NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
PubMed=12125824 [NCBI, ExPASy, EBI, Israel, Japan]
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.;
"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.";
J. Mol. Microbiol. Biotechnol. 4:453-461(2002).

Comments

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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

AE008384; AAM32478.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_634806.1; -.

3D structure databases

HSSP

P10618; 1CF2. [HSSP ENTRY / PDB]

ModBase

Q8PTD3.

Enzyme and pathway databases

BioCyc

MMAZ192952:MM2782-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0043891;	Molecular function: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity (inferred from electronic annotation from EC).
GO:0004365;	Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from HAMAP).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00559; -; 1.
PBIL [Tree]

InterPro

IPR000173; GlycerAld_3-P_DHase.
IPR006436; Glyceraldehyde-3-P_DHase_2_arc.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

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

PIRSF

PIRSF000149; GAP_DH; 1.

ProDom

PD007761; GAPDH_like; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01546; GAPDH-II_archae; 1.

PROSITE

PS00071; GAPDH; 1.

Genome annotation databases

GeneID

1481124; -.

GenomeReviews

AE008384_GR; MM_2782.

KEGG

mma:MM_2782; -.

NMPDR

fig|192952.1.peg.2782; -.

Phylogenomic databases

HOGENOM

Q8PTD3; -.

Genome annotation databases

CMR

Q8PTD3; MM_2782.

Other

ProtoNet

Q8PTD3.

UniRef

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

Keywords

Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 335`	`335`	`Glyceraldehyde-3-phosphate dehydrogenase.`	`PRO_0000145725`
`NP_BIND`	`13 14`	`2`	`NAD (By similarity).`
`REGION`	`140 142`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`195 196`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`141 141`		`Nucleophile (By similarity).`
`BINDING`	`111 111`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`169 169`		`NAD (By similarity).`
`BINDING`	`171 171`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`300 300`		`NAD; via carbonyl oxygen (By similarity).`

Sequence information

Length: 335 AA [This is the length of the unprocessed precursor]

Molecular weight: 36611 Da [This is the MW of the unprocessed precursor]

CRC64: 2AA26758A387D46E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKAKIAVNG YGTIGKRVAD AVQAQDDMEI IGVSKTKPNY EAAVAHQKGY DLFAPASNSG 

        70         80         90        100        110        120 
AFEKAGIPLA GTIEEMVEKA DLVVDCTPGG IGEANKPMYE KAGVKAIWQG GEDHELAGFS 

       130        140        150        160        170        180 
FNAASNYEGA LGRDLVRVVS CNTTGLCRVI YPIDRELGVK KVRVTLARRA TDPNDIKKGP 

       190        200        210        220        230        240 
INAIVPDPIK LPSHHGPDIK SVLPHINITT AALKIPTTLM HLHTVNMEVN TDCTAEDINR 

       250        260        270        280        290        300 
IFSSQSRIRF MSQGINSTAE IIELARDMGR PRNDMWENCI WPESITVHER EFYFFQAIHQ 

       310        320        330 
ESIVVPETVD AIRAMMELES DGAKSIQKTN KAIGL

Q8PTD3 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