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P80859 (6PGD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phosphogluconate dehydrogenase, NADP(+)-dependent, decarboxylating
EC=1.1.1.44
Alternative name(s):
GNTZII
Gene names
Name:gndA
Synonyms:yqjI
Ordered Locus Names:BSU23860
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

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

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3. Ref.5

Subunit structure

Homodimer By similarity.

Disruption phenotype

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. Ref.5

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 4694686-phosphogluconate dehydrogenase, NADP(+)-dependent, decarboxylating
PRO_0000090027

Regions

Nucleotide binding10 – 156NADP By similarity
Nucleotide binding33 – 353NADP By similarity
Nucleotide binding74 – 763NADP By similarity
Region128 – 1303Substrate binding By similarity
Region185 – 1862Substrate binding By similarity

Sites

Active site1821Proton acceptor By similarity
Active site1891Proton donor By similarity
Binding site1021NADP By similarity
Binding site1021Substrate By similarity
Binding site1901Substrate By similarity
Binding site2601Substrate; via amide nitrogen By similarity
Binding site2871Substrate By similarity
Binding site4461Substrate; shared with dimeric partner By similarity
Binding site4521Substrate; shared with dimeric partner By similarity

Experimental info

Sequence conflict111L → W AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
P80859 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: D0A94E0B4F2250EF

FASTA46951,775
        10         20         30         40         50         60 
MSKQQIGVIG LAVMGKNLAL NIESRGFSVS VYNRSSSKTE EFLQEAKGKN VVGTYSIEEF 

        70         80         90        100        110        120 
VQSLETPRKI LLMVKAGTAT DATIQSLLPH LEKDDILIDG GNTYYKDTQR RNKELAESGI 

       130        140        150        160        170        180 
HFIGTGVSGG EEGALKGPSI MPGGQKEAHE LVKPILEAIS AKVDGEPCTT YIGPDGAGHY 

       190        200        210        220        230        240 
VKMVHNGIEY GDMQLISESY FILKQVLGLS ADELHEVFAE WNKGELDSYL IEITADIFTK 

       250        260        270        280        290        300 
KDEETGKPLV DVILDKAGQK GTGKWTSQSA LDLGVPLPII TESVFARFIS AMKEERVKAS 

       310        320        330        340        350        360 
GLLSGPEVKP VTENKEELIE AVRKALFMSK ICSYAQGFAQ MKAASEEYNW DLKYGEIAMI 

       370        380        390        400        410        420 
FRGGCIIRAA FLQKIKEAYD REPELDNLLL DSYFKNIVES YQGALRQVIS LAVAQGVPVP 

       430        440        450        460 
SFSSALAYYD SYRTAVLPAN LIQAQRDYFG AHTYERTDKE GIFHTEWMK

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D84432 Genomic DNA. Translation: BAA12615.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB14318.2.
PIRA69964.
RefSeqNP_390267.2. NC_000964.3.

3D structure databases

ProteinModelPortalP80859.
SMRP80859. Positions 1-469.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU23860.

Proteomic databases

PaxDbP80859.
PRIDEP80859.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14318; CAB14318; BSU23860.
GeneID938695.
KEGGbsu:BSU23860.
PATRIC18976597. VBIBacSub10457_2489.

Organism-specific databases

GenoListBSU23860. [Micado]

Phylogenomic databases

eggNOGCOG0362.
HOGENOMHOG000255147.
KOK00033.
OMAKQQIGVI.
ProtClustDBPRK09287.

Enzyme and pathway databases

BioCycBSUB:BSU23860-MONOMER.
MetaCyc:MONOMER-6842.
BRENDA1.1.1.44. 700.
UniPathwayUPA00115; UER00410.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 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]
PfamPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFPIRSF000109. 6PGD. 1 hit.
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMsTIGR00873. gnd. 1 hit.
PROSITEPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name6PGD_BACSU
AccessionPrimary (citable) accession number: P80859
Secondary accession number(s): P54546
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 104 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents