Reviewed, UniProtKB/Swiss-Prot Q8Y5L2 (PANE_LISMO)

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:

lmo2046

Organism

Listeria monocytogenes [Complete proteome] [HAMAP]

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	297 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.
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 – 297	297	Putative 2-dehydropantoate 2-reductase		PRO_0000157315
Regions
	Nucleotide binding	11 – 16	6	NADP By similarity
Sites
	Active site	187	1	Proton donor By similarity
	Binding site	107	1	NADP; via amide nitrogen By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	191	1	Substrate By similarity
	Binding site	195	1	Substrate By similarity
	Binding site	251	1	Substrate By similarity
	Binding site	263	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y5L2-1 [UniParc]. Last modified February 21, 2002. Version 1. Checksum: BCC1A6992EA9AD8D	FASTA	297	33,042
	10 20 30 40 50 60 MANQLKVGII GAGAMGLLYA ANFANISELT LFTRRKEQSD LLNQKGLSLK DNSELKNIHI 70 80 90 100 110 120 QATVITDAEK LSEQELLIIA VKQYSLKTIL PLLRSIPERV PLLFIQNGAA HLDSMPLLGN 130 140 150 160 170 180 KRTILLGISE HGAGREDDTT VIWRGHGRTK YSIYQGELNE AVIKILDSNP DFPVEKHASY 190 200 210 220 230 240 LDIINEKLFI NAVINPLTAV LQVQNGKLLE NKEWHELLKT IVKEIQTVLP VENALEKVEV 250 260 270 280 290 ICQVTATNFS SMALDRMNNR MTEIDGIVLP ILEKGESLPT LHALYHLIKG LEGESDV

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591982 Genomic DNA. Translation: CAD00124.1.
PIR	AF1330.
RefSeq	NP_465570.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	986332.
KEGG	lmo:lmo2046.
Organism-specific databases
ListiList	LMO02046.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG668370.
OMA	ELKNIHI.
Enzyme and pathway databases
BioCyc	LMON169963:LMO2046-MONOMER.
BRENDA	1.1.1.169. 96770.
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.
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_LISMO

Accession

Primary (citable) accession number: Q8Y5L2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2002
Last sequence update:	February 21, 2002
Last modified:	February 9, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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