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Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

gnd

Organism
Mycobacterium leprae
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.UniRule annotation

Catalytic activityi

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

Pathwayi: pentose phosphate pathway

This protein is involved in step 3 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. 6-phosphogluconate dehydrogenase, decarboxylating (gnd)
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei113 – 1131NADPUniRule annotation
Binding sitei113 – 1131SubstrateUniRule annotation
Active sitei200 – 2001Proton donorUniRule annotation
Binding sitei201 – 2011SubstrateUniRule annotation
Binding sitei271 – 2711Substrate; via amide nitrogenUniRule annotation
Binding sitei298 – 2981SubstrateUniRule annotation
Binding sitei456 – 4561Substrate; shared with dimeric partnerUniRule annotation
Binding sitei462 – 4621Substrate; shared with dimeric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 256NADPUniRule annotation
Nucleotide bindingi43 – 453NADPUniRule annotation
Nucleotide bindingi85 – 873NADPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

Pentose shuntUniRule annotation

Keywords - Ligandi

NADPUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00115; UER00410.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphogluconate dehydrogenase, decarboxylatingUniRule annotation (EC:1.1.1.44UniRule annotation)
Gene namesi
Name:gndImported
OrganismiMycobacterium lepraeImported
Taxonomic identifieri1769 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272631.ML2065.

Structurei

3D structure databases

ProteinModelPortaliO32911.
SMRiO32911. Positions 14-478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini189 – 4782906PGDInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni196 – 1972Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the 6-phosphogluconate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C7Q. Bacteria.
COG0362. LUCA.

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.

O32911-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDMSAPESK TAIAQIGVTG LAVMGSNIAR NFARHGYTVA LHNRSIAKTD
60 70 80 90 100
TLLKEHGSEG NFVRTETIPE FLAALQTPRR VLIMVKAGDA TDAVINELAD
110 120 130 140 150
VMEPSDIIID GGNSLFTDTI RREKAMRERG LHFVGAGISG GEEGALNGPS
160 170 180 190 200
IMPGGPAESY TSLGPLLEEI SAHVDGVSCC THIGPGGSGH FVKMVHNGIE
210 220 230 240 250
YSDMQLIGEA YQLLRDGLGM SAPQIADVFT EWNRGDLNSY LVEITAEVLR
260 270 280 290 300
QTDIKTGRPL VDVILDKAEQ KGTGRWTVQS ALDLGVPITG IAEAVFARAL
310 320 330 340 350
SGSVLQRKAA IGLASGKLGN KPTDRETFIE DVRQALYASK IVAYAQGFNH
360 370 380 390 400
IQTGSTEFGW NITPGDLATI WRGGCIIRAK FLNRIKEAFD AAPDLASLIV
410 420 430 440 450
APYFRSAVES AIDSWRRVVS TATQLGIPNP GFSSALSYYD ALRTERLPAA
460 470 480
LTQAQRDFFG AHSYGRVDAR GKFHTLWSED RSEVTV
Length:486
Mass (Da):52,379
Last modified:January 1, 1998 - v1
Checksum:iF98F868DFCF6791D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL008609 Genomic DNA. Translation: CAA15451.1.
PIRiT44750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL008609 Genomic DNA. Translation: CAA15451.1.
PIRiT44750.

3D structure databases

ProteinModelPortaliO32911.
SMRiO32911. Positions 14-478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML2065.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C7Q. Bacteria.
COG0362. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00410.

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...

Publicationsi

  1. "Use of an ordered cosmid library to deduce the genomic organization of Mycobacterium leprae."
    Eiglmeier K., Honore N., Woods S.A., Caudron B., Cole S.T.
    Mol. Microbiol. 7:197-206(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Skelton J., Churcher C.M.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. Parkhill J., Barrell B.G., Rajandream M.A.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiO32911_MYCLR
AccessioniPrimary (citable) accession number: O32911
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.