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Protein

Fructose-bisphosphate aldolase 1, cytoplasmic

Gene

FBA1

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis (By similarity). Involved in gibberellin-mediated root growth. May be regulated by CDPK13. Associates with vacuolar proton ATPase (V-ATPase) and may regulate the V-ATPase-mediated control of root cell elongation (PubMed:15821984).By similarity1 Publication

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.Curated
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (Os06g0256500), Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (Os08g0478800), Glucose-6-phosphate isomerase (OsJ_27683), Glucose-6-phosphate isomerase (Os06g0256500), Glucose-6-phosphate isomerase, cytosolic A (Os03g0776000), Glucose-6-phosphate isomerase, cytosolic B (Os06g0256500), Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (Os09g0465600)
  3. ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (PFP-ALPHA), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (Os02g0714200), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (Os09g0298100), ATP-dependent 6-phosphofructokinase (Os09g0415800), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (PFK), ATP-dependent 6-phosphofructokinase (Os05g0524400), ATP-dependent 6-phosphofructokinase (Os10g0405600), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta (Os06g0247500), ATP-dependent 6-phosphofructokinase (PFK), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (P0652D10.35), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (P0410E11.122), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (PFPA4), Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha (Os06g0326400), ATP-dependent 6-phosphofructokinase (PFK)
  4. Fructose-bisphosphate aldolase, chloroplastic (ALDP), Fructose-bisphosphate aldolase (OsJ_21934), Fructose-bisphosphate aldolase (OsJ_00159), Fructose-bisphosphate aldolase (Os08g0120600), Fructose-bisphosphate aldolase (LOC_Os11g07020), Fructose-bisphosphate aldolase (Os06g0608700), Fructose-bisphosphate aldolase 1, cytoplasmic (FBA1), Fructose-bisphosphate aldolase (LOC_Os11g07020), Fructose-bisphosphate aldolase 2, cytoplasmic (FBA2), Fructose-bisphosphate aldolase (Os01g0118000), Fructose-bisphosphate aldolase (LOC_Os12g07210), Fructose-bisphosphate aldolase 3, cytoplasmic (FBA3)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei39SubstrateBy similarity1
Active sitei183Proton acceptorBy similarity1
Active sitei225Schiff-base intermediate with dihydroxyacetone-PBy similarity1
Binding sitei298SubstrateBy similarity1
Sitei358Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphateBy similarity1

GO - Molecular functioni

  • fructose-bisphosphate aldolase activity Source: Gramene

GO - Biological processi

  • glycolytic process Source: Gramene
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis, Stress response

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiR-OSA-114608. Platelet degranulation.
R-OSA-6798695. Neutrophil degranulation.
R-OSA-70171. Glycolysis.
R-OSA-70263. Gluconeogenesis.
R-OSA-70350. Fructose catabolism.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase 1, cytoplasmicCurated (EC:4.1.2.13By similarity)
Alternative name(s):
Cytoplasmic aldolase1 Publication
Short name:
cALD1 Publication
Gravity-specific protein GSC 2331 Publication
Gene namesi
Name:FBA1Curated
Synonyms:FBA1 Publication
Ordered Locus Names:Os05g0402700Imported, LOC_Os05g33380Curated
ORF Names:OSJNBa0035J16.18Imported, OSJNBb0006J12.6Imported
OrganismiOryza sativa subsp. japonica (Rice)
Taxonomic identifieri39947 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
Proteomesi
  • UP000059680 Componenti: Chromosome 5

Subcellular locationi

  • Cytoplasmcytosol By similarity

GO - Cellular componenti

  • cytoplasm Source: Gramene
  • cytosol Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002169221 – 358Fructose-bisphosphate aldolase 1, cytoplasmicAdd BLAST358

Proteomic databases

PaxDbiP17784.
PRIDEiP17784.

Expressioni

Tissue specificityi

Expressed in callus.1 Publication

Inductioni

By gravity stress (PubMed:1363521). Induced by gibberellin (PubMed:15821984).2 Publications

Gene expression databases

GenevisibleiP17784. OS.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi39947.LOC_Os05g33380.1.

Structurei

3D structure databases

ProteinModelPortaliP17784.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni266 – 268Substrate bindingBy similarity3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1557. Eukaryota.
COG3588. LUCA.
HOGENOMiHOG000220876.
InParanoidiP17784.
KOiK01623.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. 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.

P17784-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAYCGKYKD ELIKNAAYIG TPGKGILAAD ESTGTIGKRF ASINVENVEE
60 70 80 90 100
NRRSLRELLF CTPGALQYLS GVILFEETLY QKTKDGKPFV DVLKEGGVLP
110 120 130 140 150
GIKVDKGTIE VAGTEKETTT QGHDDLGKRC AKYYEAGARF AKWRAVLKIG
160 170 180 190 200
PNEPSQLAID LNAQGLARYA IICQENGLVP IVEPEILVDG PHDIDRCAYV
210 220 230 240 250
SEVVLAACYK ALNEHHVLLE GTLLKPNMVT PGSDAKKVSP EVIAEYTVRT
260 270 280 290 300
LQRTVPAAVP AIVFLSGGQS EEEATLNLNA MNKLSTKKPW SLSFSFGRAL
310 320 330 340 350
QQSTLKAWSG KAENIEKARA AFLTRCKANS EATLGTYKGD AVLGEGASES

LHVKDYKY
Length:358
Mass (Da):38,863
Last modified:October 25, 2005 - v2
Checksum:i2C5BBE05DD1AA83E
GO

Sequence cautioni

The sequence AAB25853 differs from that shown. Sequencing errors.Curated
The sequence AAB25853 differs from that shown. Reason: Frameshift at several positions.Curated
The sequence AAB25853 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated
The sequence BAA01911 differs from that shown. Sequencing errors.Curated
The sequence BAA01911 differs from that shown. Reason: Frameshift at several positions.Curated
The sequence BAA01911 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated
The sequence BAF17408 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAS93924 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EEE63668 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti160D → H in CAA37290 (PubMed:2374721).Curated1
Sequence conflicti196R → P in CAA37290 (PubMed:2374721).Curated1
Sequence conflicti271E → K in CAA37290 (PubMed:2374721).Curated1
Sequence conflicti276L → R in CAA37290 (PubMed:2374721).Curated1
Sequence conflicti313E → A in CAA37290 (PubMed:2374721).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53130 mRNA. Translation: CAA37290.1.
AY522925 mRNA. Translation: AAS05825.1.
EU267960 mRNA. Translation: ACA50482.1.
GQ848038 mRNA. Translation: ADM86851.1.
AC120991 Genomic DNA. Translation: AAT85207.1.
AC135418 Genomic DNA. Translation: AAT85154.1.
AP008211 Genomic DNA. Translation: BAF17408.1. Sequence problems.
AP014961 Genomic DNA. Translation: BAS93924.1. Sequence problems.
CM000142 Genomic DNA. Translation: EEE63668.1. Sequence problems.
D11137 mRNA. Translation: BAA01911.1. Sequence problems.
S56877 mRNA. Translation: AAB25853.1. Sequence problems.
PIRiJQ0543. ADRZY.
T04310.
RefSeqiXP_015639252.1. XM_015783766.1.
UniGeneiOs.7991.

Genome annotation databases

EnsemblPlantsiOS05T0402700-01; OS05T0402700-01; OS05G0402700.
GeneIDi4338737.
GrameneiOS05T0402700-01; OS05T0402700-01; OS05G0402700.
KEGGiosa:4338737.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53130 mRNA. Translation: CAA37290.1.
AY522925 mRNA. Translation: AAS05825.1.
EU267960 mRNA. Translation: ACA50482.1.
GQ848038 mRNA. Translation: ADM86851.1.
AC120991 Genomic DNA. Translation: AAT85207.1.
AC135418 Genomic DNA. Translation: AAT85154.1.
AP008211 Genomic DNA. Translation: BAF17408.1. Sequence problems.
AP014961 Genomic DNA. Translation: BAS93924.1. Sequence problems.
CM000142 Genomic DNA. Translation: EEE63668.1. Sequence problems.
D11137 mRNA. Translation: BAA01911.1. Sequence problems.
S56877 mRNA. Translation: AAB25853.1. Sequence problems.
PIRiJQ0543. ADRZY.
T04310.
RefSeqiXP_015639252.1. XM_015783766.1.
UniGeneiOs.7991.

3D structure databases

ProteinModelPortaliP17784.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os05g33380.1.

Proteomic databases

PaxDbiP17784.
PRIDEiP17784.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiOS05T0402700-01; OS05T0402700-01; OS05G0402700.
GeneIDi4338737.
GrameneiOS05T0402700-01; OS05T0402700-01; OS05G0402700.
KEGGiosa:4338737.

Phylogenomic databases

eggNOGiKOG1557. Eukaryota.
COG3588. LUCA.
HOGENOMiHOG000220876.
InParanoidiP17784.
KOiK01623.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
ReactomeiR-OSA-114608. Platelet degranulation.
R-OSA-6798695. Neutrophil degranulation.
R-OSA-70171. Glycolysis.
R-OSA-70263. Gluconeogenesis.
R-OSA-70350. Fructose catabolism.

Gene expression databases

GenevisibleiP17784. OS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALFC1_ORYSJ
AccessioniPrimary (citable) accession number: P17784
Secondary accession number(s): B7SDE6
, Q07077, Q0DIB5, Q6QWQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 25, 2005
Last modified: November 30, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants silencing FBA1 display reduced root length.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Oryza sativa (rice)
    Index of Oryza sativa entries and their corresponding gene designations
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.