ID   PMM_WHEAT               Reviewed;         249 AA.
AC   Q1W374;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 13.
DE   RecName: Full=Phosphomannomutase;
DE            EC=5.4.2.8;
DE   AltName: Full=TaPMM;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Triticum.
OX   NCBI_TaxID=4565;
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; DQ442996; ABD97875.1; -; mRNA.
DR   UniGene; Ta.3539; -.
DR   BRENDA; 5.4.2.8; 253.
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    249       Phosphomannomutase.
FT                                /FTId=PRO_0000326497.
SQ   SEQUENCE   249 AA;  28252 MW;  AB85F0AB97DCD566 CRC64;
     MAAARKDAGV LALFDVDGTL TAPRKEVTPE MLEFMKRLRE NVTVGVVGGS DLVKISEQLG
     KSVITDYDYV FSENGLVAHK DGKLIGTQSL KTYLGDDQLK EFINFTLHYI ADLDIPIKRG
     TFIEFRSGMI NVSPIGRNCS QEERDDFEKY DKVHNVRPKM VSVLREKFAH LNLTFSIGGQ
     ISFDVFPQGW DKTYCLRYLE EFKEIHFFGD KTYKGGNDHE IFESDRTVGH TVTSPNDTVQ
     QCKSIFLSE
//