PMM_ARATH
ID PMM_ARATH Reviewed; 246 AA.
AC O80840; Q1W379;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Phosphomannomutase {ECO:0000303|PubMed:17217471};
DE Short=AtPMM {ECO:0000303|PubMed:17217471};
DE EC=5.4.2.8 {ECO:0000269|PubMed:17217471};
GN Name=PMM {ECO:0000303|PubMed:17217471};
GN OrderedLocusNames=At2g45790 {ECO:0000312|Araport:AT2G45790};
GN ORFNames=F4I18.23 {ECO:0000312|EMBL:AAC28545.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, MUTAGENESIS OF GLY-7 AND ARG-37, AND DISRUPTION PHENOTYPE.
RX PubMed=18086684; DOI=10.1074/jbc.m704991200;
RA Hoeberichts F.A., Vaeck E., Kiddle G., Coppens E., van de Cotte B.,
RA Adamantidis A., Ormenese S., Foyer C.H., Zabeau M., Inze D., Perilleux C.,
RA Van Breusegem F., Vuylsteke M.;
RT "A temperature-sensitive mutation in the Arabidopsis thaliana
RT phosphomannomutase gene disrupts protein glycosylation and triggers cell
RT death.";
RL J. Biol. Chem. 283:5708-5718(2008).
CC -!- FUNCTION: Catalyzes the interconversion of mannose-6-phosphate to
CC mannose-1-phosphate, the precursor for the synthesis of GDP-mannose
CC (PubMed:17217471, PubMed:18086684). 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). {ECO:0000269|PubMed:17217471,
CC ECO:0000269|PubMed:18086684, ECO:0000305}.
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:17217471};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q92871};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29.7 uM for mannose-1-phosphate {ECO:0000269|PubMed:17217471};
CC KM=65.4 uM for glucose-1-phosphate {ECO:0000269|PubMed:17217471};
CC Vmax=14.4 umol/min/mg enzyme with mannose-1-phosphate as substrate
CC {ECO:0000269|PubMed:17217471};
CC Vmax=1.4 umol/min/mg enzyme with glucose-1-phosphate as substrate
CC {ECO:0000269|PubMed:17217471};
CC Note=Glucose-1,6-bisphosphate is essential for activity.
CC {ECO:0000269|PubMed:17217471};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17217471};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:17217471};
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.
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 -!- DISRUPTION PHENOTYPE: The thermosensitive lethality of pmm-12 results
CC from glycosylation defects rather than ascorbic acid depletion.
CC {ECO:0000269|PubMed:18086684}.
CC -!- MISCELLANEOUS: Overexpression of PMM increases total leaf ascorbate
CC content. {ECO:0000269|PubMed:17217471}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR EMBL; DQ442991; ABD97870.1; -; mRNA.
DR EMBL; AC004665; AAC28545.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10601.1; -; Genomic_DNA.
DR EMBL; AY050806; AAK92741.1; -; mRNA.
DR EMBL; AY113964; AAM45012.1; -; mRNA.
DR EMBL; AY088930; AAM67236.1; -; mRNA.
DR PIR; T02468; T02468.
DR RefSeq; NP_182103.1; NM_130142.4.
DR AlphaFoldDB; O80840; -.
DR SMR; O80840; -.
DR BioGRID; 4523; 2.
DR IntAct; O80840; 1.
DR STRING; 3702.AT2G45790.1; -.
DR iPTMnet; O80840; -.
DR PaxDb; O80840; -.
DR PRIDE; O80840; -.
DR ProteomicsDB; 226150; -.
DR DNASU; 819187; -.
DR EnsemblPlants; AT2G45790.1; AT2G45790.1; AT2G45790.
DR GeneID; 819187; -.
DR Gramene; AT2G45790.1; AT2G45790.1; AT2G45790.
DR KEGG; ath:AT2G45790; -.
DR Araport; AT2G45790; -.
DR TAIR; locus:2050751; AT2G45790.
DR eggNOG; KOG3189; Eukaryota.
DR HOGENOM; CLU_065642_0_1_1; -.
DR InParanoid; O80840; -.
DR OMA; VCPIGRQ; -.
DR OrthoDB; 1038583at2759; -.
DR PhylomeDB; O80840; -.
DR BioCyc; ARA:AT2G45790-MON; -.
DR BioCyc; MetaCyc:AT2G45790-MON; -.
DR BRENDA; 5.4.2.8; 399.
DR UniPathway; UPA00126; UER00424.
DR PRO; PR:O80840; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80840; baseline and differential.
DR Genevisible; O80840; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IDA:TAIR.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
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..246
FT /note="Phosphomannomutase"
FT /id="PRO_0000199700"
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"
FT MUTAGEN 7
FT /note="G->R: In pmm-1; 18% reduction of catalytic activity.
FT In pmm-12/dgr1; 92% reduction of catalytic activity
FT resulting in lethality when grown at restrictive
FT temperature; when associated with Q-37."
FT /evidence="ECO:0000269|PubMed:18086684"
FT MUTAGEN 37
FT /note="R->Q: In pmm-2; 86% reduction of catalytic activity.
FT In pmm-12/dgr1; 92% reduction of catalytic activity
FT resulting in lethality when grown at restrictive
FT temperature; when associated with R-7."
FT /evidence="ECO:0000269|PubMed:18086684"
SQ SEQUENCE 246 AA; 27762 MW; 52971A3F1AE08DF9 CRC64;
MAAKIPGVIA LFDVDGTLTA PRKEATPELL DFIRELRKVV TIGVVGGSDL SKISEQLGKT
VTNDYDYCFS ENGLVAHKDG KSIGIQSLKL HLGDDKLKEL INFTLHYIAD LDIPIKRGTF
IEFRNGMLNV SPIGRNCSQE ERDEFERYDK VQNIRPKMVA ELRERFAHLN LTFSIGGQIS
FDVFPKGWDK TYCLQYLEDF SEIHFFGDKT YEGGNDYEIY ESPKTIGHSV TSPDDTVAKC
KALFMS
