Reviewed, UniProtKB/Swiss-Prot Q50648 (PANE_MYCTU)

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 [Complete proteome] [HAMAP]

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.
Sequence processing	The displayed sequence is not processed.
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.
Sequence similarities	Belongs to the ketopantoate reductase family.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2-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 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)
	Q50648-1 [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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX842580 Genomic DNA. Translation: CAB01270.1. Different initiation. AE000516 Genomic DNA. Translation: AAK46962.1. Different initiation.
PIR	D70724.
RefSeq	NP_217089.2. NP_337148.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	888188. 925668.
GenomeReviews	Gene locus MT2649 in contig AE000516_GR. Gene locus Rv2573 in contig AL123456_GR.
KEGG	mtc:MT2649. mtu:Rv2573.
TIGR	MT2649.
Organism-specific databases
TubercuList	Rv2573.
Phylogenomic databases
HOGENOM	Q50648.
OMA	DASVWLR.
Enzyme and pathway databases
BRENDA	1.1.1.169. 809.
Family and domain databases
InterPro	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.
PANTHER	PTHR21708:SF21. ApbA. 1 hit.
Pfam	PF02558. ApbA. 1 hit. PF08546. ApbA_C. 1 hit. [Graphical view]
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:	November 3, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)