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P79226

- ALDOB_RABIT

UniProt

P79226 - ALDOB_RABIT

Protein

Fructose-bisphosphate aldolase B

Gene

ALDOB

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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 – 2415
    Helixi25 – 273
    Beta strandi29 – 335
    Helixi37 – 4610
    Helixi53 – 6412
    Helixi68 – 725
    Beta strandi74 – 796
    Helixi81 – 844
    Helixi94 – 1007
    Beta strandi104 – 1085
    Beta strandi113 – 1153
    Beta strandi119 – 1213
    Beta strandi123 – 1253
    Helixi131 – 14010
    Beta strandi145 – 1528
    Helixi161 – 18020
    Beta strandi184 – 1918
    Helixi199 – 21921
    Helixi224 – 2263
    Helixi246 – 25813
    Beta strandi267 – 2704
    Helixi277 – 28913
    Beta strandi296 – 3038
    Helixi304 – 31411
    Helixi318 – 3203
    Helixi321 – 33818
    Turni339 – 3413
    Beta strandi353 – 3575

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiDMEHCQY.
    OrthoDBiEOG744T94.
    TreeFamiTF314203.

    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.

    P79226-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHRFPALTP EQKKELSDIA QRIVANGKGI LAADESVGTM GNRLQRIKVE    50
    NTEENRRQFR EILFTVDNSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE 100
    KGIVVGIKLD QGGAPLAGTN KETTIQGLDG LSERCAQYKK DGVDFGKWRA 150
    VLRIADQCPS SLAIQENANT LARYASICQQ NGLVPIVEPE VIPDGDHDLE 200
    HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC TKKYTPEQVA 250
    MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF 300
    SYGRALQASA LAAWGGKAEN KKATQEAFMK RAVVNCQAAK GQYVHTGSSG 350
    AASTQSLFTA SYTY 364
    Length:364
    Mass (Da):39,605
    Last modified:January 23, 2007 - v3
    Checksum:i65A58A50906EA954
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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 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 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: October 1, 2014
    This is version 96 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