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P79226

- ALDOB_RABIT

UniProt

P79226 - ALDOB_RABIT

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Protein

Fructose-bisphosphate aldolase B

Gene

ALDOB

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 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 – 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

  1. fructose binding Source: Ensembl
  2. fructose-bisphosphate aldolase activity Source: UniProtKB-EC

GO - Biological processi

  1. fructose 1,6-bisphosphate metabolic process Source: Ensembl
  2. fructose metabolic process Source: Ensembl
  3. glycolytic process Source: UniProtKB-UniPathway
  4. NADH oxidation Source: Ensembl
  5. positive regulation of ATPase activity Source: Ensembl
  6. vacuolar proton-transporting V-type ATPase complex assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

SABIO-RKP79226.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase B (EC:4.1.2.13)
Alternative name(s):
Liver-type aldolase
Gene namesi
Name:ALDOB
Synonyms:ALDB
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  1. centriolar satellite Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 364363Fructose-bisphosphate aldolase BPRO_0000216942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei13 – 131N6-succinyllysineBy similarity
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei39 – 391PhosphothreonineBy similarity
Modified residuei121 – 1211N6-succinyllysineBy similarity
Modified residuei317 – 3171N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP79226.

Interactioni

Subunit structurei

Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000012843.

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2415Combined sources
Helixi25 – 273Combined sources
Beta strandi29 – 335Combined sources
Helixi37 – 4610Combined sources
Helixi53 – 6412Combined sources
Helixi68 – 725Combined sources
Beta strandi74 – 796Combined sources
Helixi81 – 844Combined sources
Helixi94 – 1007Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1253Combined sources
Helixi131 – 14010Combined sources
Beta strandi145 – 1528Combined sources
Helixi161 – 18020Combined sources
Beta strandi184 – 1918Combined sources
Helixi199 – 21921Combined sources
Helixi224 – 2263Combined sources
Helixi246 – 25813Combined sources
Beta strandi267 – 2704Combined sources
Helixi277 – 28913Combined sources
Beta strandi296 – 3038Combined sources
Helixi304 – 31411Combined sources
Helixi318 – 3203Combined sources
Helixi321 – 33818Combined sources
Turni339 – 3413Combined sources
Beta strandi353 – 3575Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FDJX-ray2.10A/B/C/D2-364[»]
ProteinModelPortaliP79226.
SMRiP79226. Positions 2-364.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP79226.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP79226.
OMAiDMEHCQY.
OrthoDBiEOG744T94.
TreeFamiTF314203.

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.

P79226-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAHRFPALTP EQKKELSDIA QRIVANGKGI LAADESVGTM GNRLQRIKVE
60 70 80 90 100
NTEENRRQFR EILFTVDNSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE
110 120 130 140 150
KGIVVGIKLD QGGAPLAGTN KETTIQGLDG LSERCAQYKK DGVDFGKWRA
160 170 180 190 200
VLRIADQCPS SLAIQENANT LARYASICQQ NGLVPIVEPE VIPDGDHDLE
210 220 230 240 250
HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC TKKYTPEQVA
260 270 280 290 300
MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF
310 320 330 340 350
SYGRALQASA LAAWGGKAEN KKATQEAFMK RAVVNCQAAK GQYVHTGSSG
360
AASTQSLFTA SYTY
Length:364
Mass (Da):39,605
Last modified:January 23, 2007 - v3
Checksum:i65A58A50906EA954
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85645 Genomic DNA. Translation: AAB42087.1.
PIRiA28856.
RefSeqiNP_001164585.1. NM_001171114.1.
UniGeneiOcu.4530.

Genome annotation databases

EnsembliENSOCUT00000014943; ENSOCUP00000012843; ENSOCUG00000014944.
GeneIDi100328925.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85645 Genomic DNA. Translation: AAB42087.1 .
PIRi A28856.
RefSeqi NP_001164585.1. NM_001171114.1.
UniGenei Ocu.4530.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FDJ X-ray 2.10 A/B/C/D 2-364 [» ]
ProteinModelPortali P79226.
SMRi P79226. Positions 2-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000012843.

Proteomic databases

PRIDEi P79226.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSOCUT00000014943 ; ENSOCUP00000012843 ; ENSOCUG00000014944 .
GeneIDi 100328925.

Organism-specific databases

CTDi 229.

Phylogenomic databases

eggNOGi COG3588.
GeneTreei ENSGT00390000010235.
HOGENOMi HOG000220876.
HOVERGENi HBG002386.
InParanoidi P79226.
OMAi DMEHCQY.
OrthoDBi EOG744T94.
TreeFami TF314203.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
SABIO-RK P79226.

Miscellaneous databases

EvolutionaryTracei P79226.

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 conserved promoter elements for aldB and isozyme specific residues in aldolase B."
    Berardini T.Z., Amsden A.B., Penhoet E.E., Tolan D.R.
    Comp. Biochem. Physiol. 122B:53-61(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Enhanced electron-density envelopes by extended solvent definition."
    Blom N., Sygush J.
    Acta Crystallogr. D 54:461-466(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Entry informationi

Entry nameiALDOB_RABIT
AccessioniPrimary (citable) accession number: P79226
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 98 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, 3 forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3