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Q46LG0 (Q46LG0_PROMT) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
6-phosphogluconate dehydrogenase, decarboxylating PIRNR PIRNR000109 RuleBase RU000485
EC=1.1.1.44 PIRNR PIRNR000109 RuleBase RU000485
Gene names
Ordered Locus Names:PMN2A_0176
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP] EMBL AAZ57668.1
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH By similarity. PIRNR PIRNR000109

Catalytic activity

6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH. PIRNR PIRNR000109 RuleBase RU000485

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3. PIRNR PIRNR000109 RuleBase RU004281

Subunit structure

Homodimer By similarity. PIRNR PIRNR000109

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family. PIRNR PIRNR000109 RuleBase RU000485

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding10 – 156NADP By similarity PIRSR PIRSR000109-3
Nucleotide binding33 – 353NADP By similarity PIRSR PIRSR000109-3
Nucleotide binding75 – 773NADP By similarity PIRSR PIRSR000109-3
Region129 – 1313Substrate binding By similarity PIRSR PIRSR000109-2
Region186 – 1872Substrate binding By similarity PIRSR PIRSR000109-2

Sites

Active site1831Proton acceptor By similarity PIRSR PIRSR000109-1
Active site1901Proton donor By similarity PIRSR PIRSR000109-1
Binding site1031NADP By similarity PIRSR PIRSR000109-3
Binding site1031Substrate By similarity PIRSR PIRSR000109-2
Binding site1911Substrate By similarity PIRSR PIRSR000109-2
Binding site2621Substrate; via amide nitrogen By similarity PIRSR PIRSR000109-2
Binding site2891Substrate By similarity PIRSR PIRSR000109-2
Binding site4491Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2
Binding site4551Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2

Sequences

Sequence LengthMass (Da)Tools
Q46LG0 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: E60C9C407621688F

FASTA47251,466
        10         20         30         40         50         60 
MTKAHFGLVG LGVMGENLVL NAERNGFSSV VYNRTYQKTE DFLLGRGVNK SIQGAKDLQE 

        70         80         90        100        110        120 
FVSKLERPRR VLMMVKAGAA TDAVINQISP FLEEGDLLID GGNAQFMDTE RRVKELESKS 

       130        140        150        160        170        180 
FGYIGMGVSG GAKGALEGPS MMPGGTKTSY DAIESLLNKM AAQVEDGPCV TYIGPGGSGH 

       190        200        210        220        230        240 
FVKTVHNGIE YGIEQILAEA YDLMKRVCGM SGDEMASVMG YWNKTEELSS YLVEITEACL 

       250        260        270        280        290        300 
RVKDPDDSSD LVEKIMDKAG QKGTGLWTVV SALELGASVP TIYASLNGRV MSSMKDQRNY 

       310        320        330        340        350        360 
AETILNGNKP SFVDFGKPSD GMPLLMDAVV LATIASYAQG MDILRLASEE YDYDLDMPSI 

       370        380        390        400        410        420 
AQIWKGGCII RSTLLSRIQD AFKKDPSLTN LIIDKWFTDQ VNNRLSGLTQ VVSAAANAGI 

       430        440        450        460        470 
PVPCLSSTLD YLNSFRTSRL PQNLVQAMRD CFGSHTYERV DKAGSFHTEW ID

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References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000095 Genomic DNA. Translation: AAZ57668.1.
RefSeqYP_291371.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46LG0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ46LG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3605546.
GenomeReviewsGene locus PMN2A_0176 in contig CP000095_GR.
KEGGpmn:PMN2A_0176.
PATRIC23023719. VBIProMar14922_0802.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0362.
HOGENOMHBG286913.
OMAMEHNEMA.
PhylomeDBQ46LG0.
ProtClustDBPRK09287.

Enzyme and pathway databases

BioCycPMAR59920:PMN2A_0176-MONOMER.

Family and domain databases

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]
Gene3DG3DSA:1.20.5.320. Fibritin/6PGD_C-extension. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KOK00033.
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 nameQ46LG0_PROMT
AccessionPrimary (citable) accession number: Q46LG0
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: December 14, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info