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

FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis (By similarity).
CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
COFACTOR: Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution (By similarity).
PATHWAY: Carbohydrate biosynthesis; Calvin cycle .
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4 .
SUBUNIT: Homodimer.
MISCELLANEOUS: This protein is encoded within the form II ribulose-bisphosphate carboxylase operon.
SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase 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; AAA26157.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D41080; D41080.

3D structure databases

HSSP

P42908; 1GVF. [HSSP ENTRY / PDB]

ModBase

P29271.

Ontologies

GO:0004332;	Molecular function: fructose-bisphosphate aldolase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
GO:0019253;	Biological process: reductive pentose-phosphate cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR006412; Fruct_bisP_Calv.
IPR000771; K_bP_aldolase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF01116; F_bP_aldolase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001359; F_bP_aldolase_II; 1.

ProDom

PD002376; K_bP_aldolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00167; cbbA; 1.
TIGR01521; FruBisAldo_II_B; 1.

PROSITE

PS00602; ALDOLASE_CLASS_II_1; 1.
PS00806; ALDOLASE_CLASS_II_2; 1.

Other

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

Keywords

Calvin cycle; Glycolysis; Lyase; Metal-binding; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 354`	`354`	`Fructose-bisphosphate aldolase 2.`	`PRO_0000178733`
`REGION`	`233 235`	`3`	`Dihydroxyacetone phosphate binding (By similarity).`
`REGION`	`275 278`	`4`	`Dihydroxyacetone phosphate binding (By similarity).`
`ACT_SITE`	`83 83`		`Proton donor (By similarity).`
`METAL`	`84 84`		`Zinc 1; catalytic (By similarity).`
`METAL`	`105 105`		`Zinc 2 (By similarity).`
`METAL`	`142 142`		`Zinc 2 (By similarity).`
`METAL`	`198 198`		`Zinc 1; catalytic (By similarity).`
`METAL`	`232 232`		`Zinc 1; catalytic (By similarity).`
`BINDING`	`50 50`		`Glyceraldehyde 3-phosphate (By similarity).`
`BINDING`	`199 199`		`Dihydroxyacetone phosphate; via amide nitrogen (By similarity).`

Sequence information

Length: 354 AA [This is the length of the unprocessed precursor]

Molecular weight: 38269 Da [This is the MW of the unprocessed precursor]

CRC64: 9F547E84FC72ACF5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALITLRQLL DHAAEQGYGV PAFNINNMEQ GLAIMEAARA CDAPVIIQAS RGARSYANDI 

        70         80         90        100        110        120 
MLAKMIEALA AIYPEIPLCM HQDHGNNEAT CMTAIRHGFT SVMMDGSLKA DAKTPADYDY 

       130        140        150        160        170        180 
NVDITARVSH MAHWVGASVE GELGVLGSLE TGESEAEDGH GAEGKLDHSQ LLTDPDQAVD 

       190        200        210        220        230        240 
FVKKTQVDAL AIACGTSHGA YKFSRKPDGE ILAMSVIEAI HKKLPDTHLV MHGSSSVPQE 

       250        260        270        280        290        300 
LQDIINAFGG AMPQTFGVPV EEIVRGIKMG VRKVNIDTDC RMAMTGQFRR IAQQTPSEFD 

       310        320        330        340        350 
PRKFLKPAMD AMRDLCKQRL EAFGTAGQAG KIRIIPMDDM AKRYASGALA PKTA

P29271 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