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Reviewed, UniProtKB/Swiss-Prot P29272 (G3P2_RHOSH)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase B
      Short name=GAPDH
    EC=1.2.1.12
Gene names
Name: gapB
OrganismRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifier1063 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

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Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Miscellaneous

This protein is encoded within the form II ribulose-bisphosphate carboxylase operon.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Glyceraldehyde-3-phosphate dehydrogenase B
PRO_0000145675

Regions

Nucleotide binding12 – 132NAD By similarity
Region150 – 1523Glyceraldehyde 3-phosphate binding By similarity
Region209 – 2102Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1511Nucleophile By similarity
Binding site361NAD By similarity
Binding site801NAD; via carbonyl oxygen By similarity
Binding site1811Glyceraldehyde 3-phosphate By similarity
Binding site1961Glyceraldehyde 3-phosphate By similarity
Binding site2321Glyceraldehyde 3-phosphate By similarity
Binding site3141NAD By similarity
Site1781Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
P29272-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: B072F443A20C3AFD

FASTA33335,679
        10         20         30         40         50         60 
MTIRVAINGF GRIGRNVLRA IVESGRTDIE VVAINDLGQV ETNAHLLRFD SVHGRFPAKV 

        70         80         90        100        110        120 
TSGDDWIDVG RGPIKVTAIR NPAELPWAGV DMAMECTGIF TTKEKAAAHL QNGAKRVLVS 

       130        140        150        160        170        180 
APCDGADRTI VYGVNHATLT ADDLVVSNAS CTTNCLSPVA KVLHDAIGIA KGFMTTIHSY 

       190        200        210        220        230        240 
TGDQPTLDTM HKDLYRARAA ALSMIPTSTG AAKAVGLVLP ELKGRLDGVS IRVPTPNVSV 

       250        260        270        280        290        300 
VDLVFEAARD TTVEEVNAAI EAAACGPLKG VLGFTTEPNV SSDFNHDPHS SVFHMDQTKV 

       310        320        330 
MEGRMVRILS WYDNEWGFSN RMADTAVAMG RLL

« Hide

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References

[1]"Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II CO2 fixation operon of Rhodobacter sphaeroides."
Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.
J. Biol. Chem. 266:20447-20452(1991) [PubMed: 1939098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases

M68914 Genomic DNA. Translation: AAA26156.1.
PIRC41080.

3D structure databases

HSSPHSSP built from PDB template 1NQO based on UniProtKB P00362.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 2796.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
[Graphical view]
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameG3P2_RHOSH
AccessionPrimary (citable) accession number: P29272
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents