Q50648 (PANE_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Protein existence	Inferred 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.
Sequence caution	The sequence AAK46962.1 differs from that shown. Reason: Erroneous initiation. The sequence CAB01270.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: MTBBASE
Molecular function	2-dehydropantoate 2-reductase activity Inferred from electronic annotation. Source: EC NADP binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 295	295	Putative 2-dehydropantoate 2-reductase		PRO_0000157316
Regions
	Nucleotide binding	9 – 14	6	NADP By similarity
Sites
	Active site	177	1	Proton donor By similarity
	Binding site	100	1	NADP; via amide nitrogen By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	181	1	Substrate By similarity
	Binding site	246	1	Substrate By similarity
	Binding site	258	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q50648 [UniParc]. Last modified February 21, 2002. Version 2. Checksum: BB2782E105F536C8	FASTA	295	31,033
	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

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. , 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. , 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.
PIR	D70724.
RefSeq	NP_337148.1. NC_002755.2.
3D structure databases
ProteinModelPortal	Q50648.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000001858; EBMYCP00000001858; EBMYCG00000001856. EBMYCT00000072589; EBMYCP00000070648; EBMYCG00000072584.
GeneID	925668.
GenomeReviews	Gene locus MT2649 in contig AE000516_GR. Gene locus Rv2573 in contig AL123456_GR.
KEGG	mtc:MT2649. mtu:Rv2573.
PATRIC	18127572. VBIMycTub22151_2889.
TIGR	MT2649.
Organism-specific databases
TubercuList	Rv2573.
Phylogenomic databases
GeneTree	EBGT00050000015800.
HOGENOM	HBG668370.
OMA	VCALQNG.
ProtClustDB	PRK06522.
Family and domain databases
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR003710. ApbA. IPR013752. ApbA_C. IPR013332. ApbA_N. IPR013328. DH_multihelical. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KO	K00077.
Pfam	PF02558. ApbA. 1 hit. PF08546. ApbA_C. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMs	TIGR00745. ApbA_panE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANE_MYCTU

Accession

Primary (citable) accession number: Q50648

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 21, 2002
Last modified:	January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program