PMM_NICBE
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 03-AUG-2022, entry version 60.
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}.
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DR EMBL; DQ442995; ABD97874.1; -; mRNA.
DR RefSeq; NP_001312503.1; NM_001325574.1.
DR AlphaFoldDB; Q1W375; -.
DR SMR; Q1W375; -.
DR STRING; 4097.Q1W375; -.
DR GeneID; 107794186; -.
DR KEGG; nta:107794186; -.
DR UniPathway; UPA00126; UER00424.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd02585; HAD_PMM; 1.
DR Gene3D; 3.30.1240.20; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 PANTHER; PTHR10466; PTHR10466; 1.
DR Pfam; PF03332; PMM; 1.
DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 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
