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P16096

- ALFC_SPIOL

UniProt

P16096 - ALFC_SPIOL

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Protein

Fructose-bisphosphate aldolase, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931Substrate By similarity
Binding sitei183 – 1831Substrate By similarity
Active sitei223 – 2231Proton acceptor By similarity
Active sitei265 – 2651Schiff-base intermediate with dihydroxyacetone-P By similarity
Sitei394 – 3941Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate By similarity

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12899.
SABIO-RKP16096.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase, chloroplastic (EC:4.1.2.13)
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646Chloroplast1 PublicationAdd
BLAST
Chaini47 – 394348Fructose-bisphosphate aldolase, chloroplasticPRO_0000001113Add
BLAST

Proteomic databases

PRIDEiP16096.

Structurei

3D structure databases

ProteinModelPortaliP16096.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16096-1 [UniParc]FASTAAdd to Basket

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MASASLLKTS PVLDNPEFLK GQTLRIPSVA GVRFTPSGSS SLTVRASSYA    50
DELVKTAKTV ASPGRGILAM DESNATCGKR LASIGLENTE ANRQAYRTLL 100
ISAPGLGQYV SGAILFEETL YQSTTDGKKM VDVLIEQGIV PGIKVDKGWL 150
PLPGSNDESW CQGLDGLACR SAAYYQQGAR FAKWRTVVSI PNGPSALAVK 200
EAAWGLARYA AITQDNGLDP ILEPEIMLDG EHGIDRTFRV AQQVWAEVFF 250
NLAENNVLLE GSSLKPSMVG PGALSARKGP PEQVADYPLK LLHRRRGPVV 300
PGIMVLSGGQ SEVEATLNLN AMNQSPNPWH VSFSYARALQ NTCLKTWVEG 350
QENVKAQDFA CAKSNSLAQL GKYTGEGESE ERKKDMFVKA TLTY 394
Length:394
Mass (Da):42,468
Last modified:November 1, 1995 - v3
Checksum:i9D8A813E1636B274
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2634EGSS → RDP in CAA47293. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66814 mRNA. Translation: CAA47293.1.
PIRiS31090. ADSPAP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66814 mRNA. Translation: CAA47293.1 .
PIRi S31090. ADSPAP.

3D structure databases

ProteinModelPortali P16096.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P16096.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
BioCyci MetaCyc:MONOMER-12899.
SABIO-RK P16096.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view ]
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast and cytosol enzyme from spinach."
    Pelzer-Reith B., Penger A., Schnarrenberger C.
    Plant Mol. Biol. 21:331-340(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation and characterization of the cytosolic and chloroplast forms of spinach leaf fructose diphosphate aldolase."
    Lebherz H.G., Leadbetter M.M., Bradshaw R.A.
    J. Biol. Chem. 259:1011-1017(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 47-64.
  3. Bairoch A.
    Unpublished observations (NOV-1995)
    Cited for: IDENTIFICATION OF PROBABLE FRAMESHIFT.

Entry informationi

Entry nameiALFC_SPIOL
AccessioniPrimary (citable) accession number: P16096
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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