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Q987N5 (PANE_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:mll6982
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length326 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.

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_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2-dehydropantoate 2-reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NADP binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Putative 2-dehydropantoate 2-reductase
PRO_0000157317

Regions

Nucleotide binding7 – 126NADP By similarity

Sites

Active site2051Proton donor By similarity
Binding site1031NADP; via amide nitrogen By similarity
Binding site1031Substrate By similarity
Binding site2091Substrate By similarity
Binding site2131Substrate By similarity
Binding site2741Substrate By similarity
Binding site2861NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q987N5 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: E1C28123762ACFD2

FASTA32634,712
        10         20         30         40         50         60 
MKITIFGAGA IGGYLAAKLA IAGRTDLSIV ARGAHLEAIQ ANGLRLIEDG EESMAPVRAA 

        70         80         90        100        110        120 
AKAEELGAQD YVVLALKAHS LTPALDQIAP LLGDHTSVVT MQNGVPWWYF HGVGGPLEGT 

       130        140        150        160        170        180 
RLNAVDPGGA IWQRIGPQRV IGSVVYPAVE VDAPGLIRHV EGKRFSLGEP SGERSERVTL 

       190        200        210        220        230        240 
LAEEMVKAGL QAPVRDDIRS EIWVKLWGNL SFNPISALTG STLAAIVADE GTRALARTMM 

       250        260        270        280        290        300 
LEAQAIGESL GVRFPIGVDR RIKGAGDVGE HKTSMLQDLE RGRPMEIDAL VSAVQELGRL 

       310        320 
VDKPTPTIDA VLALVRRLAV ERGCYS 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB53168.1.
RefSeqNP_107382.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ987N5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mll6982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB53168; BAB53168; BAB53168.
GeneID1230037.
KEGGmlo:mll6982.
PATRIC22485365. VBIMesLot2464_5562.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050222.
KOK00077.
OMATHATLDV.
OrthoDBEOG63NMHV.

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-5533-MONOMER.
RETL1328306-WGS:GSTH-1747-MONOMER.
UniPathwayUPA00028; UER00004.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013752. ApbA_C.
IPR013332. ApbA_N.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANE_RHILO
AccessionPrimary (citable) accession number: Q987N5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: October 1, 2001
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways