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Reviewed, UniProtKB/Swiss-Prot P34917 (G3P2_ANAVT)

Last modified June 16, 2009. Version 70. 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 2
    EC=1.2.1.12
Gene names
Name: gap2
Ordered Locus Names: Ava_2318
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

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Protein attributes

Sequence length337 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.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Glyceraldehyde-3-phosphate dehydrogenase 2
PRO_0000145626

Regions

Nucleotide binding11 – 122NAD By similarity
Region153 – 1553Glyceraldehyde 3-phosphate binding By similarity
Region212 – 2132Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1541Nucleophile By similarity
Binding site351NAD By similarity
Binding site801NAD; via carbonyl oxygen By similarity
Binding site1841Glyceraldehyde 3-phosphate By similarity
Binding site1991Glyceraldehyde 3-phosphate By similarity
Binding site2351Glyceraldehyde 3-phosphate By similarity
Binding site3171NAD By similarity
Site1811Activates thiol group during catalysis By similarity

Experimental info

Sequence conflict471K → N in AAA21996. Ref.1
Sequence conflict511M → S in AAA21996. Ref.1
Sequence conflict54 – 574KLKN → VKK in AAA21996. Ref.1
Sequence conflict1141A → V in AAA21996. Ref.1
Sequence conflict2171A → R in AAA21996. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P34917-1 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: 4FDCBD856B858863

FASTA33736,876
        10         20         30         40         50         60 
MIRVAINGFG RIGRNFARCW LGRENSNIEL VAVNDTSDPR TNAHLLKYDS MLGKLKNVDI 

        70         80         90        100        110        120 
TADDNSITVN GKTIKCVSDR NPENLPWKEW EIDLIIESTG VFTSKEGALK HVNAGAKKVL 

       130        140        150        160        170        180 
ITAPGKNEDG TFVIGVNHHD YDHNVHHIIS NASCTTNCLA PIAKVLNDKF GIIKGSMTTT 

       190        200        210        220        230        240 
HSYTGDQRLL DASHRDLRRA RAAAINIVPT STGAAKAVAL VIPELKGKLN GVALRVPTPN 

       250        260        270        280        290        300 
VSMVDFVVQV EKRTITEEVN QALKDASEGP LKGILDYSEL QLVSSDYQGT DASSIVDASL 

       310        320        330 
TLVMGNDLVK VMAWYDNEWG YSQRVLDLAE LVAEKWV

« Hide

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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].

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Cross-references

Sequence databases

L07498 Genomic DNA. Translation: AAA21996.1.
CP000117 Genomic DNA. Translation: ABA21936.1.
PIRI39603.
RefSeqYP_322831.1.

3D structure databases

HSSPHSSP built from PDB template 1NBO based on UniProtKB P19866.
SMRP34917. Positions 2-335.
ModBaseSearch...

Genome annotation databases

GeneID3683588.
GenomeReviewsGene locus Ava_2318 in contig CP000117_GR.
KEGGava:Ava_2318.
NMPDRfig|240292.3.peg.198.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP34917.
OMAP34917. NTDEKAS.

Enzyme and pathway databases

BioCycAVAR240292:AVA_2318-MON.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
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_ANAVT
AccessionPrimary (citable) accession number: P34917
Secondary accession number(s): Q3MAQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 4, 2006
Last modified: June 16, 2009
This is version 70 of the entry and version 2 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