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Reviewed, UniProtKB/Swiss-Prot Q50648 (PANE_MYCTU)

Last modified February 9, 2010. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative 2-dehydropantoate 2-reductase
    EC=1.1.1.169
Alternative name(s):
    Ketopantoate reductase
      Short name=KPA reductase
      Short name=KPR
Gene names
Ordered Locus Names: Rv2573, MT2649
ORF Names: MTCY227.28c
OrganismMycobacterium tuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid By similarity.

Catalytic activity

(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH.

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.

Subcellular location

Cytoplasm Potential.

Miscellaneous

Was identified as a high-confidence drug target.

Sequence similarities

Belongs to the ketopantoate reductase family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function2-dehydropantoate 2-reductase activity

Inferred from electronic annotation. Source: EC

NADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Putative 2-dehydropantoate 2-reductase
PRO_0000157316

Regions

Nucleotide binding9 – 146NADP By similarity

Sites

Active site1771Proton donor By similarity
Binding site1001NADP; via amide nitrogen By similarity
Binding site1001Substrate By similarity
Binding site1811Substrate By similarity
Binding site2461Substrate By similarity
Binding site2581NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q50648-1 [UniParc].

Last modified February 21, 2002. Version 2.
Checksum: BB2782E105F536C8

FASTA29531,033
        10         20         30         40         50         60 
MATGIALVGP GAVGTTVAAL LHKAGYSPLL CGHTPRAGIE LRRDGADPIV VPGPVHTSPR 

        70         80         90        100        110        120 
EVAGPVDVLI LAVKATQNDA ARPWLTRLCD ERTVVAVLQN GVEQVEQVQP HCPSSAVVPA 

       130        140        150        160        170        180 
IVWCSAETQP QGWVRLRGEA ALVVPTGPAA EQFAGLLRGA GATVDCDPDF TTAAWRKLLV 

       190        200        210        220        230        240 
NALAGFMVLS GRRSAMFRRD DVAALSRRYV AECLAVARAE GARLDDDVVD EVVRLVRSAP 

       250        260        270        280        290 
QDMGTSMLAD RAAHRPLEWD LRNGVIVRKA RAHGLATPIS DVLVPLLAAA SDGPG 

« Hide

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: 9634230] [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: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842580 Genomic DNA. Translation: CAB01270.1. Different initiation.
AE000516 Genomic DNA. Translation: AAK46962.1. Different initiation.
PIRD70724.
RefSeqNP_217089.2.
NP_337148.1.

3D structure databases

SMRQ50648. Positions 4-288.
ModBaseSearch...

Genome annotation databases

GeneID888188.
925668.
GenomeReviewsGene locus MT2649 in contig AE000516_GR.
KEGGmtc:MT2649.
mtu:Rv2573.
TIGRMT2649.

Organism-specific databases

TubercuListRv2573.

Phylogenomic databases

HOGENOMHBG668370.
OMADASVWLR.

Enzyme and pathway databases

BRENDA1.1.1.169. 809.

Family and domain databases

InterProIPR008927. 6-PGluconate_DH_C-like.
IPR003710. ApbA.
IPR013752. ApbA_C.
IPR013332. ApbA_N.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHERPTHR21708:SF21. ApbA. 1 hit.
PfamPF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00745. apbA_panE. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANE_MYCTU
AccessionPrimary (citable) accession number: Q50648
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 21, 2002
Last modified: February 9, 2010
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents