Skip Header

Contribute Send feedback
Read comments (?) or add your own

O06594 (NADC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicotinate-nucleotide pyrophosphorylase [carboxylating]

EC=2.4.2.19
Alternative name(s):
Quinolinate phosphoribosyltransferase [decarboxylating]
Short name=QAPRTase
Gene names
Name:nadC
Ordered Locus Names:Rv1596, MT1632
ORF Names:MTCY336.08c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the catabolism of quinolinic acid (QA) By similarity.

Catalytic activity

Beta-nicotinate D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.

Subunit structure

Homodimer. Hexamer formed by 3 homodimers. Ref.3

Sequence similarities

Belongs to the NadC/ModD family.

Sequence caution

The sequence AAK45900.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Nicotinate-nucleotide pyrophosphorylase [carboxylating]
PRO_0000155946

Regions

Region138 – 1403Substrate binding
Region248 – 2503Substrate binding
Region269 – 2713Substrate binding

Sites

Binding site1051Substrate
Binding site1621Substrate
Binding site1721Substrate
Binding site2011Substrate
Binding site2221Substrate

Secondary structure

............................................... 285
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O06594 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 45DE3335EC1C522F

FASTA28529,951
        10         20         30         40         50         60 
MGLSDWELAA ARAAIARGLD EDLRYGPDVT TLATVPASAT TTASLVTREA GVVAGLDVAL 

        70         80         90        100        110        120 
LTLNEVLGTN GYRVLDRVED GARVPPGEAL MTLEAQTRGL LTAERTMLNL VGHLSGIATA 

       130        140        150        160        170        180 
TAAWVDAVRG TKAKIRDTRK TLPGLRALQK YAVRTGGGVN HRLGLGDAAL IKDNHVAAAG 

       190        200        210        220        230        240 
SVVDALRAVR NAAPDLPCEV EVDSLEQLDA VLPEKPELIL LDNFAVWQTQ TAVQRRDSRA 

       250        260        270        280 
PTVMLESSGG LSLQTAATYA ETGVDYLAVG ALTHSVRVLD IGLDM 

« Hide

References

« Hide '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. expand/collapse author list , 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.
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. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., 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]"Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential tb drug target."
Sharma V., Grubmeyer C., Sacchettini J.C.
Structure 6:1587-1599(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842577 Genomic DNA. Translation: CAB09073.1.
AE000516 Genomic DNA. Translation: AAK45900.1. Different initiation.
AL123456 Genomic DNA. Translation: CCP44360.1.
PIRF70543.
RefSeqNP_216112.1. NC_000962.3.
NP_336086.1. NC_002755.2.
YP_006514985.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QPNX-ray2.60A/B/C/D/E/F2-285[»]
1QPOX-ray2.40A/B/C/D/E/F2-285[»]
1QPQX-ray2.45A/B/C/D/E/F2-285[»]
1QPRX-ray2.45A/B/C/D/E/F2-285[»]
ProteinModelPortalO06594.
SMRO06594. Positions 2-285.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv1596.

Proteomic databases

PaxDbO06594.
PRIDEO06594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK45900; AAK45900; MT1632.
GeneID13316374.
886281.
924304.
KEGGmtc:MT1632.
mtu:Rv1596.
mtv:RVBD_1596.
PATRIC18125352. VBIMycTub22151_1791.

Organism-specific databases

TubercuListRv1596.

Phylogenomic databases

eggNOGCOG0157.
HOGENOMHOG000224022.
KOK00767.
OMAAVTCGGC.
ProtClustDBPRK07896.

Enzyme and pathway databases

UniPathwayUPA00253; UER00331.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.90.1170.20. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR004393. NadC.
IPR027277. NadC/ModD.
IPR002638. Quinolinate_PRibosylTrfase_C.
IPR022412. Quinolinate_PRibosylTrfase_N.
[Graphical view]
PfamPF01729. QRPTase_C. 1 hit.
PF02749. QRPTase_N. 1 hit.
[Graphical view]
PIRSFPIRSF006250. NadC_ModD. 1 hit.
SUPFAMSSF51690. Q_phspho_trans. 1 hit.
TIGRFAMsTIGR00078. nadC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO06594.

Entry information

Entry nameNADC_MYCTU
AccessionPrimary (citable) accession number: O06594
Secondary accession number(s): L0T8R5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families