TRHBN_MYCTU
ID TRHBN_MYCTU Reviewed; 136 AA.
AC P9WN25; L0T6Z0; P0A592; Q10784;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Group 1 truncated hemoglobin GlbN;
DE Short=Truncated hemoglobin;
DE Short=trHbN;
DE AltName: Full=Hemoglobin-like protein HbN;
GN Name=glbN; OrderedLocusNames=Rv1542c; ORFNames=MTCY48.23;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP CHARACTERIZATION.
RX PubMed=10636862; DOI=10.1074/jbc.275.3.1679;
RA Yeh S.R., Couture M., Ouellet Y., Guertin M., Rousseau D.L.;
RT "A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis.
RT Stabilization of heme ligands by a distal tyrosine residue.";
RL J. Biol. Chem. 275:1679-1684(2000).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN THE OXY-FORM, SUBUNIT, AND HEME
RP COFACTOR.
RX PubMed=11483493; DOI=10.1093/emboj/20.15.3902;
RA Milani M., Pesce A., Ouellet Y., Ascenzi P., Guertin M., Bolognesi M.;
RT "Mycobacterium tuberculosis hemoglobin N displays a protein tunnel suited
RT for O2 diffusion to the heme.";
RL EMBO J. 20:3902-3909(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN THE FE(3+)-CYANIDE-DERIVATIVE
RP FORM.
RX PubMed=15122887; DOI=10.1021/bi049870+;
RA Milani M., Ouellet Y., Ouellet H., Guertin M., Boffi A., Antonini G.,
RA Bocedi A., Mattu M., Bolognesi M., Ascenzi P.;
RT "Cyanide binding to truncated hemoglobins: a crystallographic and kinetic
RT study.";
RL Biochemistry 43:5213-5221(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN THE CYANO-MET FORM.
RX PubMed=15016811; DOI=10.1074/jbc.m401320200;
RA Milani M., Pesce A., Ouellet Y., Dewilde S., Friedman J., Ascenzi P.,
RA Guertin M., Bolognesi M.;
RT "Heme-ligand tunneling in group I truncated hemoglobins.";
RL J. Biol. Chem. 279:21520-21525(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN THE CYANO-MET FORM.
RX PubMed=16846220; DOI=10.1021/bi060112o;
RA Ouellet Y., Milani M., Couture M., Bolognesi M., Guertin M.;
RT "Ligand interactions in the distal heme pocket of Mycobacterium
RT tuberculosis truncated hemoglobin N: roles of TyrB10 and GlnE11 residues.";
RL Biochemistry 45:8770-8781(2006).
CC -!- FUNCTION: Binds oxygen cooperatively with very high affinity (P(50) =
CC 0.013 mmHg at 20 degrees Celsius) because of a fast combination (25
CC microM(-1).sec(-1)) and a slow dissociation (0.2 sec(-1)) rate.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11483493}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group I
CC subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44306.1; -; Genomic_DNA.
DR PIR; C70761; C70761.
DR RefSeq; NP_216058.1; NC_000962.3.
DR RefSeq; WP_003407730.1; NZ_NVQJ01000004.1.
DR PDB; 1IDR; X-ray; 1.90 A; A/B=1-136.
DR PDB; 1RTE; X-ray; 2.00 A; A/B=1-136.
DR PDB; 1S56; X-ray; 2.43 A; A/B=1-136.
DR PDB; 1S61; X-ray; 2.10 A; A/B=1-136.
DR PDB; 2GKM; X-ray; 1.73 A; A/B=1-136.
DR PDB; 2GKN; X-ray; 2.10 A; A/B=1-136.
DR PDB; 2GL3; X-ray; 1.92 A; A/B=1-136.
DR PDB; 2GLN; X-ray; 1.98 A; A/B=1-136.
DR PDB; 5AB8; X-ray; 1.53 A; A=12-136.
DR PDBsum; 1IDR; -.
DR PDBsum; 1RTE; -.
DR PDBsum; 1S56; -.
DR PDBsum; 1S61; -.
DR PDBsum; 2GKM; -.
DR PDBsum; 2GKN; -.
DR PDBsum; 2GL3; -.
DR PDBsum; 2GLN; -.
DR PDBsum; 5AB8; -.
DR AlphaFoldDB; P9WN25; -.
DR BMRB; P9WN25; -.
DR SMR; P9WN25; -.
DR STRING; 83332.Rv1542c; -.
DR DrugBank; DB03317; Ferroheme C.
DR DrugBank; DB01826; N-Butyl Isocyanide.
DR PaxDb; P9WN25; -.
DR DNASU; 886402; -.
DR GeneID; 45425525; -.
DR GeneID; 886402; -.
DR KEGG; mtu:Rv1542c; -.
DR TubercuList; Rv1542c; -.
DR eggNOG; COG2346; Bacteria.
DR OMA; HQTQFIS; -.
DR PhylomeDB; P9WN25; -.
DR Reactome; R-HSA-1222538; Tolerance by Mtb to nitric oxide produced by macrophages.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0020037; F:heme binding; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008941; F:nitric oxide dioxygenase activity; IDA:MTBBASE.
DR GO; GO:0019825; F:oxygen binding; IDA:MTBBASE.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0051410; P:detoxification of nitrogen compound; IDA:MTBBASE.
DR GO; GO:0046210; P:nitric oxide catabolic process; IMP:MTBBASE.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR019795; Globin_bac-like_CS.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR InterPro; IPR016339; Hemoglobin_trunc_I.
DR Pfam; PF01152; Bac_globin; 1.
DR PIRSF; PIRSF002030; Globin_Protozoa/Cyanobacteria; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01213; GLOBIN_FAM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT CHAIN 1..136
FT /note="Group 1 truncated hemoglobin GlbN"
FT /id="PRO_0000162640"
FT BINDING 81
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:2GKM"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:5AB8"
FT HELIX 21..38
FT /evidence="ECO:0007829|PDB:5AB8"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:5AB8"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:5AB8"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:5AB8"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:5AB8"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:5AB8"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:5AB8"
SQ SEQUENCE 136 AA; 14449 MW; B75D01A45BC064BB CRC64;
MGLLSRLRKR EPISIYDKIG GHEAIEVVVE DFYVRVLADD QLSAFFSGTN MSRLKGKQVE
FFAAALGGPE PYTGAPMKQV HQGRGITMHH FSLVAGHLAD ALTAAGVPSE TITEILGVIA
PLAVDVTSGE STTAPV
