Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-bisphosphate aldolase A

Gene

ALDOA

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity).By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate
Binding sitei147 – 1471Substrate
Active sitei188 – 1881Proton acceptorBy similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P
Sitei364 – 3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB

GO - Biological processi

  1. glycolytic process Source: UniProtKB
  2. protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase A (EC:4.1.2.13)
Alternative name(s):
Muscle-type aldolase
Gene namesi
Name:ALDOA
OrganismiPan troglodytes (Chimpanzee)
Taxonomic identifieri9598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
ProteomesiUP000002277: Unplaced

Subcellular locationi

CytoplasmmyofibrilsarcomereI band. CytoplasmmyofibrilsarcomereM line
Note: In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca2+.By similarity

GO - Cellular componenti

  1. I band Source: UniProtKB-SubCell
  2. M band Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 364363Fructose-bisphosphate aldolase APRO_0000295307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei42 – 421N6-acetyllysineBy similarity
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei111 – 1111N6-malonyllysineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei312 – 3121N6-malonyllysineBy similarity
Modified residuei330 – 3301N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiA5A6I5.

Interactioni

Subunit structurei

Homotetramer. Interacts with SNX9 and WAS. Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+ (By similarity).By similarity

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000055755.

Structurei

3D structure databases

ProteinModelPortaliA5A6I5.
SMRiA5A6I5. Positions 2-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiA5A6I5.
KOiK01623.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
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.

A5A6I5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE
60 70 80 90 100
NTEENRRFYR QLLLTADDRV NPCIVGVILF HETLYQKADD GRPFPQVIKS
110 120 130 140 150
KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC
160 170 180 190 200
VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIAEPE ILPDGDHDLK
210 220 230 240 250
RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKFSHEEIA
260 270 280 290 300
MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF
310 320 330 340 350
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG
360
AAASESLFVS NHAY
Length:364
Mass (Da):39,434
Last modified:June 12, 2007 - v1
Checksum:iB3D6546B86D4E604
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB222113 mRNA. Translation: BAF62358.1.
RefSeqiNP_001138305.1. NM_001144833.1.
UniGeneiPtr.406.

Genome annotation databases

GeneIDi454362.
KEGGiptr:454362.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB222113 mRNA. Translation: BAF62358.1.
RefSeqiNP_001138305.1. NM_001144833.1.
UniGeneiPtr.406.

3D structure databases

ProteinModelPortaliA5A6I5.
SMRiA5A6I5. Positions 2-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000055755.

Proteomic databases

PRIDEiA5A6I5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi454362.
KEGGiptr:454362.

Organism-specific databases

CTDi226.

Phylogenomic databases

eggNOGiCOG3588.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiA5A6I5.
KOiK01623.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Miscellaneous databases

NextBioi20836037.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome."
    Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M.
    Gene 399:1-10(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cerebellum.

Entry informationi

Entry nameiALDOA_PANTR
AccessioniPrimary (citable) accession number: A5A6I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: June 12, 2007
Last modified: March 4, 2015
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.