PMM_DENOF
ID PMM_DENOF Reviewed; 252 AA.
AC A0A0U1WZ18;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Phosphomannomutase {ECO:0000303|PubMed:27987037};
DE Short=DoPMM {ECO:0000303|PubMed:27987037};
DE EC=5.4.2.8 {ECO:0000305|PubMed:27987037};
GN Name=PMM {ECO:0000303|PubMed:27987037};
OS Dendrobium officinale (Orchid).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX NCBI_TaxID=142615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chunmei H., Jun D.;
RT "Purification, separation and characterization of phosphoglucomutase and
RT phosphomannomutase from maize leaves.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=27987037; DOI=10.1007/s00709-016-1044-1;
RA He C., Zeng S., Teixeira da Silva J.A., Yu Z., Tan J., Duan J.;
RT "Molecular cloning and functional analysis of the phosphomannomutase (PMM)
RT gene from Dendrobium officinale and evidence for the involvement of an
RT abiotic stress response during germination.";
RL Protoplasma 254:1693-1704(2017).
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). Involved in the biosynthesis of
CC ascorbate and polysaccharides in response to abiotic stress during seed
CC germination (PubMed:27987037). {ECO:0000269|PubMed:27987037,
CC ECO:0000305|PubMed:27987037}.
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:27987037};
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:0000269|PubMed:27987037}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:27987037}.
CC -!- INDUCTION: Induced by abscisic acid (ABA), salicylate (SA), cold
CC stress, osmotic stress and salt stress. {ECO:0000269|PubMed:27987037}.
CC -!- MISCELLANEOUS: Overexpression of Dendrobium officinale PMM in
CC Arabidopsis increases total leaf ascorbate and polysaccharide content,
CC and increases seed germination rate under osmotic and salt stresses.
CC {ECO:0000269|PubMed:27987037}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR EMBL; KF195558; AHY34917.1; -; mRNA.
DR AlphaFoldDB; A0A0U1WZ18; -.
DR SMR; A0A0U1WZ18; -.
DR BRENDA; 5.4.2.8; 16152.
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; IDA:UniProtKB.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IDA:UniProtKB.
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_0000451446"
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; 28635 MW; D930633007A9CB83 CRC64;
MTGRMPGLIV LFDVDGTLTA PRKAITPKML EFMQDLRKVV TVGVVGGSDL VKISEQLGKS
VISDYDYVFA ENGLVAYKNG ELIGKQNFKS FLGEEKLKEL INFTLHYIAD LDIPIKRGTF
IEFRSGMLNV SPIGRNCSQE ERDEFEKYDK VHNIRSKMVS VLREKFKHLN LTFSIGGQIS
FDVFPQGWDK TYCLRYLEDF PEIHFFGDKT YKGGNDYEIY ESERTVGHTV TSPDDTAEQC
KLHFLAKQAG DA
