ID PMM_SOLLC Reviewed; 252 AA. AC Q1W377; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 15. DE RecName: Full=Phosphomannomutase; DE EC=5.4.2.8; DE AltName: Full=LePMM; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; OC Solanum; Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=17217471; DOI=10.1111/j.1365-313X.2006.02967.x; RA Qian W., Yu C., Qin H., Liu X., Zhang A., Johansen I.E., Wang D.; RT "Molecular and functional analysis of phosphomannomutase (PMM) from RT higher plants and genetic evidence for the involvement of PMM in RT ascorbic acid biosynthesis in Arabidopsis and Nicotiana benthamiana."; RL Plant J. 49:399-413(2007). CC -!- FUNCTION: Involved in ascorbic acid biosynthesis and in the CC synthesis of the GDP-mannose and dolichol-phosphate-mannose CC required for a number of critical mannosyl transfer reactions (By CC similarity). CC -!- CATALYTIC ACTIVITY: Alpha-D-mannose 1-phosphate = D-mannose 6- CC phosphate. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-D-mannose CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6- CC phosphate: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the eukaryotic PMM 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; DQ442993; ABD97872.1; -; mRNA. DR UniGene; Les.5106; -. DR BRENDA; 5.4.2.8; 281054. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004615; F:phosphomannomutase activity; IEA:EC. DR GO; GO:0019307; P:mannose biosynthetic process; IEA:InterPro. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR005002; PMM. DR PANTHER; PTHR10466; PMM; 1. DR Pfam; PF03332; PMM; 1. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Isomerase. FT CHAIN 1 252 Phosphomannomutase. FT /FTId=PRO_0000326494. SQ SEQUENCE 252 AA; 28556 MW; AE3E701AC82DCC82 CRC64; MAARKAGLIA LFDVDGTLTA PRKESTPQML KFMQELRKVV TVGVVGGSDL VKISEQLGNT VTNDYDYVFS ENGLVAHKDG KLIGKQSLKS HLGDEKLKEF INFTLHYIAD LDIPIKRGTF IEFRSGMLNV SPIGRNCSQE ERDEFEKYDK VQKIRETMVS VLREKFAHFN LTFSIGGQIS FDVFPQGWDK TYCLRYLEEF NEIHFFGDKT YKGGNDHEIY ESERTVGHTV TSPEETLKQC SVLFLGKDNG SS //