ALDOB_RABIT
ID ALDOB_RABIT Reviewed; 364 AA.
AC P79226;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Fructose-bisphosphate aldolase B;
DE EC=4.1.2.13;
DE AltName: Full=Liver-type aldolase;
GN Name=ALDOB; Synonyms=ALDB;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10327593; DOI=10.1016/s0305-0491(98)10140-2;
RA Berardini T.Z., Amsden A.B., Penhoet E.E., Tolan D.R.;
RT "Identification of conserved promoter elements for aldB and isozyme
RT specific residues in aldolase B.";
RL Comp. Biochem. Physiol. 122B:53-61(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=9761929; DOI=10.1107/s0907444997006549;
RA Blom N., Sygush J.;
RT "Enhanced electron-density envelopes by extended solvent definition.";
RL Acta Crystallogr. D 54:461-466(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriolar satellite {ECO:0000250}.
CC -!- MISCELLANEOUS: In vertebrates, 3 forms of this ubiquitous glycolytic
CC enzyme are found, aldolase A in muscle, aldolase B in liver and
CC aldolase C in brain.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; U85645; AAB42087.1; -; Genomic_DNA.
DR PIR; A28856; A28856.
DR RefSeq; NP_001164585.1; NM_001171114.1.
DR PDB; 1FDJ; X-ray; 2.10 A; A/B/C/D=2-364.
DR PDBsum; 1FDJ; -.
DR AlphaFoldDB; P79226; -.
DR SMR; P79226; -.
DR STRING; 9986.ENSOCUP00000012843; -.
DR iPTMnet; P79226; -.
DR PRIDE; P79226; -.
DR Ensembl; ENSOCUT00000014943; ENSOCUP00000012843; ENSOCUG00000014944.
DR GeneID; 100328925; -.
DR KEGG; ocu:100328925; -.
DR CTD; 229; -.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; P79226; -.
DR OMA; ANCQAAQ; -.
DR OrthoDB; 799973at2759; -.
DR TreeFam; TF314203; -.
DR SABIO-RK; P79226; -.
DR UniPathway; UPA00109; UER00183.
DR EvolutionaryTrace; P79226; -.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000014944; Expressed in adult mammalian kidney and 16 other tissues.
DR ExpressionAtlas; P79226; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; Glycolysis; Lyase;
KW Phosphoprotein; Reference proteome; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q91Y97"
FT CHAIN 2..364
FT /note="Fructose-bisphosphate aldolase B"
FT /id="PRO_0000216942"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 147
FT /ligand="substrate"
FT SITE 364
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y97"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y97"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 121
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y97"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00884"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00884"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 317
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y97"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 161..180
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 199..219
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1FDJ"
FT HELIX 321..338
FT /evidence="ECO:0007829|PDB:1FDJ"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:1FDJ"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1FDJ"
SQ SEQUENCE 364 AA; 39605 MW; 65A58A50906EA954 CRC64;
MAHRFPALTP EQKKELSDIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR
EILFTVDNSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN
KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANT LARYASICQQ
NGLVPIVEPE VIPDGDHDLE HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC
TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF
SYGRALQASA LAAWGGKAEN KKATQEAFMK RAVVNCQAAK GQYVHTGSSG AASTQSLFTA
SYTY
