[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8378350 [NCBI, ExPASy, EBI, Israel, Japan] Martin W., Brinkmann H., Savona C., Cerff R.; "Evidence for a chimeric nature of nuclear genomes: eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes."; Proc. Natl. Acad. Sci. U.S.A. 90:8692-8696(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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.; "Complete sequence of Anabaena variabilis ATCC 29413."; Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

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: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L07499; AAA21997.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000117; ABA23320.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I39604; I39604.

RefSeq

YP_324215.1; -.

3D structure databases

HSSP

P00362; 4DBV. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P34918.

Enzyme and pathway databases

BioCyc

AVAR240292:AVA_3715-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004365;	Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.

PANTHER

PTHR10836; GAP_DH; 1.

Pfam

PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000149; GAP_DH; 1.

PRINTS

PR00078; G3PDHDRGNASE.

TIGRFAMs

TIGR01534; GAPDH-I; 1.

PROSITE

PS00071; GAPDH; 1.

ProtoNet

P34918.

Genome annotation databases

GeneID

3678801; -.

GenomeReviews

CP000117_GR; Ava_3715.

KEGG

ava:Ava_3715; -.

NMPDR

fig|240292.3.peg.4868; -.

Phylogenomic databases

HOGENOM

P34918; -.

Genome annotation databases

CMR

P34918; Ava_3715.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 337`	`337`	`Glyceraldehyde-3-phosphate dehydrogenase 3.`	`PRO_0000145628`
`NP_BIND`	`12 13`	`2`	`NAD (By similarity).`
`REGION`	`152 154`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`211 212`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`153 153`		`Nucleophile (By similarity).`
`BINDING`	`183 183`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`198 198`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`234 234`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`317 317`		`NAD (By similarity).`
`SITE`	`180 180`	`1`	`Activates thiol group during catalysis (By similarity).`
`CONFLICT`	`215 215`		`T -> K (in Ref. 1; AAA21997).`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 37130 Da [This is the MW of the unprocessed precursor]

CRC64: 967BD40141E46F5C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIRVGINGF GRMGRLALRA AWGWPELEFV HINEIKGGAV AAAHLLKFDS VHGRWTPEVE 

        70         80         90        100        110        120 
AEGERVLIDS TPLSFSEYGK PEDVPWEDFG 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 
SLTDCVFEVN RPTTVEEINA LLKAASEQAP LQGILGYEER PLVSIDYKDD PRSSIIDALS 

       310        320        330 
TMVVDETQVK ILAWYDNEWG YVNRMVELAR KVALSLK

P34918 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools