NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25905 / AMRC-C165 / DSM 1728 / IFO 15155 / JCM 9062;
DOI=10.1038/35035069; PubMed=11029001 [NCBI, ExPASy, EBI, Israel, Japan]
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.";
Nature 407:508-513(2000).

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

AL445066; CAC12230.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_394562.1; -.

3D structure databases

HSSP

P10618; 1CF2. [HSSP ENTRY / PDB]

ModBase

Q9HJ69.

Enzyme and pathway databases

BioCyc

TACI273075:TA1103-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.
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.

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.

ProtoNet

Q9HJ69.

Genome annotation databases

1456612; -.

AL139299_GR; Ta1103.

tac:Ta1103; -.

fig|273075.1.peg.1084; -.

Phylogenomic databases

HOGENOM

Q9HJ69; -.

Genome annotation databases

CMR

Q9HJ69; Ta1103.

Other

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`	`1 338`	`338`	`Glyceraldehyde-3-phosphate dehydrogenase.`	`PRO_0000145737`
`NP_BIND`	`11 12`	`2`	`NAD (By similarity).`
`REGION`	`138 140`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`192 193`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`139 139`		`Nucleophile (By similarity).`
`BINDING`	`109 109`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`167 167`		`NAD (By similarity).`
`BINDING`	`169 169`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`299 299`		`NAD; via carbonyl oxygen (By similarity).`

Sequence information

Length: 338 AA [This is the length of the unprocessed precursor]

Molecular weight: 37784 Da [This is the MW of the unprocessed precursor]

CRC64: 8CEA4DF107909AE5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIRVGINGYG TIGRRVARAV SLQDDMIVTG IVKTKPDYVS MVASRDFKIF VPDKSYEKAF 

        70         80         90        100        110        120 
QDAGIKVEGT VENLIDDSEI IVDATPEGQG EKNKDLYVKR RIKAIFEGGE EPEIAQASFN 

       130        140        150        160        170        180 
AYSNFEEARS KDYVRVVSCN TTALARTLHP LRERFGIRYV DATIVRRATD PNDSKKGPIN 

       190        200        210        220        230        240 
AVEPSLSIPS HHAPDLRTVM SGLNVSTIAI KAPTTLMHVH AVRVELEKDA SKNDVIEAWR 

       250        260        270        280        290        300 
SYRRIMEIGK NSGITSTGQM MDLAREFGRD RSDLYEIAVW SQSVSVQGNH VSYIQAVHQE 

       310        320        330 
SDVVPENVDA IRSMFDIADR DRSVSMTDSK LKIEKRVF

Q9HJ69 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