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 C

Gene

ALDOC

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Pathway:iglycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
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, Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (EGM_20016)
  3. ATP-dependent 6-phosphofructokinase, ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase (EGM_03171)
  4. Fructose-bisphosphate aldolase (EGM_07550), Fructose-bisphosphate aldolase (EGM_07550), Fructose-bisphosphate aldolase (EGM_11628), Fructose-bisphosphate aldolase (EGM_11628), Fructose-bisphosphate aldolase (EGM_06789), Fructose-bisphosphate aldolase (EGM_06789), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase C (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase
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)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

GO - Biological processi

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 C (EC:4.1.2.13)
Alternative name(s):
Brain-type aldolase
Gene namesi
Name:ALDOC
ORF Names:QccE-19239, QccE-21970
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 364363Fructose-bisphosphate aldolase CPRO_0000216948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131N6-succinyllysineBy similarity
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei111 – 1111N6-acetyllysineBy similarity
Modified residuei119 – 1191PhosphothreonineBy similarity
Modified residuei132 – 1321PhosphoserineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei276 – 2761PhosphoserineBy similarity
Modified residuei309 – 3091PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

Homotetramer. Interacts with ATP6V1E1.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9GKW3.
SMRiQ9GKW3. Positions 3-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG002386.

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.

Q9GKW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE
60 70 80 90 100
NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD
110 120 130 140 150
KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC
160 170 180 190 200
VLKISERTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
210 220 230 240 250
RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYTPEEIA
260 270 280 290 300
MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC PLPRPWALTF
310 320 330 340 350
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG
360
GAAAQSLYIA NHAY
Length:364
Mass (Da):39,422
Last modified:January 23, 2007 - v3
Checksum:i0A6A5A6B333D197C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051116 mRNA. Translation: BAB18142.1.
AB169815 mRNA. Translation: BAE01896.1.
RefSeqiXP_005583297.1. XM_005583240.1.
XP_005583298.1. XM_005583241.1.
XP_005583299.1. XM_005583242.1.
XP_005583300.1. XM_005583243.1.
UniGeneiMfa.528.

Genome annotation databases

GeneIDi101865220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051116 mRNA. Translation: BAB18142.1.
AB169815 mRNA. Translation: BAE01896.1.
RefSeqiXP_005583297.1. XM_005583240.1.
XP_005583298.1. XM_005583241.1.
XP_005583299.1. XM_005583242.1.
XP_005583300.1. XM_005583243.1.
UniGeneiMfa.528.

3D structure databases

ProteinModelPortaliQ9GKW3.
SMRiQ9GKW3. Positions 3-344.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101865220.

Phylogenomic databases

HOVERGENiHBG002386.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

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. "Isolation of full-length cDNA clones from macaque brain cDNA libraries."
    Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.
  2. "DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."
    International consortium for macaque cDNA sequencing and analysis
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiALDOC_MACFA
AccessioniPrimary (citable) accession number: Q9GKW3
Secondary accession number(s): Q4R4S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 71 of the entry and version 3 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.

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.