NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1939098 [NCBI, ExPASy, EBI, Israel, Japan]
Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.;
"Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II CO2 fixation operon of Rhodobacter sphaeroides.";
J. Biol. Chem. 266:20447-20452(1991).

Comments

CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + NAD⁺ = 3-phospho-D-glyceroyl phosphate + NADH.
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: This protein is encoded within the form II ribulose-bisphosphate carboxylase operon.
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

M68914; AAA26156.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C41080; C41080.

3D structure databases

HSSP

P00362; 1NQO. [HSSP ENTRY / PDB]

ModBase

P29272.

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.

PS00071; GAPDH; 1.

Other

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

Keywords

Cytoplasm; Glycolysis; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 333`	`333`	`Glyceraldehyde-3-phosphate dehydrogenase B.`	`PRO_0000145675`
`NP_BIND`	`12 13`	`2`	`NAD (By similarity).`
`REGION`	`150 152`	`3`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`REGION`	`209 210`	`2`	`Glyceraldehyde 3-phosphate binding (By similarity).`
`ACT_SITE`	`151 151`		`Nucleophile (By similarity).`
`BINDING`	`36 36`		`NAD (By similarity).`
`BINDING`	`80 80`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`181 181`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`196 196`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`232 232`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`314 314`		`NAD (By similarity).`
`SITE`	`178 178`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 333 AA [This is the length of the unprocessed precursor]

Molecular weight: 35679 Da [This is the MW of the unprocessed precursor]

CRC64: B072F443A20C3AFD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTIRVAINGF GRIGRNVLRA IVESGRTDIE VVAINDLGQV ETNAHLLRFD SVHGRFPAKV 

        70         80         90        100        110        120 
TSGDDWIDVG RGPIKVTAIR NPAELPWAGV DMAMECTGIF TTKEKAAAHL QNGAKRVLVS 

       130        140        150        160        170        180 
APCDGADRTI VYGVNHATLT ADDLVVSNAS CTTNCLSPVA KVLHDAIGIA KGFMTTIHSY 

       190        200        210        220        230        240 
TGDQPTLDTM HKDLYRARAA ALSMIPTSTG AAKAVGLVLP ELKGRLDGVS IRVPTPNVSV 

       250        260        270        280        290        300 
VDLVFEAARD TTVEEVNAAI EAAACGPLKG VLGFTTEPNV SSDFNHDPHS SVFHMDQTKV 

       310        320        330 
MEGRMVRILS WYDNEWGFSN RMADTAVAMG RLL

P29272 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