[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=9226260 [NCBI, ExPASy, EBI, Israel, Japan] Valverde F., Losada M., Serrano A.; "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."; J. Bacteriol. 179:4513-4522(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Schubert M., Brinkmann H., Cerff R.; Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1093/dnares/3.3.109; PubMed=8905231 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; DNA Res. 3:109-136(1996).
[4]	PROTEIN SEQUENCE OF 2-11. Valverde F., Serrano A.; Submitted (NOV-1995) to UniProtKB.

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: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X83564; CAA58550.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X86376; CAA60135.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000022; BAA18633.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S54141; S54141.

RefSeq

NP_442821.1; -.

3D structure databases

HSSP

P19866; 1NBO. [HSSP ENTRY / PDB]

SMR

P80505; 3-334.

ModBase

P80505.

Protein-protein interaction databases

IntAct

P80505; -.

Enzyme and pathway databases

BioCyc

SSP1148:SLL1342-MON; -.

Ontologies

GO:0015977;	Biological process: carbon utilization by fixation of carbon dioxide (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.

PANTHER

PTHR10836; GAP_DH; 1.

Pfam

PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000149; GAP_DH; 1.

PRINTS

PR00078; G3PDHDRGNASE.

TIGRFAMs

TIGR01534; GAPDH-I; 1.

PROSITE

PS00071; GAPDH; 1.

BLOCKS

P80505.

Genome annotation databases

GeneID

952066; -.

GenomeReviews

BA000022_GR; sll1342.

KEGG

syn:sll1342; -.

Phylogenomic databases

HOGENOM

P80505; -.

Genome annotation databases

CMR

P80505; sll1342.

Other

ProtoNet

P80505.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 337`	`336`	`Glyceraldehyde-3-phosphate dehydrogenase 2.`	`PRO_0000145709`
`NP_BIND`	`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).`
`ACT_SITE`	`154 154`		`Nucleophile (By similarity).`
`BINDING`	`35 35`		`NAD (By similarity).`
`BINDING`	`79 79`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`184 184`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`199 199`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`235 235`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`317 317`		`NAD (By similarity).`
`SITE`	`181 181`	`1`	`Activates thiol group during catalysis (By similarity).`
`CONFLICT`	`57 57`		`A -> G (in Ref. 1; CAA58550).`
`CONFLICT`	`162 163`		`FG -> IA (in Ref. 2; CAA60135/BAA18633).`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 36512 Da [This is the MW of the unprocessed precursor]

CRC64: FC8FF0E7FEAC1585 [This is a checksum on the sequence]

        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

P80505 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools