Q9KPQ9 (PANE_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-dehydropantoate 2-reductase
EC=1.1.1.169

Alternative name(s):
Ketopantoate reductase
Short name=KPA reductase
Short name=KPR

Gene names

Name:	panE
Ordered Locus Names:	VC_2307

Organism

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]

Taxonomic identifier

243277 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio cholerae › Vibrio cholerae O1 › Vibrio cholerae O1 biovar El Tor

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
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 Reference proteome
Gene Ontology (GO)
Biological_process	pantothenate biosynthetic process Inferred from sequence or structural similarity Ref.1. Source: TIGR
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2-dehydropantoate 2-reductase activity Inferred from sequence or structural similarity Ref.1. Source: TIGR 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 – 296	296	2-dehydropantoate 2-reductase		PRO_0000157306
Regions
	Nucleotide binding	7 – 12	6	NADP By similarity
Sites
	Active site	175	1	Proton donor By similarity
	Binding site	31	1	NADP; via amide nitrogen By similarity
	Binding site	94	1	NADP; via amide nitrogen By similarity
	Binding site	94	1	Substrate By similarity
	Binding site	120	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	179	1	Substrate By similarity
	Binding site	183	1	Substrate By similarity
	Binding site	193	1	Substrate By similarity
	Binding site	242	1	Substrate By similarity
	Binding site	245	1	Substrate By similarity
	Binding site	257	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KPQ9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: A594D8EAFEE5EEAD	FASTA	296	32,201
	10 20 30 40 50 60 MNIVVLGPGA VGSLWALHLH SAGHQVALWS RQAQPTITLQ LDEEAPISFR NQNLDTLIHA 70 80 90 100 110 120 DLLLITVKAW QVEAALQPLL PHLNRETILL FMHNGMGAVE AISESLTHFP VLFATTTHGA 130 140 150 160 170 180 LKATLNQVSH TGFGQTQVGP FNALGARCDF IADVFNHALA PVTWNPEIQQ ALWRKLAVNC 190 200 210 220 230 240 AINPLTAIHQ CANGALVAPE FTPIITAILD EVTAVMQAEA ISGEAEALRD GVYQVIQATA 250 260 270 280 290 ANLSSMHQDV FHRRPTEIDF ITGYVVRKGE QHGIATPVNS ALYQQIKTLE QSWSKA

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF95451.1.
PIR	D82092.
RefSeq	NP_231938.1. NC_002505.1.
3D structure databases
ProteinModelPortal	Q9KPQ9.
ModBase	Search...
Protein-protein interaction databases
STRING	243277.VC2307.
Protocols and materials databases
DNASU	2613103.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF95451; AAF95451; VC_2307.
GeneID	2613103.
KEGG	vch:VC2307.
PATRIC	20083649. VBIVibCho83274_2199.
Phylogenomic databases
eggNOG	COG1893.
KO	K00077.
OMA	CIRDGRC.
ProtClustDB	PRK06522.
Enzyme and pathway databases
UniPathway	UPA00028; UER00004.
Family and domain databases
Gene3D	1.10.1040.10. 1 hit. 3.40.50.720. 1 hit.
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]
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_VIBCH

Accession

Primary (citable) accession number: Q9KPQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2002
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program