Reviewed, UniProtKB/Swiss-Prot P84998 (G3P1_KLUMA)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 1
      Short name=GAPDH 1
    EC=1.2.1.12

Gene names

Name:

GAP1

Organism

Kluyveromyces marxianus (Yeast) (Candida kefyr)

Taxonomic identifier

4911 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH. Ref.1
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. Ref.1
Subunit structure	Homotetramer By similarity. UniProtKB P22513
Subcellular location	Cytoplasm By similarity. UniProtKB P00359
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 329

329

Glyceraldehyde-3-phosphate dehydrogenase 1

PRO_0000253990

Regions

Nucleotide binding

11 – 12

2

NAD By similarity UniProtKB P22513

Region

148 – 150

3

Glyceraldehyde 3-phosphate binding By similarity UniProtKB P22513

Region

208 – 209

2

Glyceraldehyde 3-phosphate binding By similarity UniProtKB P22513

Sites

Active site

149

1

Nucleophile By similarity UniProtKB P22513

Binding site

33

1

NAD By similarity UniProtKB P22513

Binding site

77

1

NAD; via carbonyl oxygen By similarity UniProtKB P22513

Binding site

179

1

Glyceraldehyde 3-phosphate By similarity UniProtKB P22513

Binding site

231

1

Glyceraldehyde 3-phosphate By similarity UniProtKB P22513

Binding site

313

1

NAD By similarity UniProtKB P22513

Site

176

1

Activates thiol group during catalysis By similarity UniProtKB P22513

Amino acid modifications

Modified residue

148

1

Phosphoserine By similarity UniProtKB P00359

Modified residue

177

1

Phosphoserine By similarity UniProtKB P00359

Modified residue

200

1

Phosphoserine By similarity UniProtKB P00359

Secondary structure

1

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329

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

11 – 20

10

Beta strand

26 – 32

7

Beta strand

34 – 36

3

Helix

38 – 46

9

Turn

49 – 51

3

Beta strand

58 – 60

3

Beta strand

62 – 67

6

Beta strand

70 – 75

6

Helix

80 – 82

3

Helix

85 – 88

4

Beta strand

91 – 95

5

Beta strand

97 – 100

4

Helix

103 – 111

9

Beta strand

115 – 121

7

Beta strand

124 – 126

3

Turn

131 – 133

3

Helix

135 – 137

3

Beta strand

142 – 145

4

Helix

149 – 164

16

Beta strand

167 – 176

10

Beta strand

204 – 207

4

Helix

210 – 217

8

Helix

219 – 221

3

Beta strand

224 – 231

8

Beta strand

235 – 248

14

Helix

252 – 264

13

Helix

266 – 269

4

Beta strand

271 – 274

4

Helix

280 – 283

4

Beta strand

288 – 301

14

Beta strand

304 – 314

11

Helix

315 – 328

14

Sequences

	Sequence		Length	Mass (Da)
	P84998-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 4C5C08D5C7858672	FASTA	329	35,253
	10 20 30 40 50 60 MVSIAINGFG RIGRLVLRIA LERKNIDVVA INDPFISVDY AAYMFKYDST HGKYKGEVSH 70 80 90 100 110 120 DGSNLIINGK KVAVFQEKDP ATLPWGKLGV DIAVDSTGVF KELDSAQKHI DAGAKKVVIT 130 140 150 160 170 180 APSKTAPMFV VGVNEDKYNG EKIVSNASCT TNCLAPIAKI INDEFGIEEG LMTTVHSITA 190 200 210 220 230 240 TQKTVDGPSH KDWRGGRTAS GNIIPSSTGA AKAVGKVLPE LQGKLTGMAF RVPTTDVSVV 250 260 270 280 290 300 DLTVKLVKAA TYDEIKAAVK KVSEGKLKDV VGYTEDAVVS SDFLGDTHST IFDAAAGIQL 310 320 SPKFVKLVAW YDNEYGYSTR VVDLVEHVA

References

[1]

"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." Fernandes P.A., Sena-Esteves M., Moradas-Ferreira P. Yeast 11:725-733(1995) [PubMed: 7668042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, PATHWAY. Strain: ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665.

[2]

"The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures." Ferreira-da-Silva F., Pereira P.J.B., Gales L., Roessle M., Svergun D.I., Moradas-Ferreira P., Damas A.M. J. Biol. Chem. 281:33433-33440(2006) [PubMed: 16963457] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). Strain: ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665.

Cross-references

Sequence databases

PIR

S57279.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I5P	X-ray	2.30	O/P	1-329	[»]

SMR

P84998. Positions 1-329.

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.2.1.12. 97088.

Family and domain databases

InterPro

IPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
[Graphical view]

PANTHER

PTHR10836. GAP_DH. 1 hit.

Pfam

PF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000149. GAP_DH. 1 hit.

PRINTS

PR00078. G3PDHDRGNASE.

TIGRFAMs

TIGR01534. GAPDH-I. 1 hit.

PROSITE

PS00071. GAPDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

G3P1_KLUMA

Accession

Primary (citable) accession number: P84998

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	October 17, 2006
Last modified:	June 16, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)