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Reviewed, UniProtKB/Swiss-Prot P34916 (G3P1_ANAVT)

Last modified February 9, 2010. Version 75. 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 1
    EC=1.2.1.12
Gene names
Name: gap1
Ordered Locus Names: Ava_0495
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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-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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 343342Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000145624

Regions

Nucleotide binding13 – 142NAD By similarity
Region154 – 1563Glyceraldehyde 3-phosphate binding By similarity
Region214 – 2152Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1551Nucleophile By similarity
Binding site351NAD By similarity
Binding site791NAD; via carbonyl oxygen By similarity
Binding site1851Glyceraldehyde 3-phosphate By similarity
Binding site2371Glyceraldehyde 3-phosphate By similarity
Binding site3191NAD By similarity
Site1821Activates thiol group during catalysis By similarity

Experimental info

Sequence conflict2401T → I in AAA21995. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P34916-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 307D0703DF8D279C

FASTA34336,666
        10         20         30         40         50         60 
MAKLKVGING FGRIGRLVLR AGINNPNIEF VGINDLVPPD NLAYLLKYDS THGKLRSQVE 

        70         80         90        100        110        120 
AKDDGIVIDG HFIPCVSVRN PAELPWGKLG ADYVVESTGL FTDSEGASKH LQAGAKRVII 

       130        140        150        160        170        180 
SAPTKDPDRV RTLLVGVNHD LFDPSKDVIV SNASCTTNCL APIAKVINDN FGLTEGLMTT 

       190        200        210        220        230        240 
VHAMTATQPT VDGPSKKDWR GGRGAAQNII PSSTGAAKAV ALVLPELKGK LTGMAFRVPT 

       250        260        270        280        290        300 
PDVSVVDLTF KTAKATSYKE ICAAMKQASE GSLAGILGYT DEEVVSTDFQ GDTHSSIFDA 

       310        320        330        340 
GAGIELNSNF FKVVAWYDNE WGYSNRVVDL MLSMIQKEQL AAV 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for a chimeric nature of nuclear genomes: eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes."
Martin W., Brinkmann H., Savona C., Cerff R.
Proc. Natl. Acad. Sci. U.S.A. 90:8692-8696(1993) [PubMed: 8378350] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07497 Genomic DNA. Translation: AAA21995.2.
CP000117 Genomic DNA. Translation: ABA20119.1.
PIRI39602.
RefSeqYP_321014.1.

3D structure databases

SMRP34916. Positions 3-338.
ModBaseSearch...

Protein-protein interaction databases

STRINGP34916.

Genome annotation databases

GeneID3682402.
GenomeReviewsGene locus Ava_0495 in contig CP000117_GR.
KEGGava:Ava_0495.
NMPDRfig|240292.3.peg.1853.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHBG571736.
OMAKEICTEV.
PhylomeDBP34916.

Enzyme and pathway databases

BioCycAVAR240292:AVA_0495-MONOMER.

Family and domain databases

InterProIPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020832. GlycerAld_3-P_DH_cat_sub.
IPR020831. GlycerAld_3-P_DH_family.
IPR020828. GlycerAld_3-P_DH_NAD(P)_bd.
IPR000173. GlycerAld_3-P_DH_subfam.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[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.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P1_ANAVT
AccessionPrimary (citable) accession number: P34916
Secondary accession number(s): Q3MFW7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 75 of the entry and version 4 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