Reviewed, UniProtKB/Swiss-Prot Q9YFS9 (G3P_AERPE)

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
Ordered Locus Names:	APE_0171.1

Organism

Aeropyrum pernix [Complete proteome] [HAMAP]

Taxonomic identifier

56636 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H. HAMAP MF_00559
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. HAMAP MF_00559
Subunit structure	Homotetramer By similarity. HAMAP MF_00559
Subcellular location	Cytoplasm By similarity HAMAP MF_00559.
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	Complete proteome
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: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADP or NADPH 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 – 343	343	Glyceraldehyde-3-phosphate dehydrogenase HAMAP MF_00559		PRO_0000145715
Regions
	Nucleotide binding	13 – 14	2	NAD By similarity
	Region	141 – 143	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	196 – 197	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	142	1	Nucleophile By similarity
	Binding site	112	1	NAD; via amide nitrogen By similarity
	Binding site	170	1	NAD By similarity
	Binding site	303	1	NAD; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YFS9-1 [UniParc]. Last modified May 27, 2002. Version 2. Checksum: DA75B0577A5A64CB	FASTA	343	37,173
	10 20 30 40 50 60 MSVVKVGVNG FGTIGRRVAL AITLQKDMKL VGVVKRTPDY AALYAASRGI PIYTPTAKEA 70 80 90 100 110 120 EEFEKRGIKV GGTLRELLAR VDVVVDATPE GQGAKNKPLY REAGVKQVYQ GGEKPEVAEA 130 140 150 160 170 180 SFSTLCNYEE SKGRGSLRVV SCNTTGLLRL ICTLNREFGV ESVRAVLVRR GADPKEVKKG 190 200 210 220 230 240 PIDSIVLNPP TLPSHHAVDV RTVLPWLDIK TAAVAVPTTF MHMHHVTLKL AKPVEKREVL 250 260 270 280 290 300 ETLASAPRIM LVSSGDTGIK STSQLVDAAR LSRMGYDIPE LVVFEESVAV DGREVMLFQA 310 320 330 340 VHQESIVVPE NIDAIRAVAS SPLTLDETLK ATDGSLGLRK TLW

References

[1]

"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000002 Genomic DNA. Translation: BAA79082.2.
PIR	H72772.
RefSeq	NP_147019.2.
3D structure databases
SMR	Q9YFS9. Positions 3-342.
ModBase	Search...
Genome annotation databases
GeneID	1445701.
GenomeReviews	Gene locus APE_0171.1 in contig BA000002_GR.
KEGG	ape:APE_0171.1.
NMPDR	fig|272557.1.peg.126.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG392099.
OMA	ESHPIAG.
Enzyme and pathway databases
BioCyc	APER272557:APE0171-MONOMER.
BRENDA	1.2.1.59. 256344.
Family and domain databases
HAMAP	MF_00559. G3P_dehdrog_arch. [Tree]
InterPro	IPR020830. GlycerAld_3-P_DH_AS. IPR020829. GlycerAld_3-P_DH_cat. IPR020831. GlycerAld_3-P_DH_family. IPR020828. GlycerAld_3-P_DH_NAD(P)_bd. IPR000173. GlycerAld_3-P_DH_subfam. IPR006436. Glyceraldehyde-3-P_DH_2_arc. 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.
SMART	SM00846. Gp_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01546. GAPDH-II_archae. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P_AERPE

Accession

Primary (citable) accession number: Q9YFS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 27, 2002
Last modified:	February 9, 2010
This is version 72 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)