NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SD11;
DOI=10.1093/nar/18.14.4271; PubMed=2377477 [NCBI, ExPASy, EBI, Israel, Japan]
Shuster J.R.;
"Kluyveromyces lactis glyceraldehyde-3-phosphate dehydrogenase and alcohol dehydrogenase-1 genes are linked and divergently transcribed.";
Nucleic Acids Res. 18:4271-4271(1990).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).

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

X52871; CAA37051.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382126; CAG98730.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S12721; DEVKGL.

RefSeq

XP_456022.1; -.

3D structure databases

PDB

2I5P; X-ray; 2.30 A; O=5-329.

[ExPASy / RCSB / EBI]

PDBsum

2I5P; -.

ModBase

P17819.

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.

BLOCKS

P17819.

Genome annotation databases

GeneID

2894950; -.

KEGG

kla:KLLA0F20988g; -.

Phylogenomic databases

HOGENOM

P17819; -.

Other

ProtoNet

P17819.

UniRef

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

Keywords

3D-structure; Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 329`	`329`	`Glyceraldehyde-3-phosphate dehydrogenase 1.`	`PRO_0000145556`
`NP_BIND`	`11 12`	`2`	`NAD (By similarity).`
`REGION`	`148 150`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`208 209`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`149 149`		`Nucleophile (By similarity).`
`BINDING`	`33 33`		`NAD (By similarity).`
`BINDING`	`78 78`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`179 179`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`231 231`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`313 313`		`NAD (By similarity).`
`SITE`	`176 176`	`1`	`Activates thiol group during catalysis (By similarity).`
`STRAND`	`5 7`	`3`
`HELIX`	`11 20`	`10`
`STRAND`	`26 32`	`7`
`HELIX`	`38 46`	`9`
`TURN`	`49 51`	`3`
`STRAND`	`58 60`	`3`
`STRAND`	`62 67`	`6`
`STRAND`	`70 75`	`6`
`HELIX`	`80 82`	`3`
`TURN`	`85 89`	`5`
`STRAND`	`91 95`	`5`
`STRAND`	`97 100`	`4`
`HELIX`	`103 111`	`9`
`STRAND`	`115 121`	`7`
`STRAND`	`124 126`	`3`
`TURN`	`131 133`	`3`
`HELIX`	`135 137`	`3`
`STRAND`	`142 145`	`4`
`HELIX`	`149 164`	`16`
`STRAND`	`167 176`	`10`
`STRAND`	`204 207`	`4`
`TURN`	`210 213`	`4`
`HELIX`	`214 217`	`4`
`HELIX`	`219 221`	`3`
`STRAND`	`224 231`	`8`
`STRAND`	`236 248`	`13`
`HELIX`	`252 264`	`13`
`TURN`	`265 270`	`6`
`STRAND`	`271 274`	`4`
`HELIX`	`280 283`	`4`
`STRAND`	`288 293`	`6`
`TURN`	`294 296`	`3`
`STRAND`	`298 301`	`4`
`STRAND`	`304 314`	`11`
`HELIX`	`315 328`	`14`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 35324 Da [This is the MW of the unprocessed precursor]

CRC64: EDE4F68FEDC86933 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKVAINGFG RIGRLVLRIA LQRKALEVVA VNDPFISVDY AAYMFKYDST HGRYKGEVTT 

        70         80         90        100        110        120 
SGNDLVIDGH KIAVFQEKDP ANLPWGKLGV DIVIDSTGVF KELDSAQKHL DAGAKKVVIT 

       130        140        150        160        170        180 
APSKTAPMFV VGVNEDKYNG ETIVSNASCT TNCLAPIAKI INDEFGIDEA LMTTVHSITA 

       190        200        210        220        230        240 
TQKTVDGPSH KDWRGGRTAS GNIIPSSTGA AKAVGKVLPE LQGKLTGMAF RVPTVDVSVV 

       250        260        270        280        290        300 
DLTVKLAKEA TYDEIKAAVK KASQGKLKNV VGYTEDSVVS SDFLGDTHST IFDASAGIQL 

       310        320 
SPKFVKVVAW YDNEYGYSER VVDLVEHVA

P17819 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