Reviewed, UniProtKB/Swiss-Prot P80505 (G3P2_SYNY3)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
    EC=1.2.1.59
Alternative name(s):
    NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
    GAPDH 2
      Short name=GAP-2

Gene names

Name:	gap2
Ordered Locus Names:	sll1342

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Works with both NADP and NAD.
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
Molecular function	Oxidoreductase
Technical term	Complete proteome 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 (NAD(P)+) (phosphorylating) activity Inferred from electronic annotation. Source: EC glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 337	336	Glyceraldehyde-3-phosphate dehydrogenase 2		PRO_0000145709
Regions
	Nucleotide binding	11 – 12	2	NAD By similarity
	Region	153 – 155	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	212 – 213	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	154	1	Nucleophile By similarity
	Binding site	35	1	NAD By similarity
	Binding site	79	1	NAD; via carbonyl oxygen By similarity
	Binding site	184	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	199	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	235	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	317	1	NAD By similarity
	Site	181	1	Activates thiol group during catalysis By similarity
Experimental info
	Sequence conflict	57	1	A → G in CAA58550. Ref.1
	Sequence conflict	162 – 163	2	FG → IA in CAA60135. Ref.2
	Sequence conflict	162 – 163	2	FG → IA in BAA18633. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P80505-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FC8FF0E7FEAC1585	FASTA	337	36,512
	10 20 30 40 50 60 MTRVAINGFG RIGRNFLRCW LGRTDSQLEV VGINDTSDPR TNAHLLRYDS MLGKLDADIS 70 80 90 100 110 120 ADENSITVNG KTIKCVSDRN PLNLPWAEWN VDLVIEATGV FVTHEGATKH VQAGAKKVLI 130 140 150 160 170 180 TAPGKGPNIG TYVVGVNAHE YKHEEYEVIS NASCTTNCLA PFGKVINDNF GIIKGTMTTT 190 200 210 220 230 240 HSYTGDQRIL DASHRDLRRA RAAAVNIVPT STGAAKAVAL VIPELQGKLN GIALRVPTPN 250 260 270 280 290 300 VSVVDLVVQV EKNTIAEQVN GVLKEAANTS LKGVLEYTDL ELVSSDFRGT DCSSTVDGSL 310 320 330 TMVMGGDMVK VIAWYDNEWG YSQRVVDLAE IVAKNWK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803." Valverde F., Losada M., Serrano A. J. Bacteriol. 179:4513-4522(1997) [PubMed: 9226260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Schubert M., Brinkmann H., Cerff R. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Valverde F., Serrano A. Submitted (NOV-1995) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X83564 Genomic DNA. Translation: CAA58550.1. X86376 Genomic DNA. Translation: CAA60135.1. BA000022 Genomic DNA. Translation: BAA18633.1.
PIR	S54141.
RefSeq	NP_442821.1.
3D structure databases
HSSP	HSSP built from PDB template 1NBO based on UniProtKB P19866.
SMR	P80505. Positions 3-334.
ModBase	Search...
Genome annotation databases
GeneID	952066.
GenomeReviews	Gene locus sll1342 in contig BA000022_GR.
KEGG	syn:sll1342.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P80505.
Enzyme and pathway databases
BioCyc	SSP1148:SLL1342-MON.
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

G3P2_SYNY3

Accession

Primary (citable) accession number: P80505

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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