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P53448

- ALDOC_CARAU

UniProt

P53448 - ALDOC_CARAU

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Protein

Fructose-bisphosphate aldolase C

Gene

aldoc

Organism
Carassius auratus (Goldfish)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561SubstrateBy similarity
Binding sitei147 – 1471SubstrateBy similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-PBy similarity
Sitei363 – 3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphateBy similarity

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB

GO - Biological processi

  1. fructose 1,6-bisphosphate metabolic process Source: UniProtKB
  2. glycolytic process Source: UniProtKB-UniPathway
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
OrganismiCarassius auratus (Goldfish)
Taxonomic identifieri7957 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeCarassius

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 363362Fructose-bisphosphate aldolase CPRO_0000216953Add
BLAST

Proteomic databases

PRIDEiP53448.

Expressioni

Tissue specificityi

Expressed in brain but not in liver or muscle.1 Publication

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP53448.
SMRiP53448. Positions 3-363.
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.

P53448 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTHQYPALTT EQKRELQDIA QRIVAPGKGI LAADESTGSM AKRLNPIGVE
60 70 80 90 100
NTEENRRLYR QLLFTADERM DKCIGGVIFF HETLYQKADD GTPFAKMIKD
110 120 130 140 150
RGIVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRS
160 170 180 190 200
VLKISETSPS ELAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
210 220 230 240 250
RCQYVTEKVL AACYKALSDH HVYLEGTLLK PNMVTAGHSC PTKFSNQEIA
260 270 280 290 300
MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINNC PLTKPWALTF
310 320 330 340 350
SYGRALQASA LSAWRGVKEN EKAATEEFLK RAEANGLAAQ GKYVSSGMDG
360
SAGQSLYVAN HAY
Length:363
Mass (Da):39,475
Last modified:January 23, 2007 - v2
Checksum:i23ED53BABED42327
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U36777 mRNA. Translation: AAA84887.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U36777 mRNA. Translation: AAA84887.1 .

3D structure databases

ProteinModelPortali P53448.
SMRi P53448. Positions 3-363.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P53448.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG002386.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view ]
PANTHERi PTHR11627. PTHR11627. 1 hit.
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Identification of neuronal isozyme specific residues by comparison of goldfish aldolase C to other aldolases."
    Berardini T.Z., Drygas-Williams M., Callard G.V., Tolan D.R.
    Comp. Biochem. Physiol. 117A:471-476(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.

Entry informationi

Entry nameiALDOC_CARAU
AccessioniPrimary (citable) accession number: P53448
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3