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P12013

- 6PGDH_BACSU

UniProt

P12013 - 6PGDH_BACSU

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Protein
6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating
Gene
gntZ, BSU40080
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

6-phospho-D-gluconate + NAD+ = D-ribulose 5-phosphate + CO2 + NADH.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011NAD By similarity
Binding sitei101 – 1011Substrate By similarity
Active sitei181 – 1811Proton acceptor By similarity
Active sitei188 – 1881Proton donor By similarity
Binding sitei189 – 1891Substrate By similarity
Binding sitei259 – 2591Substrate; via amide nitrogen By similarity
Binding sitei286 – 2861Substrate By similarity
Binding sitei445 – 4451Substrate; shared with dimeric partner By similarity
Binding sitei451 – 4511Substrate; shared with dimeric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146NAD By similarity
Nucleotide bindingi32 – 343NAD By similarity
Nucleotide bindingi73 – 753NAD By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. D-gluconate metabolic process Source: UniProtKB-KW
  2. pentose-phosphate shunt Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Gluconate utilization

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciBSUB:BSU40080-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating (EC:1.1.1.343)
Gene namesi
Name:gntZ
Ordered Locus Names:BSU40080
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU40080. [Micado]

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene exhibit no detectable phenotype on glucose as the sole carbon source, and they grow normally on gluconate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4684686-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating
PRO_0000090026Add
BLAST

Proteomic databases

PaxDbiP12013.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

STRINGi224308.BSU40080.

Structurei

3D structure databases

ProteinModelPortaliP12013.
SMRiP12013. Positions 1-468.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 1293Substrate binding By similarity
Regioni184 – 1852Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0362.
HOGENOMiHOG000255147.
KOiK00033.
OMAiHYEDTER.
OrthoDBiEOG6MSS4W.
PhylomeDBiP12013.

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.

P12013-1 [UniParc]FASTAAdd to Basket

« Hide

MFNSIGVIGL GVMGSNIALN MANKGENVAV YNYTRDLTDQ LIQKLDGQSL    50
SPYYELEDFV QSLEKPRKIF LMVTAGKPVD SVIQSLKPLL EEGDVIMDGG 100
NSHYEDTERR YDELKEKGIG YLGVGISGGE VGALTGPSIM PGGDRDVYEK 150
AAPILTKIAA QVGDDPCCVY IGPKGAGHFT KMVHNGIEYA DMQLIAEAYT 200
FLRETLRLPL DEIASIFETW NQGELKSYLI EITAEILRKK DEKTGQPLID 250
VILDKTGQKG TGKWTSMQAI DNGIPSTIIT ESLFARYLSS LKEERMAAQD 300
VLAGPEAEEK HLDKDTWIEY VRQALYMGKV CAYAQGFAQY KMSSELYGWN 350
LPLKDIALIF RGGCIIRADF LNVISEAFSE QPNLANLLIA PYFTDKLHAY 400
QTGLRKVVCE GISTGISFPC LTTALSYYDG YRTGRSNANL LQAQRDYFGA 450
HTYERTDMDG VFHTNWSE 468
Length:468
Mass (Da):51,983
Last modified:October 1, 1989 - v1
Checksum:i56D88BEB8E553856
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02584 Genomic DNA. Translation: AAA56927.1.
AB005554 Genomic DNA. Translation: BAA21576.1.
AL009126 Genomic DNA. Translation: CAB16045.1.
D78193 Genomic DNA. Translation: BAA11267.1.
PIRiD26190.
RefSeqiNP_391888.1. NC_000964.3.
WP_003243876.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB16045; CAB16045; BSU40080.
GeneIDi937716.
KEGGibsu:BSU40080.
PATRICi18980086. VBIBacSub10457_4205.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02584 Genomic DNA. Translation: AAA56927.1 .
AB005554 Genomic DNA. Translation: BAA21576.1 .
AL009126 Genomic DNA. Translation: CAB16045.1 .
D78193 Genomic DNA. Translation: BAA11267.1 .
PIRi D26190.
RefSeqi NP_391888.1. NC_000964.3.
WP_003243876.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali P12013.
SMRi P12013. Positions 1-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU40080.

Proteomic databases

PaxDbi P12013.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB16045 ; CAB16045 ; BSU40080 .
GeneIDi 937716.
KEGGi bsu:BSU40080.
PATRICi 18980086. VBIBacSub10457_4205.

Organism-specific databases

GenoListi BSU40080. [Micado ]

Phylogenomic databases

eggNOGi COG0362.
HOGENOMi HOG000255147.
KOi K00033.
OMAi HYEDTER.
OrthoDBi EOG6MSS4W.
PhylomeDBi P12013.

Enzyme and pathway databases

BioCyci BSUB:BSU40080-MONOMER.

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

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry namei6PGDH_BACSU
AccessioniPrimary (citable) accession number: P12013
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 3, 2014
This is version 115 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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