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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 – 561Substrate By similarity
Binding sitei147 – 1471Substrate By similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P By similarity
Sitei363 – 3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate By 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 – 11Removed By similarity
Chaini2 – 363362Fructose-bisphosphate aldolase C
PRO_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.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG002386.

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.

P53448-1 [UniParc]FASTAAdd to Basket

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MTHQYPALTT EQKRELQDIA QRIVAPGKGI LAADESTGSM AKRLNPIGVE    50
NTEENRRLYR QLLFTADERM DKCIGGVIFF HETLYQKADD GTPFAKMIKD 100
RGIVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRS 150
VLKISETSPS ELAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK 200
RCQYVTEKVL AACYKALSDH HVYLEGTLLK PNMVTAGHSC PTKFSNQEIA 250
MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINNC PLTKPWALTF 300
SYGRALQASA LSAWRGVKEN EKAATEEFLK RAEANGLAAQ GKYVSSGMDG 350
SAGQSLYVAN HAY 363
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 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. "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: September 3, 2014
This is version 66 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

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