ID   PMM_ORYSJ               Reviewed;         248 AA.
AC   Q7XPW5; B7E696;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   24-JAN-2024, entry version 128.
DE   RecName: Full=Phosphomannomutase {ECO:0000303|PubMed:17217471};
DE            Short=OsPMM {ECO:0000303|PubMed:17217471};
DE            EC=5.4.2.8 {ECO:0000269|PubMed:20920368};
GN   Name=PMM {ECO:0000303|PubMed:17217471};
GN   OrderedLocusNames=Os04g0682300 {ECO:0000312|EMBL:BAS91688.1},
GN   LOC_Os04g58580 {ECO:0000305};
GN   ORFNames=OsJ_015937 {ECO:0000312|EMBL:EAZ32454.1}, OSJNBa0032F06.16
GN   {ECO:0000312|EMBL:CAE03433.2};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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). {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   -!- 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   -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR   EMBL; DQ442992; ABD97871.1; -; mRNA.
DR   EMBL; AL606641; CAE03433.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF16209.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS91688.1; -; Genomic_DNA.
DR   EMBL; CM000141; EAZ32454.1; -; Genomic_DNA.
DR   EMBL; AK061384; BAG87893.1; -; mRNA.
DR   EMBL; AK104004; BAG96367.1; -; mRNA.
DR   RefSeq; XP_015633714.1; XM_015778228.1.
DR   AlphaFoldDB; Q7XPW5; -.
DR   SMR; Q7XPW5; -.
DR   STRING; 39947.Q7XPW5; -.
DR   PaxDb; 39947-Q7XPW5; -.
DR   EnsemblPlants; Os04t0682300-01; Os04t0682300-01; Os04g0682300.
DR   EnsemblPlants; Os04t0682300-02; Os04t0682300-02; Os04g0682300.
DR   GeneID; 4337437; -.
DR   Gramene; Os04t0682300-01; Os04t0682300-01; Os04g0682300.
DR   Gramene; Os04t0682300-02; Os04t0682300-02; Os04g0682300.
DR   KEGG; osa:4337437; -.
DR   eggNOG; KOG3189; Eukaryota.
DR   HOGENOM; CLU_065642_0_1_1; -.
DR   InParanoid; Q7XPW5; -.
DR   OMA; ISHRVYT; -.
DR   OrthoDB; 167037at2759; -.
DR   PlantReactome; R-OSA-1119410; Ascorbate biosynthesis.
DR   PlantReactome; R-OSA-1119628; GDP-mannose metabolism.
DR   UniPathway; UPA00126; UER00424.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000007752; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   ExpressionAtlas; Q7XPW5; 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:SF0; PHOSPHOMANNOMUTASE; 1.
DR   Pfam; PF03332; PMM; 1.
DR   SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR   SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   Genevisible; Q7XPW5; OS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isomerase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..248
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000326493"
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   ACT_SITE        16
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         23
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         125
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         136
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         143
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         181
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         183
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P31353"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
SQ   SEQUENCE   248 AA;  28193 MW;  C28CA4DD5B233DE5 CRC64;
     MAARKNAGVL ALFDVDGTLT APRKVVTPEM LQFMKQLREH VTVGVVGGSD LVKISEQLGK
     SVTTDYDYCF SENGLVAHKN GELIGTQSLK SFLGDDQLKE FINFTLHYIA DLDIPIKRGT
     FIEFRSGMLN VSPIGRNCSQ EERDEFEKYD KVHNIRPKMV SVLREKFAHL NLTFSIGGQI
     SFDVFPQGWD KTYCLRYLEE FQEIHFFGDK TYKGGNDYEI FESDRTIGHT VTSPDDTAEQ
     CRSLFMSK
//