ID F26_CAEEL Reviewed; 457 AA. AC Q21122; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 16-JUN-2009, entry version 67. DE RecName: Full=Putative 6PF-2-K/Fru-2,6-P2ASE; DE Includes: DE RecName: Full=6-phosphofructo-2-kinase; DE EC=2.7.1.105; DE Includes: DE RecName: Full=Fructose-2,6-bisphosphatase; DE EC=3.1.3.46; GN ORFNames=K02B2.1; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate CC (By similarity). CC -!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O = D- CC fructose 6-phosphate + phosphate. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D- CC fructose 2,6-bisphosphate. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC phosphoglycerate mutase 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; U41558; AAK39245.2; -; Genomic_DNA. DR RefSeq; NP_500893.2; -. DR UniGene; Cel.7619; -. DR HSSP; P07953; 1C80. DR Ensembl; K02B2.1; Caenorhabditis elegans. DR GeneID; 177363; -. DR KEGG; cel:K02B2.1; -. DR NMPDR; fig|6239.3.peg.13532; -. DR WormBase; WBGene00019295; K02B2.1. DR WormPep; K02B2.1; CE30082. DR OMA; Q21122; FNNGELR. DR BRENDA; 2.7.1.105; 672. DR BRENDA; 3.1.3.46; 672. DR NextBio; 896460; -. DR ArrayExpress; Q21122; -. DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase act...; IEA:EC. DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro. DR InterPro; IPR003094; 6Pfruct_kin. DR InterPro; IPR013079; 6Phosfructo_kin. DR InterPro; IPR016260; Bifunct_6PFK/fruc_bisP_Ptase. DR InterPro; IPR001345; PG/BPGM_mutase. DR InterPro; IPR013078; PG_mutase. DR PANTHER; PTHR10606; 6Pfruct_kin; 1. DR Pfam; PF01591; 6PF2K; 1. DR Pfam; PF00300; PGAM; 1. DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1. DR PRINTS; PR00991; 6PFRUCTKNASE. DR PROSITE; PS00175; PG_MUTASE; 1. PE 2: Evidence at transcript level; KW ATP-binding; Complete proteome; Hydrolase; Kinase; KW Multifunctional enzyme; Nucleotide-binding; Transferase. FT CHAIN 1 457 Putative 6PF-2-K/Fru-2,6-P2ASE. FT /FTId=PRO_0000179974. FT NP_BIND 36 43 ATP (Potential). FT REGION 1 244 6-phosphofructo-2-kinase. FT REGION 245 457 Fructose-2,6-bisphosphatase. FT ACT_SITE 124 124 Potential. FT ACT_SITE 154 154 Potential. FT ACT_SITE 253 253 Tele-phosphohistidine intermediate (By FT similarity). FT ACT_SITE 324 324 Potential. FT ACT_SITE 389 389 Proton donor (By similarity). FT BINDING 98 98 Fructose-6-phosphate (By similarity). FT BINDING 190 190 Fructose-6-phosphate (By similarity). SQ SEQUENCE 457 AA; 52091 MW; E04A9A892378E413 CRC64; MEIPPGLETT KRKVAHSDEH GFSDQVRVPN VIVMVGLPAR GKTYISKKLC RYLKWTGFTT KVFNVGEYRR SDANAADAIH GANASFFSPN NADALKVRAE SARRAMEDMA DYLNSGTGGV AIFDATNTTK DRRRIIIDFC KKQRLRCFFI ESVCDDPAII DCNVTDVKVN SPDYKGLMTA EQAKEDFMNR IENYKKQYEP LDESEDESLS FIKVINAGRS FKVHQVRGHV QSRVVYFLMN IHLLPRSIYL TRHGQSEYNA MGRLGGDSPL TEDGQKYASA LADFFEEEEV PGLRVWCSQK VRAAQTAQHL KPDFHTEYWK ALDELDAGIC EGLTYEDILQ RYPKQADDRA TDKYHYRYPS GESYEDVVSR LEPVIMELER QANVLVVSHQ AVLRCVLAYF YDRPLSELPY IDIPLHSLVK LTPRAYHCDS TIYALDLESG EWTETSDQLP LCDSPRD //