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P12013 (6PGDH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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, NAD(+)-dependent, decarboxylating
EC=1.1.1.343
Gene names
Name:gntZ
Ordered Locus Names:BSU40080
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
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 NAD to NADH. Does not contribute to oxidative pentose phosphate (PP) pathway fluxes during growth on glucose. The functional role of GntZ remains obscure. Ref.5 Ref.6

Catalytic activity

6-phospho-D-gluconate + NAD+ = D-ribulose 5-phosphate + CO2 + NADH. Ref.6

Subunit structure

Homodimer By similarity.

Disruption phenotype

Cells lacking this gene exhibit no detectable phenotype on glucose as the sole carbon source, and they grow normally on gluconate. Ref.6

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family.

Ontologies

Keywords
   Biological processGluconate utilization
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processD-gluconate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

phosphogluconate dehydrogenase (decarboxylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4684686-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating
PRO_0000090026

Regions

Nucleotide binding9 – 146NAD By similarity
Nucleotide binding32 – 343NAD By similarity
Nucleotide binding73 – 753NAD By similarity
Region127 – 1293Substrate binding By similarity
Region184 – 1852Substrate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Active site1881Proton donor By similarity
Binding site1011NAD By similarity
Binding site1011Substrate By similarity
Binding site1891Substrate By similarity
Binding site2591Substrate; via amide nitrogen By similarity
Binding site2861Substrate By similarity
Binding site4451Substrate; shared with dimeric partner By similarity
Binding site4511Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
P12013 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 56D88BEB8E553856

FASTA46851,983
        10         20         30         40         50         60 
MFNSIGVIGL GVMGSNIALN MANKGENVAV YNYTRDLTDQ LIQKLDGQSL SPYYELEDFV 

        70         80         90        100        110        120 
QSLEKPRKIF LMVTAGKPVD SVIQSLKPLL EEGDVIMDGG NSHYEDTERR YDELKEKGIG 

       130        140        150        160        170        180 
YLGVGISGGE VGALTGPSIM PGGDRDVYEK AAPILTKIAA QVGDDPCCVY IGPKGAGHFT 

       190        200        210        220        230        240 
KMVHNGIEYA DMQLIAEAYT FLRETLRLPL DEIASIFETW NQGELKSYLI EITAEILRKK 

       250        260        270        280        290        300 
DEKTGQPLID VILDKTGQKG TGKWTSMQAI DNGIPSTIIT ESLFARYLSS LKEERMAAQD 

       310        320        330        340        350        360 
VLAGPEAEEK HLDKDTWIEY VRQALYMGKV CAYAQGFAQY KMSSELYGWN LPLKDIALIF 

       370        380        390        400        410        420 
RGGCIIRADF LNVISEAFSE QPNLANLLIA PYFTDKLHAY QTGLRKVVCE GISTGISFPC 

       430        440        450        460 
LTTALSYYDG YRTGRSNANL LQAQRDYFGA HTYERTDMDG VFHTNWSE

« Hide

References

« Hide 'large scale' references
[1]"Organization and transcription of the gluconate operon, gnt, of Bacillus subtilis."
Fujita Y., Fujita T., Miwa Y., Nihashi J., Aratani Y.
J. Biol. Chem. 261:13744-13753(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome between the gnt and iol operons."
Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.
DNA Res. 2:61-69(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / BGSC1A1.
[3]"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.
[4]"Sequence analysis of the 36-kb region between gntZ and trnY genes of Bacillus subtilis genome."
Kasahara Y., Nakai S., Ogasawara N.
DNA Res. 4:155-159(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 460-468.
Strain: 168.
[5]"Analysis of the gluconate (gnt) operon of Bacillus subtilis."
Reizer A., Deutscher J., Saier M.H. Jr., Reizer J.
Mol. Microbiol. 5:1081-1089(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE FUNCTION.
[6]"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, DISRUPTION PHENOTYPE.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J02584 Genomic DNA. Translation: AAA56927.1.
AB005554 Genomic DNA. Translation: BAA21576.1.
AL009126 Genomic DNA. Translation: CAB16045.1.
D78193 Genomic DNA. Translation: BAA11267.1.
PIRD26190.
RefSeqNP_391888.1. NC_000964.3.

3D structure databases

ProteinModelPortalP12013.
SMRP12013. Positions 1-468.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU40080.

Proteomic databases

PaxDbP12013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB16045; CAB16045; BSU40080.
GeneID937716.
KEGGbsu:BSU40080.
PATRIC18980086. VBIBacSub10457_4205.

Organism-specific databases

GenoListBSU40080. [Micado]

Phylogenomic databases

eggNOGCOG0362.
HOGENOMHOG000255147.
KOK00033.
OMADIALIFR.
ProtClustDBPRK09287.

Enzyme and pathway databases

BioCycBSUB:BSU40080-MONOMER.

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 name6PGDH_BACSU
AccessionPrimary (citable) accession number: P12013
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 1, 2013
This is version 109 of the entry and version 1 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

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