NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-349, AND PROTEIN SEQUENCE OF 1-32.
STRAIN=cv. Little Marvel, and cv. Sparkle;
TISSUE=Leaf;
DOI=10.1016/0003-9861(92)90112-A; PubMed=1524427 [NCBI, ExPASy, EBI, Israel, Japan]
Razdan K., Heinrikson R.L., Zurcher-Neely H., Morris P.W., Anderson L.E.;
"Chloroplast and cytoplasmic enzymes: isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases.";
Arch. Biochem. Biophys. 298:192-197(1992).

Comments

CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4 .
SUBCELLULAR LOCATION: Plastid, chloroplast.
SIMILARITY: Belongs to the class I 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

M97477; AAA33643.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S29048; S29048.

3D structure databases

HSSP

P14223; 1A5C. [HSSP ENTRY / PDB]

ModBase

Q01517.

Family and domain databases

InterPro

IPR000741; Aldolase_I.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR11627; Aldolase_I; 1.

Pfam

PF00274; Glycolytic; 1.
Pfam graphical view of domain structure.

ProDom

PD001128; Aldolase_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00158; ALDOLASE_CLASS_I; 1.

Other

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

Keywords

Chloroplast; Direct protein sequencing; Glycolysis; Lyase; Plastid; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 349`	`349`	`Fructose-bisphosphate aldolase 2, chloroplastic.`	`PRO_0000216926`
`ACT_SITE`	`177 177`		`Proton acceptor (By similarity).`
`ACT_SITE`	`219 219`		`Schiff-base intermediate with dihydroxyacetone-P (By similarity).`
`BINDING`	`47 47`		`Substrate (By similarity).`
`BINDING`	`137 137`		`Substrate (By similarity).`
`SITE`	`349 349`	`1`	`Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate (By similarity).`
`VARIANT`	`29 29`	`1`	`A -> W (in strain: cv. Little Marvel).`

Sequence information

Length: 349 AA [This is the length of the unprocessed precursor]

Molecular weight: 37827 Da [This is the MW of the unprocessed precursor]

CRC64: E50715D246B5D7D1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
GSYADELVKT AKTIASPGRG ILAMDESNAT CGKRLDSIGL ENTEANRQAW RTLLVTVPTL 

        70         80         90        100        110        120 
GEYISGAILF EETLYQSTVD GRKIVDVLVE QNIIPGIKVD KGLVPLAGSN NESWCQGLDG 

       130        140        150        160        170        180 
LASRSAAYYQ QGARFAKWRT VVSIPNGPSA LAVKEAAWGL ARYAAISQDN GLVPIVEPEI 

       190        200        210        220        230        240 
LLDGEHGIDR TFEVAQKVWA EVFYYLAENN VQFEGILLKP SMVTPGAESK DKASPTKVAE 

       250        260        270        280        290        300 
YTLNLLHRRI PPAVPGIMFL SGGQSEVEAT LNLNAMNKSP NPWHVSFSYA RALQNTALKT 

       310        320        330        340 
WGGLPENVKA AQEALLFRAK SNSLAQLGKY IGDGESEEAK KDCCQGYSY

Q01517 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