P22513 (G3PG_TRYCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glyceraldehyde-3-phosphate dehydrogenase, glycosomal Short name=GAPDH EC=1.2.1.12
Organism	Trypanosoma cruzi
Taxonomic identifier	5693 [NCBI]
Taxonomic lineage	Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Schizotrypanum

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.2 Ref.3 Ref.4
Subcellular location	Glycosome.
Miscellaneous	There are two identical genes that code for glycosomal GAPDH.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Glycosome Peroxisome
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glycosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD+) (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 – 359

359

Glyceraldehyde-3-phosphate dehydrogenase, glycosomal

PRO_0000145532

Regions

Nucleotide binding

12 – 13

2

NAD

Region

165 – 167

3

Glyceraldehyde 3-phosphate binding

Region

226 – 227

2

Glyceraldehyde 3-phosphate binding

Motif

357 – 359

3

Microbody targeting signal Potential

Sites

Active site

166

1

Nucleophile

Binding site

38

1

NAD

Binding site

91

1

NAD; via carbonyl oxygen

Binding site

134

1

NAD

Binding site

197

1

Glyceraldehyde 3-phosphate

Binding site

249

1

Glyceraldehyde 3-phosphate

Binding site

335

1

NAD

Site

194

1

Activates thiol group during catalysis

Secondary structure

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359

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

12 – 23

12

Turn

28 – 30

3

Beta strand

31 – 39

9

Helix

43 – 51

9

Turn

54 – 56

3

Beta strand

63 – 66

4

Beta strand

77 – 80

4

Beta strand

83 – 89

7

Helix

94 – 96

3

Helix

99 – 102

4

Beta strand

106 – 109

4

Beta strand

111 – 113

3

Helix

117 – 120

4

Helix

122 – 125

4

Beta strand

129 – 135

7

Beta strand

138 – 140

3

Turn

146 – 148

3

Helix

150 – 152

3

Turn

155 – 157

3

Beta strand

159 – 162

4

Helix

166 – 180

15

Beta strand

186 – 195

10

Beta strand

200 – 204

5

Helix

212 – 214

3

Helix

217 – 219

3

Beta strand

222 – 225

4

Helix

228 – 235

8

Helix

237 – 239

3

Turn

240 – 242

3

Beta strand

243 – 251

9

Beta strand

256 – 263

8

Helix

270 – 282

13

Turn

283 – 288

6

Beta strand

289 – 292

4

Helix

298 – 301

4

Beta strand

307 – 311

5

Helix

312 – 317

6

Beta strand

324 – 333

10

Helix

337 – 358

22

Sequences

	Sequence		Length	Mass (Da)
	P22513 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 741ED29A4426453B	FASTA	359	39,061
	10 20 30 40 50 60 MPIKVGINGF GRIGRMVFQA LCEDGLLGTE IDVVAVVDMN TDAEYFAYQM RYDTVHGKFK 70 80 90 100 110 120 YEVTTTKSSP SVAKDDTLVV NGHRILCVKA QRNPADLPWG KLGVEYVIES TGLFTAKAAA 130 140 150 160 170 180 EGHLRGGARK VVISAPASGG AKTLVMGVNH HEYNPSEHHV VSNASCTTNC LAPIVHVLVK 190 200 210 220 230 240 EGFGVQTGLM TTIHSYTATQ KTVDGVSVKD WRGGRAAAVN IIPSTTGAAK AVGMVIPSTQ 250 260 270 280 290 300 GKLTGMSFRV PTPDVSVVDL TFTAARDTSI QEIDAALKRA SKTYMKGILG YTDEELVSAD 310 320 330 340 350 FINDNRSSIY DSKATLQNNL PKERRFFKIV SWYDNEWGYS HRVVDLVRHM ASKDRSARL

References

[1]	"Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase does not conform to the 'hotspot' topogenic signal model." Kendall G., Wilderspin A.F., Ashall F., Miles M.A., Kelly J.M. EMBO J. 9:2751-2758(1990) [PubMed: 2167831] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: X10/6.
[2]	"Structure of Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase complexed with chalepin, a natural product inhibitor, at 1.95 A resolution." Pavao F., Castilho M.S., Pupo M.T., Dias R.L.A., Correa A.G., Fernandes J.B., da Silva M.F.G.F., Mafezoli J., Vieira P.C., Oliva G. FEBS Lett. 520:13-17(2002) [PubMed: 12044862] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH CHALEPIN, SUBUNIT.
[3]	"Evidence for the two phosphate binding sites of an analogue of the thioacyl intermediate for the Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase-catalyzed reaction, from its crystal structure." Castilho M.S., Pavao F., Oliva G., Ladame S., Willson M., Perie J. Biochemistry 42:7143-7151(2003) [PubMed: 12795610] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.
[4]	"Crystal structure of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-d-glyceric acid." Ladame S., Castilho M.S., Silva C.H.T.P., Denier C., Hannaert V., Perie J., Oliva G., Willson M. Eur. J. Biochem. 270:4574-4586(2003) [PubMed: 14622286] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52898 Genomic DNA. Translation: CAA37080.1.
X52898 Genomic DNA. Translation: CAA37079.1.

PIR

DEUT1C. S12565.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K3T	X-ray	1.95	A/B/C/D	1-359	[»]
1ML3	X-ray	2.50	A/B/C/D	1-359	[»]
1QXS	X-ray	2.75	A/B/C/D	1-359	[»]
3DMT	X-ray	2.30	A/B/C/D	1-359	[»]
3IDS	X-ray	1.80	A/B/C/D	1-359	[»]

ProteinModelPortal

P22513.

SMR

P22513. Positions 1-359.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

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.

SMART

SM00846. Gp_dh_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01534. GAPDH-I. 1 hit.

PROSITE

PS00071. GAPDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

G3PG_TRYCR

Accession

Primary (citable) accession number: P22513

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	December 14, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)