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)

P80859

- 6PGD_BACSU

UniProt

P80859 - 6PGD_BACSU

Protein

6-phosphogluconate dehydrogenase, NADP(+)-dependent, decarboxylating

Gene

gndA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH. Is the predominant 6-P-gluconate dehydrogenase isoenzyme in B.subtilis during growth on glucose and gluconate.1 Publication

    Catalytic activityi

    6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei102 – 1021NADPBy similarity
    Binding sitei102 – 1021SubstrateBy similarity
    Active sitei182 – 1821Proton acceptorBy similarity
    Active sitei189 – 1891Proton donorBy similarity
    Binding sitei190 – 1901SubstrateBy similarity
    Binding sitei260 – 2601Substrate; via amide nitrogenBy similarity
    Binding sitei287 – 2871SubstrateBy similarity
    Binding sitei446 – 4461Substrate; shared with dimeric partnerBy similarity
    Binding sitei452 – 4521Substrate; shared with dimeric partnerBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 156NADPBy similarity
    Nucleotide bindingi33 – 353NADPBy similarity
    Nucleotide bindingi74 – 763NADPBy similarity

    GO - Molecular functioni

    1. NADP binding Source: InterPro
    2. phosphogluconate dehydrogenase (decarboxylating) activity Source: UniProtKB-EC

    GO - Biological processi

    1. D-gluconate metabolic process Source: UniProtKB-KW
    2. pentose-phosphate shunt Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Gluconate utilization, Pentose shunt

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciBSUB:BSU23860-MONOMER.
    MetaCyc:MONOMER-6842.
    RETL1328306-WGS:GSTH-2489-MONOMER.
    BRENDAi1.1.1.44. 700.
    UniPathwayiUPA00115; UER00410.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-phosphogluconate dehydrogenase, NADP(+)-dependent, decarboxylating (EC:1.1.1.44)
    Alternative name(s):
    GNTZII
    Gene namesi
    Name:gndA
    Synonyms:yqjI
    Ordered Locus Names:BSU23860
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU23860. [Micado]

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene exhibit a reduced growth on glucose as the sole carbon source, and they do not use the pentose phosphate (PP) pathway at all.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 4694686-phosphogluconate dehydrogenase, NADP(+)-dependent, decarboxylatingPRO_0000090027Add
    BLAST

    Proteomic databases

    PaxDbiP80859.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiP80859. 1 interaction.
    MINTiMINT-8364930.
    STRINGi224308.BSU23860.

    Structurei

    3D structure databases

    ProteinModelPortaliP80859.
    SMRiP80859. Positions 1-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni128 – 1303Substrate bindingBy similarity
    Regioni185 – 1862Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0362.
    HOGENOMiHOG000255147.
    KOiK00033.
    OMAiDKDGVFH.
    OrthoDBiEOG6MSS4W.
    PhylomeDBiP80859.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    1.20.5.320. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR006114. 6PGDH_C.
    IPR006113. 6PGDH_decarbox.
    IPR006115. 6PGDH_NADP-bd.
    IPR006184. 6PGdom_BS.
    IPR013328. DH_multihelical.
    IPR012284. Fibritin/6PGD_C-extension.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00393. 6PGD. 1 hit.
    PF03446. NAD_binding_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000109. 6PGD. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR00873. gnd. 1 hit.
    PROSITEiPS00461. 6PGD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P80859-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKQQIGVIG LAVMGKNLAL NIESRGFSVS VYNRSSSKTE EFLQEAKGKN    50
    VVGTYSIEEF VQSLETPRKI LLMVKAGTAT DATIQSLLPH LEKDDILIDG 100
    GNTYYKDTQR RNKELAESGI HFIGTGVSGG EEGALKGPSI MPGGQKEAHE 150
    LVKPILEAIS AKVDGEPCTT YIGPDGAGHY VKMVHNGIEY GDMQLISESY 200
    FILKQVLGLS ADELHEVFAE WNKGELDSYL IEITADIFTK KDEETGKPLV 250
    DVILDKAGQK GTGKWTSQSA LDLGVPLPII TESVFARFIS AMKEERVKAS 300
    GLLSGPEVKP VTENKEELIE AVRKALFMSK ICSYAQGFAQ MKAASEEYNW 350
    DLKYGEIAMI FRGGCIIRAA FLQKIKEAYD REPELDNLLL DSYFKNIVES 400
    YQGALRQVIS LAVAQGVPVP SFSSALAYYD SYRTAVLPAN LIQAQRDYFG 450
    AHTYERTDKE GIFHTEWMK 469
    Length:469
    Mass (Da):51,775
    Last modified:January 23, 2007 - v4
    Checksum:iD0A94E0B4F2250EF
    GO

    Sequence cautioni

    The sequence BAA12615.1 differs from that shown. Reason: Frameshift at position 42.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111L → W AA sequence (PubMed:9298659)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84432 Genomic DNA. Translation: BAA12615.1. Frameshift.
    AL009126 Genomic DNA. Translation: CAB14318.2.
    PIRiA69964.
    RefSeqiNP_390267.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14318; CAB14318; BSU23860.
    GeneIDi938695.
    KEGGibsu:BSU23860.
    PATRICi18976597. VBIBacSub10457_2489.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84432 Genomic DNA. Translation: BAA12615.1 . Frameshift.
    AL009126 Genomic DNA. Translation: CAB14318.2 .
    PIRi A69964.
    RefSeqi NP_390267.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P80859.
    SMRi P80859. Positions 1-469.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P80859. 1 interaction.
    MINTi MINT-8364930.
    STRINGi 224308.BSU23860.

    Proteomic databases

    PaxDbi P80859.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14318 ; CAB14318 ; BSU23860 .
    GeneIDi 938695.
    KEGGi bsu:BSU23860.
    PATRICi 18976597. VBIBacSub10457_2489.

    Organism-specific databases

    GenoListi BSU23860. [Micado ]

    Phylogenomic databases

    eggNOGi COG0362.
    HOGENOMi HOG000255147.
    KOi K00033.
    OMAi DKDGVFH.
    OrthoDBi EOG6MSS4W.
    PhylomeDBi P80859.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00410 .
    BioCyci BSUB:BSU23860-MONOMER.
    MetaCyc:MONOMER-6842.
    RETL1328306-WGS:GSTH-2489-MONOMER.
    BRENDAi 1.1.1.44. 700.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    1.20.5.320. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR006114. 6PGDH_C.
    IPR006113. 6PGDH_decarbox.
    IPR006115. 6PGDH_NADP-bd.
    IPR006184. 6PGdom_BS.
    IPR013328. DH_multihelical.
    IPR012284. Fibritin/6PGD_C-extension.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00393. 6PGD. 1 hit.
    PF03446. NAD_binding_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000109. 6PGD. 1 hit.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR00873. gnd. 1 hit.
    PROSITEi PS00461. 6PGD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
      Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
      Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    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.
    3. "Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence."
      Medigue C., Rose M., Viari A., Danchin A.
      Genome Res. 9:1116-1127(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
      Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
      Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-14.
      Strain: 168 / IS58.
    5. "The Bacillus subtilis yqjI gene encodes the NADP+-dependent 6-P-gluconate dehydrogenase in the pentose phosphate pathway."
      Zamboni N., Fischer E., Laudert D., Aymerich S., Hohmann H.P., Sauer U.
      J. Bacteriol. 186:4528-4534(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ROLE IN PP PATHWAY, GENE NAME, DISRUPTION PHENOTYPE.
      Strain: 168.

    Entry informationi

    Entry namei6PGD_BACSU
    AccessioniPrimary (citable) accession number: P80859
    Secondary accession number(s): P54546
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 111 of the entry and version 4 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. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3