PMM_WHEAT
ID PMM_WHEAT Reviewed; 249 AA.
AC Q1W374; C8CK06;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Phosphomannomutase {ECO:0000303|PubMed:17217471};
DE Short=TaPMM {ECO:0000303|PubMed:17217471};
DE EC=5.4.2.8 {ECO:0000269|PubMed:20920368};
GN Name=PMM {ECO:0000303|PubMed:17217471};
GN Synonyms=PMM-A1 {ECO:0000303|PubMed:20920368};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=20920368; DOI=10.1186/1471-2229-10-214;
RA Yu C., Li Y., Li B., Liu X., Hao L., Chen J., Qian W., Li S., Wang G.,
RA Bai S., Ye H., Qin H., Shen Q., Chen L., Zhang A., Wang D.;
RT "Molecular analysis of phosphomannomutase (PMM) genes reveals a unique PMM
RT duplication event in diverse Triticeae species and the main PMM isozymes in
RT bread wheat tissues.";
RL BMC Plant Biol. 10:214-214(2010).
CC -!- FUNCTION: Catalyzes the interconversion of mannose-6-phosphate to
CC mannose-1-phosphate, the precursor for the synthesis of GDP-mannose
CC (Probable) (PubMed:20920368). GDP-mannose is an essential sugar
CC nucleotide for the synthesis of D-mannose-containing cell wall
CC polysaccharides (galactomannans and glucomannans), glycolipids,
CC glycoproteins and the antioxidant L-ascorbate (Probable). Can
CC complement the yeast temperature-sensitive mutant sec53-6
CC (PubMed:17217471, PubMed:20920368). {ECO:0000269|PubMed:17217471,
CC ECO:0000269|PubMed:20920368, ECO:0000305, 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:0000269|PubMed:20920368};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q92871};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.46 mM for alpha-D-mannose 1-phosphate
CC {ECO:0000269|PubMed:20920368};
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, leaves, flag leaves and
CC immature spikes. {ECO:0000269|PubMed:20920368}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR EMBL; DQ442996; ABD97875.1; -; mRNA.
DR EMBL; GQ412259; ACV41076.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1W374; -.
DR SMR; Q1W374; -.
DR STRING; 4565.Traes_4BL_D08D5FFB5.1; -.
DR PRIDE; Q1W374; -.
DR EnsemblPlants; TraesCLE_scaffold_043065_01G000100.1; TraesCLE_scaffold_043065_01G000100.1; TraesCLE_scaffold_043065_01G000100.
DR EnsemblPlants; TraesPAR_scaffold_068067_01G000300.1; TraesPAR_scaffold_068067_01G000300.1; TraesPAR_scaffold_068067_01G000300.
DR EnsemblPlants; TraesWEE_scaffold_029483_01G000200.1; TraesWEE_scaffold_029483_01G000200.1; TraesWEE_scaffold_029483_01G000200.
DR Gramene; TraesCLE_scaffold_043065_01G000100.1; TraesCLE_scaffold_043065_01G000100.1; TraesCLE_scaffold_043065_01G000100.
DR Gramene; TraesPAR_scaffold_068067_01G000300.1; TraesPAR_scaffold_068067_01G000300.1; TraesPAR_scaffold_068067_01G000300.
DR Gramene; TraesWEE_scaffold_029483_01G000200.1; TraesWEE_scaffold_029483_01G000200.1; TraesWEE_scaffold_029483_01G000200.
DR eggNOG; KOG3189; Eukaryota.
DR BRENDA; 5.4.2.8; 6500.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q1W374; baseline and differential.
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; Reference proteome.
FT CHAIN 1..249
FT /note="Phosphomannomutase"
FT /id="PRO_0000326497"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT ACT_SITE 17
FT /note="Proton donor/acceptor"
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 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 24
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 126
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 137
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 144
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 184
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
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
