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P54216

- ALF1_CAEEL

UniProt

P54216 - ALF1_CAEEL

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Protein

Fructose-bisphosphate aldolase 1

Gene

aldo-1

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein 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 sitei189 – 1891Proton acceptorBy similarity
Active sitei231 – 2311Schiff-base intermediate with dihydroxyacetone-PBy similarity
Sitei366 – 3661Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB
  2. identical protein binding Source: IntAct

GO - Biological processi

  1. glycolytic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiREACT_231555. Glycolysis.
REACT_258890. Fructose catabolism.
REACT_261547. Gluconeogenesis.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase 1 (EC:4.1.2.13)
Alternative name(s):
Aldolase CE-1
Short name:
CE1
Gene namesi
Name:aldo-1
ORF Names:T05D4.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome III

Organism-specific databases

WormBaseiT05D4.1; CE16341; WBGene00011474; aldo-1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: WormBase
  2. sarcomere Source: WormBase
  3. striated muscle dense body Source: WormBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Fructose-bisphosphate aldolase 1PRO_0000216928Add
BLAST

Proteomic databases

PaxDbiP54216.

Expressioni

Tissue specificityi

Ubiquitous.

Developmental stagei

All stages of development.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-327260,EBI-327260

Protein-protein interaction databases

BioGridi41956. 1 interaction.
DIPiDIP-25939N.
IntActiP54216. 1 interaction.
MINTiMINT-1094145.

Structurei

3D structure databases

ProteinModelPortaliP54216.
SMRiP54216. Positions 8-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
HOGENOMiHOG000220876.
InParanoidiP54216.
KOiK01623.
PhylomeDBiP54216.

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.

P54216-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASYSQFLTK AQEDELRSIA NAIVTPGKGI LAADESTGSM DKRLNSIGLE
60 70 80 90 100
NTEENRRKYR QLLFTAGADL NKYISGVIMF HETFYQKTDD GKPFTALLQE
110 120 130 140 150
QGIIPGIKVD KGVVPMAGTI GEGTTQGLDD LNARCAQYKK DGAQFAKWRC
160 170 180 190 200
VHKISSTTPS VTALKEIASN LGSRYASICQ QNGLVPIVEP EILPDGEHCL
210 220 230 240 250
ARGQKITETV LSYVYHALNE HHVFLEGTLL KPNMVTSGQS FTGEKPSNAD
260 270 280 290 300
IGLATVTALQ RGVPSAVPGV VFLSGGQSEE DATLNLNAIN QVSGKKPWAL
310 320 330 340 350
TFSYGRALQA SCLAKWAGKD ENIAAAQEVL LHRAQVNSLA SVGKYTGDAS
360
ADAAASQSLF VANHSY
Length:366
Mass (Da):39,240
Last modified:October 1, 1996 - v1
Checksum:i5B9F91D486FFAEB5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1732GS → A in CAB03291. (PubMed:9851916)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83738 mRNA. Translation: BAA12091.1.
Z81115 Genomic DNA. Translation: CAB03291.1.
PIRiT24514.
RefSeqiNP_741281.1. NM_171235.3.
UniGeneiCel.6851.

Genome annotation databases

GeneIDi176788.
KEGGicel:CELE_T05D4.1.
UCSCiT05D4.1.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83738 mRNA. Translation: BAA12091.1 .
Z81115 Genomic DNA. Translation: CAB03291.1 .
PIRi T24514.
RefSeqi NP_741281.1. NM_171235.3.
UniGenei Cel.6851.

3D structure databases

ProteinModelPortali P54216.
SMRi P54216. Positions 8-346.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 41956. 1 interaction.
DIPi DIP-25939N.
IntActi P54216. 1 interaction.
MINTi MINT-1094145.

Proteomic databases

PaxDbi P54216.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 176788.
KEGGi cel:CELE_T05D4.1.
UCSCi T05D4.1.1. c. elegans.

Organism-specific databases

CTDi 176788.
WormBasei T05D4.1 ; CE16341 ; WBGene00011474 ; aldo-1.

Phylogenomic databases

eggNOGi COG3588.
HOGENOMi HOG000220876.
InParanoidi P54216.
KOi K01623.
PhylomeDBi P54216.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
Reactomei REACT_231555. Glycolysis.
REACT_258890. Fructose catabolism.
REACT_261547. Gluconeogenesis.

Miscellaneous databases

NextBioi 894008.

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

« Hide 'large scale' publications
  1. "Caenorhabditis elegans has two isozymic forms, CE-1 and CE-2, of fructose-1,6-bisphosphate aldolase which are encoded by different genes."
    Inoue T., Yatsuki H., Kusakabe T., Joh K., Hori K.
    Arch. Biochem. Biophys. 339:226-234(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Bristol N2.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiALF1_CAEEL
AccessioniPrimary (citable) accession number: P54216
Secondary accession number(s): O45747
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3