Reviewed, UniProtKB/Swiss-Prot P39460 (G3P_SULSO)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase
      Short name=GAPDH
    EC=1.2.1.59
Alternative name(s):
    NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase

Gene names

Name:	gap
Synonyms:	agaPD
Ordered Locus Names:	SSO0528
ORF Names:	C22_023

Organism

Sulfolobus solfataricus [Complete proteome] [HAMAP]

Taxonomic identifier

2287 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Can use both NAD and NADP as cofactors, but exhibits a marked preference for NADP.
Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity Inferred from electronic annotation. Source: EC glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 340

340

Glyceraldehyde-3-phosphate dehydrogenase

PRO_0000145735

Regions

Nucleotide binding

11 – 12

2

NAD By similarity

Region

138 – 140

3

Glyceraldehyde 3-phosphate binding By similarity

Region

193 – 194

2

Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site

139

1

Nucleophile By similarity

Binding site

109

1

NAD; via amide nitrogen By similarity

Binding site

167

1

NAD By similarity

Binding site

300

1

NAD; via carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond

123 ↔ 149

Experimental info

Sequence conflict

48

1

I → Y in CAA47040. Ref.1

Sequence conflict

52

1

V → AL in CAA47040. Ref.1

Sequence conflict

72 – 73

2

ED → DY in CAA47040. Ref.1

Sequence conflict

159

1

K → N in CAA47040. Ref.1

Secondary structure

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340

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

11 – 21

11

Beta strand

26 – 32

7

Helix

38 – 45

8

Helix

54 – 56

3

Helix

57 – 61

5

Turn

62 – 64

3

Helix

71 – 77

7

Beta strand

79 – 83

5

Helix

89 – 99

11

Beta strand

103 – 106

4

Helix

112 – 114

3

Helix

121 – 128

8

Beta strand

132 – 136

5

Helix

139 – 152

14

Beta strand

157 – 169

13

Beta strand

183 – 190

8

Helix

193 – 198

6

Beta strand

205 – 214

10

Beta strand

219 – 229

11

Helix

233 – 241

9

Beta strand

246 – 249

4

Beta strand

251 – 254

4

Helix

258 – 267

10

Helix

271 – 273

3

Beta strand

277 – 281

5

Helix

282 – 284

3

Beta strand

286 – 288

3

Beta strand

291 – 298

8

Turn

300 – 303

4

Helix

304 – 315

12

Helix

321 – 331

11

Sequences

	Sequence		Length	Mass (Da)
	P39460-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 609C9260C3062B6D	FASTA	340	37,596
	10 20 30 40 50 60 MINVAVNGYG TIGKRVADAI IKQPDMKLVG VAKTSPNYEA FIAHRRGIRI YVPQQSIKKF 70 80 90 100 110 120 EESGIPVAGT VEDLIKTSDI VVDTTPNGVG AQYKPIYLQL QRNAIFQGGE KAEVADISFS 130 140 150 160 170 180 ALCNYNEALG KKYIRVVSCN TTALLRTICT VNKVSKVEKV RATIVRRAAD QKEVKKGPIN 190 200 210 220 230 240 SLVPDPATVP SHHAKDVNSV IRNLDIATMA VIAPTTLMHM HFINITLKDK VEKKDILSVL 250 260 270 280 290 300 ENTPRIVLIS SKYDAEATAE LVEVARDLKR DRNDIPEVMI FSDSIYVKDD EVMLMYAVHQ 310 320 330 340 ESIVVPENID AIRASMKLMS AEDSMRITNE SLGILKGYLI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and molecular evolution of the gene coding for glyceraldehyde-3-phosphate dehydrogenase in the thermoacidophilic archaebacterium Sulfolobus solfataricus." Arcari P., Russo A.D., Ianniciello G., Gallo M., Bocchini V. Biochem. Genet. 31:241-251(1993) [PubMed: 8259927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: DSM 5833 / MT-4.
[2]	"The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulfolobus solfataricus overlap by 8-bp. Isolation, sequencing of the genes and expression in Escherichia coli." Jones C.E., Fleming T.M., Cowan D.A., Littlechild J.A., Piper P.W. Eur. J. Biochem. 233:800-808(1995) [PubMed: 8521845] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2." Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C., Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T., Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E., Medina N. , Peng X., Penny S.L., She Q., St Jean A., van der Oost J., Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W. Genome 43:116-136(2000) [PubMed: 10701121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[4]	"The complete genome of the crenarchaeon Sulfolobus solfataricus P2." She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J. Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[5]	"Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus." Isupov M.N., Fleming T.M., Dalby A.R., Crowhurst G.S., Bourne P.C., Littlechild J.A. J. Mol. Biol. 291:651-660(1999) [PubMed: 10448043] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

X66409 Genomic DNA. Translation: CAA47040.1.
X80178 Genomic DNA. Translation: CAA56460.1.
Y18930 Genomic DNA. Translation: CAB57771.1.
AE006683 Genomic DNA. Translation: AAK40848.1.

PIR

S51230.
S63529.

RefSeq

NP_342058.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B7G	X-ray	2.05	O/Q	1-340	[»]

ModBase

Search...

Genome annotation databases

GeneID

1454815.

GenomeReviews

Gene locus SSO0528 in contig AE006641_GR.

KEGG

sso:SSO0528.

NMPDR

fig|273057.1.peg.481.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P39460.

Enzyme and pathway databases

BioCyc

SSOL273057:SSO0528-MON.

Family and domain databases

HAMAP

MF_00559.
[Tree]

InterPro

IPR000173. GlycerAld_3-P_DHase.
IPR006436. Glyceraldehyde-3-P_DHase_2_arc.
[Graphical view]

Pfam

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

PIRSF

PIRSF000149. GAP_DH. 1 hit.

ProDom

PD007761. GAPDH_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01546. GAPDH-II_archae. 1 hit.

PROSITE

PS00071. GAPDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

G3P_SULSO

Accession

Primary (citable) accession number: P39460

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	December 1, 2000
Last modified:	November 25, 2008
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)