Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q42690 (ALFC_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase 1, chloroplastic
EC=4.1.2.13
Gene names
Name:ALDCHL
ORF Names:CHLREDRAFT_24459
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii) [Reference proteome]
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 377Fructose-bisphosphate aldolase 1, chloroplasticPRO_0000001111

Sites

Active site2041Proton acceptor By similarity
Active site2461Schiff-base intermediate with dihydroxyacetone-P By similarity
Binding site741Substrate By similarity
Binding site1641Substrate By similarity
Site3771Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate By similarity

Experimental info

Sequence conflict16 – 2712AGRSR…VVVRA → LAALAAPSLCAP in AAC60574. Ref.1
Sequence conflict16 – 2712AGRSR…VVVRA → LAALAAPSLCAP in CAA49590. Ref.1
Sequence conflict133 – 1397LSNTNGE → CPTPTM in AAC60574. Ref.1
Sequence conflict133 – 1397LSNTNGE → CPTPTM in CAA49590. Ref.1
Sequence conflict148 – 1525LDKRC → WTSA in AAC60574. Ref.1
Sequence conflict148 – 1525LDKRC → WTSA in CAA49590. Ref.1
Sequence conflict178 – 1836IAARDC → MLPRL in AAC60574. Ref.1
Sequence conflict178 – 1836IAARDC → MLPRL in CAA49590. Ref.1
Sequence conflict240 – 2412FE → LQ in AAC60574. Ref.1
Sequence conflict240 – 2412FE → LQ in CAA49590. Ref.1
Sequence conflict274 – 2807RRRVPPA → AARAPP in AAC60574. Ref.1
Sequence conflict274 – 2807RRRVPPA → AARAPP in CAA49590. Ref.1
Sequence conflict3211Q → T in AAC60574. Ref.1
Sequence conflict3211Q → T in CAA49590. Ref.1
Sequence conflict330 – 3345GKPEN → ASPRT in AAC60574. Ref.1
Sequence conflict330 – 3345GKPEN → ASPRT in CAA49590. Ref.1
Sequence conflict338 – 3469AQAALLKRA → PRLAAQAR in AAC60574. Ref.1
Sequence conflict338 – 3469AQAALLKRA → PRLAAQAR in CAA49590. Ref.1
Sequence conflict3741G → GKG in AAC60574. Ref.1
Sequence conflict3741G → GKG in CAA49590. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q42690 [UniParc].

Last modified February 22, 2012. Version 2.
Checksum: 76B5BED0C422E77C

FASTA37740,985
        10         20         30         40         50         60 
MALMMKSSAS LKAVSAGRSR RAVVVRAGKY DEELIKTAGT VASKGRGILA MDESNATCGK 

        70         80         90        100        110        120 
RLDSIGVENT EENRRAYREL LVTAPGLGQY ISGAILFEET LYQSTASGKK FVDVMKEQNI 

       130        140        150        160        170        180 
VPGIKVDKGL VPLSNTNGES WCMGLDGLDK RCAEYYKAGA RFAKWRSVVS IPHGPSIIAA 

       190        200        210        220        230        240 
RDCAYGLARY AAIAQNAGLV PIVEPEVLLD GEHDIDRCLE VQEAIWAETF KYMADNKVMF 

       250        260        270        280        290        300 
EGILLKPAMV TPGADCKNKA GPAKVAEYTL KMLRRRVPPA VPGIMFLSGG QSELESTLNL 

       310        320        330        340        350        360 
NAMNQSPNPW HVSFSYARAL QNTVLKTWQG KPENVQAAQA ALLKRAKANS DAQQGKYDAT 

       370 
TEGKEAAQGM YEKGYVY

« Hide

References

« Hide 'large scale' references
[1]"Expression and sequence of the only detectable aldolase in Chlamydomonas reinhardtii."
Schnarrenberger C., Pelzer-Reith B., Yatsuki H., Freund S., Jacobshagen S., Hori K.
Arch. Biochem. Biophys. 313:173-178(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"The plastid aldolase gene from Chlamydomonas reinhardtii: intron/exon organization, evolution, and promoter structure."
Pelzer-Reith B., Freund S., Schnarrenberger C., Yatsuki H., Hori K.
Mol. Gen. Genet. 248:481-486(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The Chlamydomonas genome reveals the evolution of key animal and plant functions."
Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P. expand/collapse author list , Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.
Science 318:245-250(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC-503.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X69969 mRNA. Translation: CAA49590.1.
S72951 Genomic DNA. Translation: AAC60574.1.
X85495 Genomic DNA. No translation available.
DS496165 Genomic DNA. Translation: EDO97897.1.
PIRS48639.
RefSeqXP_001700659.1. XM_001700607.1.
UniGeneCre.9890.

3D structure databases

ProteinModelPortalQ42690.
SMRQ42690. Positions 28-363.
ModBaseSearch...

Protein-protein interaction databases

STRING3055.JGI24459.

Proteomic databases

PRIDEQ42690.
ProMEXQ42690.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5726208.
KEGGcre:CHLREDRAFT_24459.

Phylogenomic databases

eggNOGCOG3588.
KOK01623.
OMAAEAKEGM.
ProtClustDBCLSN2923487.

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALFC_CHLRE
AccessionPrimary (citable) accession number: Q42690
Secondary accession number(s): A8JE10, Q36725
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 22, 2012
Last modified: April 3, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents