ID PMM_ORYSI Reviewed; 248 AA. AC Q259G4; A2XZ30; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 13-SEP-2023, entry version 80. DE RecName: Full=Phosphomannomutase {ECO:0000305}; DE Short=OsPMM {ECO:0000305}; DE EC=5.4.2.8 {ECO:0000250|UniProtKB:Q7XPW5}; GN Name=PMM {ECO:0000305}; GN ORFNames=H0124B04.12 {ECO:0000312|EMBL:CAJ86295.1}, OsI_017323 GN {ECO:0000312|EMBL:CM000129}; OS Oryza sativa subsp. indica (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=39946; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Guang-Lu-Ai No.4; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11; 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). CC -!- FUNCTION: Catalyzes the interconversion of mannose-6-phosphate to CC mannose-1-phosphate, the precursor for the synthesis of GDP-mannose (By CC similarity). 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). {ECO:0000250|UniProtKB:Q7XPW5, CC 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:0000250|UniProtKB:Q7XPW5}; 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}. 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; AL732352; CAJ86295.1; -; Genomic_DNA. DR EMBL; CM000129; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; Q259G4; -. DR SMR; Q259G4; -. DR STRING; 39946.Q259G4; -. DR UniPathway; UPA00126; UER00424. DR Proteomes; UP000007015; Chromosome 4. 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; IEA:UniProtKB-EC. DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway. 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. PE 3: Inferred from homology; KW Cytoplasm; Isomerase; Magnesium; Metal-binding; Reference proteome. FT CHAIN 1..248 FT /note="Phosphomannomutase" FT /id="PRO_0000326492" 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 //