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P49433 (G3P1_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glyceraldehyde-3-phosphate dehydrogenase 1

Short name=GAP-1
Short name=GAPDH 1
EC=1.2.1.12
Gene names
Name:gap1
Ordered Locus Names:slr0884
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechocystis

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
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.

Sequence caution

The sequence BAA17609.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000145708

Regions

Nucleotide binding11 – 122NAD By similarity
Region152 – 1543Glyceraldehyde 3-phosphate binding By similarity
Region212 – 2132Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1531Nucleophile By similarity
Binding site331NAD By similarity
Binding site771NAD; via carbonyl oxygen By similarity
Binding site1831Glyceraldehyde 3-phosphate By similarity
Binding site2351Glyceraldehyde 3-phosphate By similarity
Binding site3171NAD By similarity
Site1801Activates thiol group during catalysis By similarity

Experimental info

Sequence conflict781N → D in BAA17609. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P49433 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 4C97358AD070B1E6

FASTA33936,146
        10         20         30         40         50         60 
MLKIGINGFG RIGRLVARIA MANPQVTLVG INDLVPASNL AYLFKYDSTH GSYGGTVVAK 

        70         80         90        100        110        120 
EEGIVIDDQF IPCFSQRNPA QLPWGDLGAD YVVESTGLFT TYATAENHLK AGAKRVIISA 

       130        140        150        160        170        180 
PSKDPEKIPT FVVGVNHLNY NADTDKIVSN ASCTTNCLAP IAKILDDNFG IVEGLMTTVH 

       190        200        210        220        230        240 
AMTATQPTVD GPSKKDFRGG RGAAQNIIPS STGAAKAAAL VLPQLKGKLT GMAFRVPTPN 

       250        260        270        280        290        300 
VSVVDLTFKT EKATSYEEIC AAMKTAAEGE LKGILGYTAD DVVSMDFRTD PRSSIFDAGA 

       310        320        330 
GIGLNSNFFK VVSWYDNEWG YSCRVIDLML TMASKDGLV 

« Hide

References

« Hide 'large scale' references
[1]Schubert M., Brinkmann H., Cerff R.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86375 Genomic DNA. Translation: CAA60134.1.
BA000022 Genomic DNA. Translation: BAA17609.1. Different initiation.
PIRS77275.
RefSeqNP_440929.1. NC_000911.1.

3D structure databases

ProteinModelPortalP49433.
SMRP49433. Positions 2-336.
ModBaseSearch...

Protein-protein interaction databases

IntActP49433. 1 interaction.
STRINGP49433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID954234.
GenomeReviewsGene locus slr0884 in contig BA000022_GR.
KEGGsyn:slr0884.
PATRIC23839130. VBISynSp132158_1129.

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHBG571736.
OMADARTSIF.
PhylomeDBP49433.
ProtClustDBCLSK892914.

Enzyme and pathway databases

BioCycSSP1148:SLR0884-MONOMER.

Family and domain databases

InterProIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00134.
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.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P1_SYNY3
AccessionPrimary (citable) accession number: P49433
Secondary accession number(s): P73569
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families