Nitrate reductase-like protein NarX - Mycobacterium tuberculosis

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P71994 (NARX_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nitrate reductase-like protein NarX
EC=1.7.99.4

Gene names

Name:	narX
Ordered Locus Names:	Rv1736c, MT1778

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	652 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Does not seem to have nitrate reductase activity.
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor.
Cofactor	Binds 1 4Fe-4S cluster per subunit Potential. Binds 1 molybdenum ion per subunit Potential. Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit By similarity. Binds 2 heme groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the extracellular interface. Electrons are transferred from the extracellular to the cytoplasmic heme Potential.
Subcellular location	Cell membrane; Multi-pass membrane protein Potential.
Induction	A member of the dormancy regulon. Induced in response to reduced oxygen tension (hypoxia), low levels of nitric oxide (NO) and carbon monoxide (CO). It is hoped that this regulon will give insight into the latent, or dormant phase of infection. Induction by hypoxia is independent of nitrate and nitrate levels. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7
Disruption phenotype	No visible phenotype. Ref.4
Biotechnological use	This protein serves as an immunogenic antigen, inducing gamma-interferon responses in whole-blood cultures from M.tuberculosis-exposed adults in Uganda and South Africa, indicating this might be a good vaccine candidate. Ref.8
Sequence similarities	In the N-terminal section; belongs to the nitrate reductase alpha subunit family. In the central section; belongs to the NarJ/NarW family. In the C-terminal section; belongs to the nitrate reductase gamma subunit family.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	4Fe-4S Heme Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to nitrosative stress Inferred from expression pattern PubMed 12925133. Source: MTBBASE chaperone-mediated protein complex assembly Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW response to hypoxia Inferred from expression pattern Ref.4. Source: MTBBASE
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 652

652

Nitrate reductase-like protein NarX

PRO_0000392915

Regions

Transmembrane

416 – 436

Helical; Potential

Transmembrane

466 – 486

Helical; Potential

Transmembrane

504 – 524

Helical; Potential

Transmembrane

545 – 565

Helical; Potential

Transmembrane

595 – 615

Helical; Potential

Region

1 – 251

251

Nitrate reductase alpha subunit

Region

258 – 415

158

Nitrate reductase delta subunit

Region

416 – 652

237

Nitrate reductase gamma subunit

Sites

Metal binding

Iron-sulfur (4Fe-4S); via pros nitrogen By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

103

Iron-sulfur (4Fe-4S) By similarity

Metal binding

233

Molybdenum By similarity

Metal binding

469

Iron (heme B 1 axial ligand) By similarity

Metal binding

479

Iron (heme B 2 axial ligand) By similarity

Metal binding

602

Iron (heme B 2 axial ligand) By similarity

Metal binding

620

Iron (heme B 1 axial ligand) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P71994 [UniParc].

Last modified July 1, 1997. Version 2.
Checksum: E2D0513A9CB29F3E
Show »

FASTA

652

72,825

        10         20         30         40         50         60 
MTVTPRTGSR IEELLARSGR FFIPGEISAD LRTVTRRGGR DGDVFYRDRW SHDKVVRSTH 

        70         80         90        100        110        120 
GVNCTGSCSW KIYVKDDIIT WETQETDYPS VGPDRPEYEP RGCPRGAAFS WYTYSPTRVR 

       130        140        150        160        170        180 
HPYARGVLVE MYREAKARLG DPVAAWADIQ ADPRRRRRYQ RARGKGGLVR VSWAEATEMI 

       190        200        210        220        230        240 
AAAHVHTIST YGPDRVAGFS PIPAMSMVSH AAGSRFVELI GGVMTSFYDW YADLPVASPQ 

       250        260        270        280        290        300 
VFGDQTDVPE SGDWWDVVWQ CASVLLTYPN SRQLGTAEEL LAHIDGPAAD LLGRTVSELR 

       310        320        330        340        350        360 
RADPLTAATR YVDTFDLRGR ATLYLTYWTA GDTRNRGREM LAFAQTYRST DVAPPRGETP 

       370        380        390        400        410        420 
DFLPVVLEFA ATVDPEAGRR LLSGYRVPIA ALCNALTEAA LPYAHTVAAV CRTGDMMGEL 

       430        440        450        460        470        480 
FWTVVPYVTM TIVAVGSWWR YRYDKFGWTT RSSQLYESRL LRIASPMFHF GILVVIVGHG 

       490        500        510        520        530        540 
IGLVIPQSWT QAAGLSEGAY HVQAVVLGSI AGITTLAGVT LLIYRRRTRG PVFMATTVND 

       550        560        570        580        590        600 
KVMYLVLVAA IVAGLGATAL GSGVVGEAYN YRETVSVWFR SVWVLQPRGD LMAEAPLYYQ 

       610        620        630        640        650 
IHVLIGLALF ALWPFTRLVH AFSAPIGYLF RPYIIYRSRE ELVLTRPRRR GW

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." 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. Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin." Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I., Schoolnik G.K. Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY HYPOXIA. Strain: ATCC 25618 / H37Rv.
[4]	"Role of narK2X and narGHJI in hypoxic upregulation of nitrate reduction by Mycobacterium tuberculosis." Sohaskey C.D., Wayne L.G. J. Bacteriol. 185:7247-7256(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LACK OF NITRATE REDUCTASE ACTIVITY, INDUCTION BY HYPOXIA, DISRUPTION PHENOTYPE. Strain: ATCC 25618 / H37Rv.
[5]	"Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program." Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M., Sherman D.R., Schoolnik G.K. J. Exp. Med. 198:705-713(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, DORMANCY REGULON. Strain: 1254, ATCC 25618 / H37Rv and CDC 1551 / Oshkosh.
[6]	"Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection." Shiloh M.U., Manzanillo P., Cox J.S. Cell Host Microbe 3:323-330(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY CARBON MONOXIDE (CO). Strain: ATCC 35801 / TMC 107 / Erdman.
[7]	"Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium tuberculosis dormancy regulon." Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I., Agarwal A., Steyn A.J. J. Biol. Chem. 283:18032-18039(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY CARBON MONOXIDE (CO), DORMANCY REGULON. Strain: ATCC 25618 / H37Rv.
[8]	"Immunogenicity of novel DosR regulon-encoded candidate antigens of Mycobacterium tuberculosis in three high-burden populations in Africa." Black G.F., Thiel B.A., Ota M.O., Parida S.K., Adegbola R., Boom W.H., Dockrell H.M., Franken K.L., Friggen A.H., Hill P.C., Klein M.R., Lalor M.K., Mayanja H., Schoolnik G., Stanley K., Weldingh K., Kaufmann S.H., Walzl G., Ottenhoff T.H. Clin. Vaccine Immunol. 16:1203-1212(2009) [PubMed] [Europe PMC] [Abstract] Cited for: BIOTECHNOLOGY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000516 Genomic DNA. Translation: AAK46051.1. BX842577 Genomic DNA. Translation: CAB03699.1. AL123456 Genomic DNA. Translation: CCP44502.1.
PIR	C70688.
RefSeq	NP_216252.1. NC_000962.3. NP_336237.1. NC_002755.2. YP_006515134.1. NC_018143.1.
3D structure databases
HSSP	HSSP built from PDB template 1Q16 based on UniProtKB P11350.
ProteinModelPortal	P71994.
SMR	P71994. Positions 40-256, 420-639.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv1736c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK46051; AAK46051; MT1778.
GeneID	13316525. 885213. 923930.
KEGG	mtc:MT1778. mtu:Rv1736c. mtv:RVBD_1736c.
PATRIC	18125664. VBIMycTub22151_1945.
Organism-specific databases
TubercuList	Rv1736c.
Phylogenomic databases
eggNOG	COG5013.
HOGENOM	HOG000220446.
KO	K00369.
ProtClustDB	CLSK791361.
Family and domain databases
InterPro	IPR020945. DMSO/NO3_reduct_chaperone. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR006655. Mopterin_OxRdtase_prok_CS. IPR023234. NarG-like_domain. IPR003816. Nitrate_red_gam. IPR003765. NO3_reductase_chaperone_NarJ. [Graphical view]
Pfam	PF00384. Molybdopterin. 1 hit. PF02613. Nitrate_red_del. 1 hit. PF02665. Nitrate_red_gam. 1 hit. [Graphical view]
SMART	SM00926. Molybdop_Fe4S4. 1 hit. [Graphical view]
SUPFAM	SSF103501. NarG-like_domain. 1 hit.
TIGRFAMs	TIGR00351. narI. 1 hit. TIGR00684. narJ. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. 1 hit. PS00932. MOLYBDOPTERIN_PROK_3. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NARX_MYCTU

Accession

Primary (citable) accession number: P71994
Secondary accession number(s): L0T7S1, Q7D821

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents