ALDOB_PONAB
ID ALDOB_PONAB Reviewed; 364 AA.
AC Q5RFA6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Fructose-bisphosphate aldolase B;
DE EC=4.1.2.13;
DE AltName: Full=Liver-type aldolase;
GN Name=ALDOB;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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.
CC {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; CR857255; CAH89551.1; -; mRNA.
DR RefSeq; NP_001127166.1; NM_001133694.1.
DR AlphaFoldDB; Q5RFA6; -.
DR SMR; Q5RFA6; -.
DR STRING; 9601.ENSPPYP00000021797; -.
DR GeneID; 100174217; -.
DR KEGG; pon:100174217; -.
DR CTD; 229; -.
DR eggNOG; KOG1557; Eukaryota.
DR InParanoid; Q5RFA6; -.
DR OrthoDB; 799973at2759; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000001595; Unplaced.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Cytoskeleton; Glycolysis; Lyase; Phosphoprotein;
KW 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_0000230296"
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 /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 364
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 364 AA; 39447 MW; 992D2580A7F34CB9 CRC64;
MAHRFPALTQ EQKKELSEIA QSIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR
EILFSVDSSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN
KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANA LARYASICQQ
NGLVPIVEPE VIPDGDHDLE HCQYVTEKVL AAAYKALNDH HVYLEGTLLK PNMVTAGHAC
TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF
SYGRALQASA LAAWGGKAAN KEATQEAFMK RAVANHQAAK GQYVHTGSSG AASTQSLFTA
CYTY
