Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P37402

- PANE_SALTY

UniProt

P37402 - PANE_SALTY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

2-dehydropantoate 2-reductase

Gene

panE

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. Has a strong preference for NADPH over NADH as the electron acceptor. Pantoate, ketoisovalerate, oxaloacetate, pyruvate, 3-hydroxypyruvate, alpha-ketoglutarate, alpha-ketobutyrate, and acetaldehyde can not served as substrates for reduction.1 Publication

Catalytic activityi

(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH.1 Publication

Kineticsi

  1. KM=0.0776 mM for NADPH1 Publication
  2. KM=0.0742 mM for 2-dehydropantoate1 Publication

Vmax=89.3 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.25.1 Publication

Temperature dependencei

Optimum temperature is 42 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311NADP; via amide nitrogenBy similarity
Binding sitei98 – 981NADP; via amide nitrogenBy similarity
Binding sitei98 – 981SubstrateBy similarity
Binding sitei122 – 1221NADP; via amide nitrogen and carbonyl oxygenBy similarity
Active sitei176 – 1761Proton donor
Binding sitei180 – 1801SubstrateBy similarity
Binding sitei184 – 1841SubstrateBy similarity
Binding sitei194 – 1941SubstrateBy similarity
Binding sitei241 – 2411SubstrateBy similarity
Binding sitei244 – 2441SubstrateBy similarity
Binding sitei256 – 2561NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 126NADPBy similarity

GO - Molecular functioni

  1. 2-dehydropantoate 2-reductase activity Source: UniProtKB-EC
  2. NADP binding Source: InterPro

GO - Biological processi

  1. pantothenate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciSENT99287:GCTI-435-MONOMER.
UniPathwayiUPA00028; UER00004.

Names & Taxonomyi

Protein namesi
Recommended name:
2-dehydropantoate 2-reductase (EC:1.1.1.169)
Alternative name(s):
Ketopantoate reductase
Short name:
KPA reductase
Short name:
KPR
Gene namesi
Name:panE
Synonyms:apbA
Ordered Locus Names:STM0434
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3033032-dehydropantoate 2-reductasePRO_0000157304Add
BLAST

Proteomic databases

PaxDbiP37402.
PRIDEiP37402.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM0434.

Structurei

3D structure databases

ProteinModelPortaliP37402.
SMRiP37402. Positions 1-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ketopantoate reductase family.Curated

Phylogenomic databases

eggNOGiCOG1893.
HOGENOMiHOG000050223.
KOiK00077.
OMAiIEFINGW.
OrthoDBiEOG68SVW3.
PhylomeDBiP37402.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR003710. ApbA.
IPR013328. DH_multihelical.
IPR013752. KPA_reductase.
IPR013332. KPR_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR00745. apbA_panE. 1 hit.

Sequencei

Sequence statusi: Complete.

P37402-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKITVLGCGA LGQLWLSALC KHGHDVQGWL RVPQPYCSVN LIDTDGSFFN
60 70 80 90 100
ESLTANDPDF LAKSELLLVT LKAWQVSDAV RTLASTLPVT SPILLIHNGM
110 120 130 140 150
GTIEELQNIQ QPMLMGTITH AARRDGNIII HVANGTTHIG PAREQDGDYS
160 170 180 190 200
YLADILQGVL PDVAWHNNIR AEMWRKLAVN CVINPLTALW NCPNGELRHH
210 220 230 240 250
TDEINAICEE VAAVIEREGY HTSADDLRYY VEQVIDSTAE NISSMLQDVR
260 270 280 290 300
AMRHTEIDYI TGYLLKRARV HGLAVPENSR LFEMVKRKES EYERSGTGMP

RPW
Length:303
Mass (Da):33,938
Last modified:January 23, 2002 - v2
Checksum:i060DA21B75B891A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 8613WQVSD…TLAST → GFRRSTNPGVN in AAA56681. (PubMed:7519593)CuratedAdd
BLAST
Sequence conflicti124 – 1241Missing in AAA56681. (PubMed:7519593)Curated
Sequence conflicti246 – 2472LQ → FE in AAA56681. (PubMed:7519593)Curated
Sequence conflicti275 – 30329VPENS…MPRPW → FRKIAACLKW in AAA56681. (PubMed:7519593)CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti121 – 1211A → T in strain: DM4593.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09529 Genomic DNA. Translation: AAA56681.1.
AE006468 Genomic DNA. Translation: AAL19388.1.
PIRiA55849.
RefSeqiNP_459429.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19388; AAL19388; STM0434.
GeneIDi1251953.
KEGGistm:STM0434.
PATRICi32379203. VBISalEnt20916_0463.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09529 Genomic DNA. Translation: AAA56681.1 .
AE006468 Genomic DNA. Translation: AAL19388.1 .
PIRi A55849.
RefSeqi NP_459429.1. NC_003197.1.

3D structure databases

ProteinModelPortali P37402.
SMRi P37402. Positions 1-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM0434.

Proteomic databases

PaxDbi P37402.
PRIDEi P37402.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL19388 ; AAL19388 ; STM0434 .
GeneIDi 1251953.
KEGGi stm:STM0434.
PATRICi 32379203. VBISalEnt20916_0463.

Phylogenomic databases

eggNOGi COG1893.
HOGENOMi HOG000050223.
KOi K00077.
OMAi IEFINGW.
OrthoDBi EOG68SVW3.
PhylomeDBi P37402.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00004 .
BioCyci SENT99287:GCTI-435-MONOMER.

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR008927. 6-PGluconate_DH_C-like.
IPR003710. ApbA.
IPR013328. DH_multihelical.
IPR013752. KPA_reductase.
IPR013332. KPR_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 1 hit.
TIGRFAMsi TIGR00745. apbA_panE. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "apbA, a new genetic locus involved in thiamine biosynthesis in Salmonella typhimurium."
    Downs D.M., Petersen L.
    J. Bacteriol. 176:4858-4864(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway."
    Frodyma M.E., Downs D.M.
    J. Biol. Chem. 273:5572-5576(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  4. "The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is allelic to apbA in Salmonella typhimurium."
    Frodyma M.E., Downs D.M.
    J. Bacteriol. 180:4757-4759(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SHOWS THAT APBA IS PANE.

Entry informationi

Entry nameiPANE_SALTY
AccessioniPrimary (citable) accession number: P37402
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2002
Last modified: October 29, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3