Reviewed, UniProtKB/Swiss-Prot P00357 (G3P_HOMAM)

Names and origin

Protein names	Recommended name:     Glyceraldehyde-3-phosphate dehydrogenase       Short name=GAPDH     EC=1.2.1.12
Organism	Homarus americanus (American lobster)
Taxonomic identifier	6706 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Astacidea › Nephropoidea › Nephropidae › Homarus

Protein attributes

Sequence length	333 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.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer. Ref.2
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
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 – 333

333

Glyceraldehyde-3-phosphate dehydrogenase

PRO_0000145505

Regions

Nucleotide binding

10 – 11

2

NAD

Region

147 – 149

3

Glyceraldehyde 3-phosphate binding By similarity

Region

207 – 208

2

Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site

148

1

Nucleophile

Binding site

31

1

NAD

Binding site

118

1

NAD; via carbonyl oxygen

Binding site

178

1

Glyceraldehyde 3-phosphate By similarity

Binding site

230

1

Glyceraldehyde 3-phosphate By similarity

Binding site

312

1

NAD

Site

175

1

Activates thiol group during catalysis

Amino acid modifications

Modified residue

1

1

N-acetylserine Ref.1

Experimental info

Sequence conflict

6

1

N → D AA sequence Ref.1

Secondary structure

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333

Helix Strand Turn

Details...

Helix

10 – 14

5

Helix

16 – 19

4

Turn

20 – 23

4

Helix

36 – 44

9

Beta strand

47 – 49

3

Beta strand

56 – 59

4

Beta strand

62 – 67

6

Helix

78 – 80

3

Turn

84 – 87

4

Beta strand

90 – 93

4

Beta strand

95 – 97

3

Helix

101 – 105

5

Helix

106 – 110

5

Beta strand

114 – 119

6

Beta strand

122 – 124

3

Helix

129 – 135

7

Helix

148 – 164

17

Beta strand

165 – 176

12

Beta strand

179 – 181

3

Helix

192 – 194

3

Helix

209 – 214

6

Beta strand

227 – 232

6

Beta strand

237 – 247

11

Helix

251 – 263

13

Turn

264 – 269

6

Beta strand

288 – 292

5

Beta strand

298 – 300

3

Beta strand

303 – 309

7

Helix

314 – 331

18

Sequences

	Sequence		Length	Mass (Da)
	P00357-1 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 6EEB5577D06D756A	FASTA	333	35,716
	10 20 30 40 50 60 SKIGINGFGR IGRLVLRAAL SCGAQVVAVN DPFIALEYMV YMFKYDSTHG VFKGEVKMED 70 80 90 100 110 120 GALVVDGKKI TVFNEMKPEN IPWSKAGAEY IVESTGVFTT IEKASAHFKG GAKKVVISAP 130 140 150 160 170 180 SADAPMFVCG VNLEKYSKDM TVVSNASCTT NCLAPVAKVL HENFEIVEGL MTTVHAVTAT 190 200 210 220 230 240 QKTVDGPSAK DWRGGRGAAQ NIIPSSTGAA KAVGKVIPEL DGKLTGMAFR VPTPDVSVVD 250 260 270 280 290 300 LTVRLGKECS YDDIKAAMKT ASEGPLQGFL GYTEDDVVSS DFIGDNRSSI FDAKAGIQLS 310 320 330 KTFVKVVSWY DNEFGYSQRV IDLLKHMQKV DSA

References

[1]	"Amino-acid sequence of glyceraldehyde 3-phosphate dehydrogenase from lobster muscle." Davidson B.E., Sajgo M., Noller H.F., Harris J.I. Nature 216:1181-1185(1967) [PubMed: 4294736] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase." Moras D., Olsen K.W., Sabesan M.N., Buehner M., Ford G.C., Rossmann M.G. J. Biol. Chem. 250:9137-9162(1975) [PubMed: 127793] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH NAD AND INORGANIC PHOSPHATE, SUBUNIT, SEQUENCE REVISION TO 6.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

DELOG3. A00369.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GPD	X-ray	2.90	G/R	1-333	[»]
4GPD	X-ray	2.80	1/2/3/4	1-333	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.2.1.12. 189984.

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

G3P_HOMAM

Accession

Primary (citable) accession number: P00357

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 15, 1999
Last modified:	June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)