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   27-MAR-2024, entry version 72.
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}.
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; DQ442996; ABD97875.1; -; mRNA.
DR   EMBL; GQ412259; ACV41076.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1W374; -.
DR   SMR; Q1W374; -.
DR   STRING; 4565.Q1W374; -.
DR   PaxDb; 4565-Traes_4BL_D08D5FFB5-1; -.
DR   EnsemblPlants; TraesCLE_scaffold_043065_01G000100.1; TraesCLE_scaffold_043065_01G000100.1; TraesCLE_scaffold_043065_01G000100.
DR   EnsemblPlants; TraesKAR2A01G0489860.1; cds.TraesKAR2A01G0489860.1; TraesKAR2A01G0489860.
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; TraesKAR2A01G0489860.1; cds.TraesKAR2A01G0489860.1; TraesKAR2A01G0489860.
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; 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:SF15; 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; 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
//