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Reviewed, UniProtKB/Swiss-Prot P58559 (G3P3_ANASP)

Last modified November 25, 2008. Version 44. 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

Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 3
    EC=1.2.1.12
Gene names
Name: gap3
Ordered Locus Names: alr1095
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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 By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords

   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome

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-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Glyceraldehyde-3-phosphate dehydrogenase 3
PRO_0000145627

Regions

Nucleotide binding12 – 132NAD By similarity
Region152 – 1543Glyceraldehyde 3-phosphate binding By similarity
Region211 – 2122Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1531Nucleophile By similarity
Binding site1831Glyceraldehyde 3-phosphate By similarity
Binding site1981Glyceraldehyde 3-phosphate By similarity
Binding site2341Glyceraldehyde 3-phosphate By similarity
Binding site3171NAD By similarity
Site1801Activates thiol group during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P58559-1 [UniParc].

Last modified January 23, 2002. Version 1.
Checksum: F86B22C5BCAD32AF

FASTA33737,117
        10         20         30         40         50         60 
MKVRVGINGF GRMGRLALRA AWDWPELEFV HINEIKGGAV AAAHLLKFDS VHGRWTPEVE 

        70         80         90        100        110        120 
AEGERVLIDG TPLSFSEYGK PDDVPWEDFG VDLVLECSGK FRTPATLDPY FKRGVQKVIV 

       130        140        150        160        170        180 
AAPVKEEALN IVMGVNDYLY EPEKHHLLTA ASCTTNCLAP VVKVIHEGLG IKHGIITTIH 

       190        200        210        220        230        240 
DNTNTQTLVD APHKDLRRAR ATSLSLIPTT TGSATAIALI YPELKGKLNG IAVRVPLLNA 

       250        260        270        280        290        300 
SLTDCVFEVT RPTTVEEINA LLKAASEQAP LQGILGYEER PLVSIDYKDD PRSSIIDALS 

       310        320        330 
TMVVDETQVK ILAWYDNEWG YVNRMVELAR KVALSLK 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BA000019 Genomic DNA. Translation: BAB73052.1.
PIRAD1943.
RefSeqNP_485138.1.

3D structure databases

HSSPHSSP built from PDB template 4DBV based on UniProtKB P00362.
ModBaseSearch...

Genome annotation databases

GeneID1104689.
GenomeReviewsGene locus alr1095 in contig BA000019_GR.
KEGGana:alr1095.
NMPDRfig|103690.1.peg.1405.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP58559.

Enzyme and pathway databases

BioCycNSP103690:ALR1095-MON.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DHase.
IPR006424. Glyceraldehyde-3-P_DHase_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...

Entry information

Entry nameG3P3_ANASP
AccessionPrimary (citable) accession number: P58559
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: November 25, 2008
This is version 44 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)

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