ALDOB_RAT
ID ALDOB_RAT Reviewed; 364 AA.
AC P00884; P70706;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Fructose-bisphosphate aldolase B;
DE EC=4.1.2.13;
DE AltName: Full=Liver-type aldolase;
GN Name=Aldob;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6094564; DOI=10.1016/s0021-9258(17)42639-1;
RA Tsutsumi K., Mukai T., Tsutsumi R., Mori M., Daimon M., Tanaka T.,
RA Yatsuki H., Hori K., Ishikawa K.;
RT "Nucleotide sequence of rat liver aldolase B messenger RNA.";
RL J. Biol. Chem. 259:14572-14575(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=2580098; DOI=10.1016/0022-2836(85)90081-6;
RA Tsutsumi K., Mukai T., Tsutsumi R., Hidaka S., Arai Y., Hori K.,
RA Ishikawa K.;
RT "Structure and genomic organization of the rat aldolase B gene.";
RL J. Mol. Biol. 181:153-160(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 185-364.
RX PubMed=6304044; DOI=10.1016/s0021-9258(18)32445-1;
RA Tsutsumi K., Mukai T., Hidaka S., Miyahara H., Tsutsumi R., Tanaka T.,
RA Hori K., Ishikawa K.;
RT "Rat aldolase isozyme gene.";
RL J. Biol. Chem. 258:6537-6542(1983).
RN [4]
RP PROTEIN SEQUENCE OF 41-68.
RX PubMed=1834654; DOI=10.1016/s0021-9258(18)54808-0;
RA Brand I.A., Heinickel A.;
RT "Key enzymes of carbohydrate metabolism as targets of the 11.5-kDa Zn(2+)-
RT binding protein (parathymosin).";
RL J. Biol. Chem. 266:20984-20989(1991).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-132; SER-299
RP AND SER-301, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; M10149; AAA40716.1; -; mRNA.
DR EMBL; X02284; CAA26156.1; -; Genomic_DNA.
DR EMBL; X02285; CAA26156.1; JOINED; Genomic_DNA.
DR EMBL; X02286; CAA26156.1; JOINED; Genomic_DNA.
DR EMBL; X02287; CAA26156.1; JOINED; Genomic_DNA.
DR EMBL; X02288; CAA26156.1; JOINED; Genomic_DNA.
DR EMBL; X02289; CAA26156.1; JOINED; Genomic_DNA.
DR EMBL; X02290; CAA26156.1; JOINED; Genomic_DNA.
DR EMBL; X02291; CAA26156.1; JOINED; Genomic_DNA.
DR EMBL; V01223; CAA24533.1; -; mRNA.
DR PIR; A22585; ADRTB.
DR AlphaFoldDB; P00884; -.
DR SMR; P00884; -.
DR IntAct; P00884; 1.
DR MINT; P00884; -.
DR STRING; 10116.ENSRNOP00000009111; -.
DR iPTMnet; P00884; -.
DR PhosphoSitePlus; P00884; -.
DR jPOST; P00884; -.
DR PaxDb; P00884; -.
DR PRIDE; P00884; -.
DR UCSC; RGD:2090; rat.
DR RGD; 2090; Aldob.
DR eggNOG; KOG1557; Eukaryota.
DR InParanoid; P00884; -.
DR PhylomeDB; P00884; -.
DR BRENDA; 4.1.2.13; 5301.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR Reactome; R-RNO-70350; Fructose catabolism.
DR SABIO-RK; P00884; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:P00884; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0034451; C:centriolar satellite; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0070061; F:fructose binding; ISO:RGD.
DR GO; GO:0061609; F:fructose-1-phosphate aldolase activity; ISO:RGD.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0031210; F:phosphatidylcholine binding; IPI:RGD.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISO:RGD.
DR GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; ISO:RGD.
DR GO; GO:0006000; P:fructose metabolic process; ISO:RGD.
DR GO; GO:0006096; P:glycolytic process; IDA:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0006116; P:NADH oxidation; ISO:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR GO; GO:0009750; P:response to fructose; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0070741; P:response to interleukin-6; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IDA:RGD.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; ISO:RGD.
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 Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Glycolysis; Lyase; 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_0000216943"
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:0007744|PubMed:22673903"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 CONFLICT 234
FT /note="L -> V (in Ref. 2; CAA26156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39618 MW; E120FC119F0180F8 CRC64;
MAHRFPALTS EQKKELSEIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR
ELLFSVDNSI SQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN
KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRISDQCPS SLAIQENANA LARYASICQQ
NGLVPIVEPE VLPDGDHDLE HCQYVSEKVL AAVYKALNDH HVYLEGTLLK PNMLTAGHAC
TKKYTPEQVA MATVTALHRT VPAAVPSICF LSGGMSEEDA TLNLNAIYRC PLPRPWKLSF
SYGRALQASA LAAWGGKAAN KKATQEAFMK RAVANCQAAQ GQYVHTGSSG AASTQSLFTA
SYTY
