; A/B=1-136.
PDB; 5AB8; X-ray; 1.53 A; A=12-136.
PDBsum; 1IDR; -.
PDBsum; 1RTE; -.
PDBsum; 1S56; -.
PDBsum; 1S61; -.
PDBsum; 2GKM; -.
PDBsum; 2GKN; -.
PDBsum; 2GL3; -.
PDBsum; 2GLN; -.
PDBsum; 5AB8; -.
ProteinModelPortal; P9WN25; -.
SMR; P9WN25; -.
STRING; 83332.Rv1542c; -.
PaxDb; P9WN25; -.
EnsemblBacteria; CCP44306; CCP44306; Rv1542c.
GeneID; 886402; -.
KEGG; mtu:Rv1542c; -.
TubercuList; Rv1542c; -.
eggNOG; ENOG4105K6B; Bacteria.
eggNOG; COG2346; LUCA.
KO; K06886; -.
OMA; GGPCKYT; -.
PhylomeDB; P9WN25; -.
Reactome; R-HSA-1222538; Tolerance by Mtb to nitric oxide produced by macrophages.
Proteomes; UP000001584; Chromosome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0020037; F:heme binding; IDA:MTBBASE.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008941; F:nitric oxide dioxygenase activity; IDA:MTBBASE.
GO; GO:0019825; F:oxygen binding; IDA:MTBBASE.
GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
GO; GO:0051410; P:detoxification of nitrogen compound; IDA:MTBBASE.
GO; GO:0052060; P:evasion or tolerance by symbiont of host-produced nitric oxide; TAS:Reactome.
GO; GO:0046210; P:nitric oxide catabolic process; IMP:MTBBASE.
InterPro; IPR009050; Globin-like_sf.
InterPro; IPR019795; Globin_bac-like_CS.
InterPro; IPR001486; Hemoglobin_trunc.
InterPro; IPR016339; Hemoglobin_trunc_I.
Pfam; PF01152; Bac_globin; 1.
PIRSF; PIRSF002030; Globin_Protozoa/Cyanobacteria; 1.
SUPFAM; SSF46458; SSF46458; 1.
PROSITE; PS01213; GLOBIN_FAM_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Heme; Iron; Metal-binding;
Oxygen transport; Reference proteome; Transport.
CHAIN 1 136 Group 1 truncated hemoglobin GlbN.
/FTId=PRO_0000162640.
METAL 81 81 Iron (heme proximal ligand).
HELIX 3 8 {ECO:0000244|PDB:2GKM}.
HELIX 15 19 {ECO:0000244|PDB:5AB8}.
HELIX 21 38 {ECO:0000244|PDB:5AB8}.
TURN 40 42 {ECO:0000244|PDB:5AB8}.
HELIX 43 46 {ECO:0000244|PDB:5AB8}.
HELIX 51 65 {ECO:0000244|PDB:5AB8}.
HELIX 77 81 {ECO:0000244|PDB:5AB8}.
HELIX 88 104 {ECO:0000244|PDB:5AB8}.
HELIX 109 123 {ECO:0000244|PDB:5AB8}.
SEQUENCE 136 AA; 14449 MW; B75D01A45BC064BB CRC64;
MGLLSRLRKR EPISIYDKIG GHEAIEVVVE DFYVRVLADD QLSAFFSGTN MSRLKGKQVE
FFAAALGGPE PYTGAPMKQV HQGRGITMHH FSLVAGHLAD ALTAAGVPSE TITEILGVIA
PLAVDVTSGE STTAPV


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