Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

O34661

- PANE_BACSU

UniProt

O34661 - PANE_BACSU

Protein

Probable 2-dehydropantoate 2-reductase

Gene

panE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981NADP; via amide nitrogenBy similarity
    Binding sitei98 – 981SubstrateBy similarity
    Active sitei179 – 1791Proton donorBy similarity
    Binding sitei183 – 1831SubstrateBy similarity
    Binding sitei187 – 1871SubstrateBy similarity
    Binding sitei246 – 2461SubstrateBy similarity
    Binding sitei258 – 2581NADPBy 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-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pantothenate biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciBSUB:BSU15110-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable 2-dehydropantoate 2-reductase (EC:1.1.1.169)
    Alternative name(s):
    Ketopantoate reductase
    Short name:
    KPA reductase
    Gene namesi
    Name:panE
    Synonyms:apbA, ylbQ
    Ordered Locus Names:BSU15110
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU15110. [Micado]

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 298298Probable 2-dehydropantoate 2-reductasePRO_0000157311Add
    BLAST

    Proteomic databases

    PaxDbiO34661.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU15110.

    Structurei

    Secondary structure

    1
    298
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi10 – 2011
    Beta strandi23 – 286
    Helixi32 – 4110
    Beta strandi43 – 475
    Beta strandi50 – 545
    Beta strandi57 – 615
    Beta strandi67 – 715
    Helixi75 – 773
    Helixi78 – 847
    Beta strandi92 – 954
    Beta strandi98 – 1003
    Helixi101 – 1077
    Beta strandi114 – 1207
    Beta strandi123 – 1264
    Beta strandi128 – 1369
    Beta strandi140 – 1445
    Helixi150 – 1534
    Turni154 – 1574
    Beta strandi166 – 1683
    Helixi172 – 19322
    Helixi199 – 2024
    Helixi204 – 22118
    Helixi226 – 23914
    Turni240 – 2423
    Helixi246 – 2538
    Helixi259 – 27214
    Helixi278 – 28912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EGOX-ray1.90A/B2-297[»]
    ProteinModelPortaliO34661.
    SMRiO34661. Positions 10-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO34661.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ketopantoate reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG1893.
    HOGENOMiHOG000050222.
    KOiK00077.
    OMAiQEVAFLI.
    OrthoDBiEOG68SVW3.
    PhylomeDBiO34661.

    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.

    O34661-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIGIIGGGS VGLLCAYYLS LYHDVTVVTR RQEQAAAIQS EGIRLYKGGE    50
    EFRADCSADT SINSDFDLLV VTVKQHQLQS VFSSLERIGK TNILFLQNGM 100
    GHIHDLKDWH VGHSIYVGIV EHGAVRKSDT AVDHTGLGAI KWSAFDDAEP 150
    DRLNILFQHN HSDFPIYYET DWYRLLTGKL IVNACINPLT ALLQVKNGEL 200
    LTTPAYLAFM KLVFQEACRI LKLENEEKAW ERVQAVCGQT KENRSSMLVD 250
    VIGGRQTEAD AIIGYLLKEA SLQGLDAVHL EFLYGSIKAL ERNTNKVF 298
    Length:298
    Mass (Da):33,287
    Last modified:January 1, 1998 - v1
    Checksum:iA0B645A0A415FFD5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z98682 Genomic DNA. Translation: CAB11364.1.
    AL009126 Genomic DNA. Translation: CAB13384.1.
    PIRiF69875.
    RefSeqiNP_389394.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13384; CAB13384; BSU15110.
    GeneIDi936782.
    KEGGibsu:BSU15110.
    PATRICi18974827. VBIBacSub10457_1605.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z98682 Genomic DNA. Translation: CAB11364.1 .
    AL009126 Genomic DNA. Translation: CAB13384.1 .
    PIRi F69875.
    RefSeqi NP_389394.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EGO X-ray 1.90 A/B 2-297 [» ]
    ProteinModelPortali O34661.
    SMRi O34661. Positions 10-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU15110.

    Proteomic databases

    PaxDbi O34661.

    Protocols and materials databases

    DNASUi 936782.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13384 ; CAB13384 ; BSU15110 .
    GeneIDi 936782.
    KEGGi bsu:BSU15110.
    PATRICi 18974827. VBIBacSub10457_1605.

    Organism-specific databases

    GenoListi BSU15110. [Micado ]

    Phylogenomic databases

    eggNOGi COG1893.
    HOGENOMi HOG000050222.
    KOi K00077.
    OMAi QEVAFLI.
    OrthoDBi EOG68SVW3.
    PhylomeDBi O34661.

    Enzyme and pathway databases

    BioCyci BSUB:BSU15110-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O34661.

    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

    1. "Bacillus subtilis chromosomal region downstream nprE."
      Bertero M., Presecan E., Glaser P., Richou A., Danchin A.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.

    Entry informationi

    Entry nameiPANE_BACSU
    AccessioniPrimary (citable) accession number: O34661
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3