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Protein

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

Gene

gntZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei101NADBy similarity1
Binding sitei101SubstrateBy similarity1
Active sitei181Proton acceptorBy similarity1
Active sitei188Proton donorBy similarity1
Binding sitei189SubstrateBy similarity1
Binding sitei259Substrate; via amide nitrogenBy similarity1
Binding sitei286SubstrateBy similarity1
Binding sitei445Substrate; shared with dimeric partnerBy similarity1
Binding sitei451Substrate; shared with dimeric partnerBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi9 – 14NADBy similarity6
Nucleotide bindingi32 – 34NADBy similarity3
Nucleotide bindingi73 – 75NADBy similarity3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Gluconate utilization

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciBSUB:BSU40080-MONOMER.
BRENDAi1.1.1.343. 658.

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
Proteomesi
  • UP000001570 Componenti: Chromosome

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000900261 – 4686-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylatingAdd BLAST468

Proteomic databases

PaxDbiP12013.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021616.

Structurei

3D structure databases

ProteinModelPortaliP12013.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni127 – 129Substrate bindingBy similarity3
Regioni184 – 185Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C7Q. Bacteria.
COG0362. LUCA.
HOGENOMiHOG000255147.
InParanoidiP12013.
KOiK00033.
OMAiHYEDTER.
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.
IPR013328. 6PGD_dom_2.
IPR012284. 6PGD_dom_3.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_Gnd/GntZ.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR016040. NAD(P)-bd_dom.
IPR006183. Pgluconate_DH.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000109. 6PGD. 1 hit.
PRINTSiPR00076. 6PGDHDRGNASE.
SMARTiSM01350. 6PGD. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00873. gnd. 1 hit.
PROSITEiPS00461. 6PGD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12013-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNSIGVIGL GVMGSNIALN MANKGENVAV YNYTRDLTDQ LIQKLDGQSL
60 70 80 90 100
SPYYELEDFV QSLEKPRKIF LMVTAGKPVD SVIQSLKPLL EEGDVIMDGG
110 120 130 140 150
NSHYEDTERR YDELKEKGIG YLGVGISGGE VGALTGPSIM PGGDRDVYEK
160 170 180 190 200
AAPILTKIAA QVGDDPCCVY IGPKGAGHFT KMVHNGIEYA DMQLIAEAYT
210 220 230 240 250
FLRETLRLPL DEIASIFETW NQGELKSYLI EITAEILRKK DEKTGQPLID
260 270 280 290 300
VILDKTGQKG TGKWTSMQAI DNGIPSTIIT ESLFARYLSS LKEERMAAQD
310 320 330 340 350
VLAGPEAEEK HLDKDTWIEY VRQALYMGKV CAYAQGFAQY KMSSELYGWN
360 370 380 390 400
LPLKDIALIF RGGCIIRADF LNVISEAFSE QPNLANLLIA PYFTDKLHAY
410 420 430 440 450
QTGLRKVVCE GISTGISFPC LTTALSYYDG YRTGRSNANL LQAQRDYFGA
460
HTYERTDMDG VFHTNWSE
Length:468
Mass (Da):51,983
Last modified:October 1, 1989 - v1
Checksum:i56D88BEB8E553856
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_JNCM01000034.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_JNCM01000034.1.

3D structure databases

ProteinModelPortaliP12013.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021616.

Proteomic databases

PaxDbiP12013.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105C7Q. Bacteria.
COG0362. LUCA.
HOGENOMiHOG000255147.
InParanoidiP12013.
KOiK00033.
OMAiHYEDTER.
PhylomeDBiP12013.

Enzyme and pathway databases

BioCyciBSUB:BSU40080-MONOMER.
BRENDAi1.1.1.343. 658.

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.
IPR013328. 6PGD_dom_2.
IPR012284. 6PGD_dom_3.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_Gnd/GntZ.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR016040. NAD(P)-bd_dom.
IPR006183. Pgluconate_DH.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000109. 6PGD. 1 hit.
PRINTSiPR00076. 6PGDHDRGNASE.
SMARTiSM01350. 6PGD. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00873. gnd. 1 hit.
PROSITEiPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: October 5, 2016
This is version 131 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.