ID PMM_NICBE Reviewed; 252 AA. AC Q1W375; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 1. DT 08-NOV-2023, entry version 66. DE RecName: Full=Phosphomannomutase {ECO:0000303|PubMed:17217471}; DE Short=NbPMM {ECO:0000303|PubMed:17217471}; DE EC=5.4.2.8 {ECO:0000305|PubMed:17217471}; GN Name=PMM {ECO:0000303|PubMed:17217471}; OS Nicotiana benthamiana. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4100; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE RP SPECIFICITY. 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 higher RT plants and genetic evidence for the involvement of PMM in ascorbic acid RT biosynthesis in Arabidopsis and Nicotiana benthamiana."; RL Plant J. 49:399-413(2007). CC -!- FUNCTION: Catalyzes the interconversion of mannose-6-phosphate to CC mannose-1-phosphate, the precursor for the synthesis of GDP-mannose CC (Probable). GDP-mannose is an essential sugar nucleotide for the CC synthesis of D-mannose-containing cell wall polysaccharides CC (galactomannans and glucomannans), glycolipids, glycoproteins and the CC antioxidant L-ascorbate (Probable). Can complement the yeast CC temperature-sensitive mutant sec53-6 (PubMed:17217471). CC {ECO:0000269|PubMed:17217471, ECO:0000305, CC ECO:0000305|PubMed:17217471}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; CC EC=5.4.2.8; Evidence={ECO:0000305|PubMed:17217471}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q92871}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: CC step 2/2. {ECO:0000305}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q92871}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A0U1WZ18}. CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and CC immature fruits. {ECO:0000269|PubMed:17217471}. CC -!- MISCELLANEOUS: Overexpression of PMM increases total leaf ascorbate CC content (PubMed:17217471). Silencing of PMM decreases significantly CC total leaf ascorbate content (PubMed:17217471). CC {ECO:0000269|PubMed:17217471}. CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ442995; ABD97874.1; -; mRNA. DR AlphaFoldDB; Q1W375; -. DR SMR; Q1W375; -. DR STRING; 4097.Q1W375; -. DR PaxDb; 4097-Q1W375; -. DR UniPathway; UPA00126; UER00424. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC. DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd02585; HAD_PMM; 1. DR Gene3D; 3.30.1240.20; -; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR005002; PMM. DR InterPro; IPR043169; PMM_cap. DR NCBIfam; TIGR01484; HAD-SF-IIB; 1. DR PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1. DR PANTHER; PTHR10466:SF0; PHOSPHOMANNOMUTASE; 1. DR Pfam; PF03332; PMM; 1. DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 1: Evidence at protein level; KW Cytoplasm; Isomerase; Magnesium; Metal-binding. FT CHAIN 1..252 FT /note="Phosphomannomutase" FT /id="PRO_0000326496" FT ACT_SITE 13 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT ACT_SITE 15 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 13 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 15 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 22 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 124 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 135 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 142 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 180 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 182 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 208 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P31353" FT BINDING 220 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P31353" FT BINDING 225 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q92871" SQ SEQUENCE 252 AA; 28575 MW; E9820AF015B0099A CRC64; MAARKPGLIA LFDVDGTLTA PRKEVTPEML KFMKELRKVV TVGVVGGSDL VKISEQLGKT VTTDYDYCFS ENGLVAHKDG KLIGTQSLKS FLGDEKLKEF INFTLHYIAD LDIPIKRGTF IEFRSGMLNV SPIGRDCSQE ERDEFEKYDK VHKIRQTMVS VLREKFAHLN LTFSIGGQIS FDVFPQGWDK TYCLRYLEEF NEIHFFGDKT YKGGNDHEIY ESERTVGHTV TSPEDTVKQC SEQFLGKDNG SS //