ID ALDOB_DANRE Reviewed; 364 AA. AC Q8JH71; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 47. DE RecName: Full=Fructose-bisphosphate aldolase B; DE EC=4.1.2.13; DE AltName: Full=Liver-type aldolase; GN Name=aldob; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12486526; DOI=10.1007/s00239-002-2363-8; RA Merritt T.J.S., Quattro J.M.; RT "Negative charge correlates with neural expression in vertebrate RT aldolase isozymes."; RL J. Mol. Evol. 55:674-683(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney marrow; RX PubMed=15520368; DOI=10.1073/pnas.0407241101; RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., RA Sheng Y., Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., RA Kanki J.P., Liu T.X., Look A.T., Chen Z.; RT "Hematopoietic gene expression profile in zebrafish kidney marrow."; RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (NOV-2003) 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 -!- 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; AF533646; AAN04477.1; -; mRNA. DR EMBL; AY394965; AAQ94592.1; -; mRNA. DR EMBL; BC062830; AAH62830.1; -; mRNA. DR IPI; IPI00505184; -. DR RefSeq; NP_919348.3; -. DR UniGene; Dr.76309; -. DR HSSP; P05062; 1QO5. DR SMR; Q8JH71; 3-364. DR Ensembl; ENSDARG00000053684; Danio rerio. DR GeneID; 321664; -. DR KEGG; dre:321664; -. DR ZFIN; ZDB-GENE-030131-383; aldob. DR HOVERGEN; Q8JH71; -. DR OMA; Q8JH71; INQVPLH. DR BRENDA; 4.1.2.13; 96826. DR ArrayExpress; Q8JH71; -. DR Bgee; Q8JH71; -. 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 Glycolysis; Lyase; Schiff base. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 364 Fructose-bisphosphate aldolase B. FT /FTId=PRO_0000291611. 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). SQ SEQUENCE 364 AA; 39288 MW; FB2DD9CDDCF4DB9E CRC64; MTHQFPALST EQKKELATIA ERIVAPGKGI LAADESTGTM AKRFQKINVE NTEENRRSFR DLLFSVDDSI SESIGGVILF HETLYQKSDK GVLFPKVIKD KGIVVGIKVD KGTAGLAGTD GETTTQGLDG LSERCAQYKK DGCDFAKWRC VLKISDSCPS ALGIAENANV LARYASICQQ NGLVPIVEPE ILPDGDHDLK QCQYATEKVL AAVYKALSDH HVYLEGTLLK PNMVTAGHSC TKKYTPLEVA MATVTALRRT VPAAVPGICF LSGGQSEEEA SLNLNAMNQL SLHRPWKLSF SYGRALQASA LSAWKGQAAN KKASQDAFVT RAKINSLASK GEYKPSGQAG QASTQSLFTA SYTY //