NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PATHWAY.
STRAIN=ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665;
PubMed=7668042 [NCBI, ExPASy, EBI, Israel, Japan]
Fernandes P.A., Sena-Esteves M., Moradas-Ferreira P.;
"Characterization of the glyceraldehyde-3-phosphate dehydrogenase gene family from Kluyveromyces marxianus -- polymerase chain reaction-single-strand conformation polymorphism as a tool for the study of multigenic families.";
Yeast 11:725-733(1995).

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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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
PIR	S57281; S57281.
3D structure databases
SMR	P84999; 1-329.
ModBase	P84999.
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	P84999.
Other
ProtoNet	P84999.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 331`	`331`	`Glyceraldehyde-3-phosphate dehydrogenase 3.`	`PRO_0000253991`
`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`	`77 77`		`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).`
`MOD_RES`	`148 148`		`Phosphoserine (By similarity).`
`MOD_RES`	`177 177`		`Phosphoserine (By similarity).`
`MOD_RES`	`200 200`		`Phosphoserine (By similarity).`

Sequence information

Length: 331 AA [This is the length of the unprocessed precursor]

Molecular weight: 35524 Da [This is the MW of the unprocessed precursor]

CRC64: 5E09084264795F01 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVRIAINGFG RIGRLVLRIA LSRKNIEVVA INDPFITVDY AAYMFKYDST HGRFDGEVSH 

        70         80         90        100        110        120 
DGKALIIDGK KVLVFQERDP ATLPWGAEKI DIAIDSTGIF KELDSAQKHI DAGAKKVVIT 

       130        140        150        160        170        180 
APSSTAPMFV VGVNEDKYAG QTIVSNASCT TNCLAPLAKI INNAFGIEEG LMTTVHSITA 

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

       250        260        270        280        290        300 
DLTVKLAKPA TYEEIKAVVK KASENELKGV MGYTEDAVVS SDFLGDTHSS IFDAAAGIQL 

       310        320        330 
SPQFVKLVSW YDNEFGYSTR VVDLVELVAK N

P84999 in FASTA format

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View entry in raw text format (no links)
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	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