ID ALDOB_BOVIN Reviewed; 364 AA. AC Q3T0S5; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 33. DE RecName: Full=Fructose-bisphosphate aldolase B; DE EC=4.1.2.13; DE AltName: Full=Liver-type aldolase; GN Name=ALDOB; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone CC phosphate + D-glyceraldehyde 3-phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in CC liver and aldolase C in brain. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC102278; AAI02279.1; -; mRNA. DR IPI; IPI00686881; -. DR RefSeq; NP_001029657.1; -. DR UniGene; Bt.46035; -. DR SMR; Q3T0S5; 2-364. DR PRIDE; Q3T0S5; -. DR Ensembl; ENSBTAG00000015358; Bos taurus. DR GeneID; 515263; -. DR KEGG; bta:515263; -. DR HOVERGEN; Q3T0S5; -. DR BRENDA; 4.1.2.13; 251. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:EC. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR InterPro; IPR000741; Aldolase_I. DR InterPro; IPR013785; Aldolase_TIM. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR PANTHER; PTHR11627; Aldolase_I; 1. DR Pfam; PF00274; Glycolytic; 1. DR ProDom; PD001128; Aldolase_I; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. PE 2: Evidence at transcript level; KW Acetylation; Glycolysis; Lyase; Phosphoprotein; Schiff base. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 364 Fructose-bisphosphate aldolase B. FT /FTId=PRO_0000284089. FT ACT_SITE 188 188 Proton acceptor (By similarity). FT ACT_SITE 230 230 Schiff-base intermediate with FT dihydroxyacetone-P (By similarity). FT BINDING 56 56 Substrate (By similarity). FT BINDING 147 147 Substrate (By similarity). FT SITE 364 364 Necessary for preference for fructose FT 1,6-bisphosphate over fructose 1- FT phosphate (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 36 36 Phosphoserine (By similarity). SQ SEQUENCE 364 AA; 39543 MW; 935BA56BC83353EA CRC64; MAHQFPALTS EQKKALSETA RRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR ELLFTVDSSV SQSIGGVILF HETLYQKDGQ GKLFRDILKE KGIVVGIKLD QGVAPLAGTN KETTVQGLDG LSERCAQYKK DGADFGKWRA VLKIDNQCPS HLAIQENANT LARYASICQQ NGLVPIVEPE VIPDGSHDME HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF SYGRALQASA LAAWGGKAEN KKTTQEAFMK RALANSQAAK GQYVHMGSSG SASTQSLFTA SYTY //