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P91759

- ALF_LYMST

UniProt

P91759 - ALF_LYMST

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Protein

Fructose-bisphosphate aldolase

Gene
N/A
Organism
Lymnaea stagnalis (Great pond snail) (Helix stagnalis)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Schiff-base intermediate with dihydroxyacetone-P By similarity

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC

GO - Biological processi

  1. 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 (EC:4.1.2.13)
OrganismiLymnaea stagnalis (Great pond snail) (Helix stagnalis)
Taxonomic identifieri6523 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataHygrophilaLymnaeoideaLymnaeidaeLymnaea

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›101›101Fructose-bisphosphate aldolasePRO_0000216932Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP91759.
SMRiP91759. Positions 1-100.

Family & Domainsi

Sequence similaritiesi

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: Fragment.

P91759-1 [UniParc]FASTAAdd to Basket

« Hide

HNMFLEGTLL KPNMVTAGQG CPKKYTPEDI ARATVTALNR TVPAAVAGIT    50
FLSGGQSEED ATINLNAINQ FPGRKPWPLT FSYGRALQAS VLKAWGGKDE 100
L 101
Length:101
Mass (Da):10,831
Last modified:May 1, 1997 - v1
Checksum:iA151A6471A6AAFBD
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei101 – 1011

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U73114 mRNA. Translation: AAC47398.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U73114 mRNA. Translation: AAC47398.1 .

3D structure databases

ProteinModelPortali P91759.
SMRi P91759. Positions 1-100.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. Fainzilber M., Kesteren R.E., Smit A.B.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiALF_LYMST
AccessioniPrimary (citable) accession number: P91759
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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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