ID PMM_ENCCU Reviewed; 256 AA. AC Q8SVM5; DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 13-SEP-2023, entry version 97. DE RecName: Full=Phosphomannomutase; DE Short=PMM; DE EC=5.4.2.8; GN Name=SEC53; OrderedLocusNames=ECU05_0260; OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite). OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae; OC Encephalitozoon. OX NCBI_TaxID=284813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GB-M1; RX PubMed=11719806; DOI=10.1038/35106579; RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., RA Vivares C.P.; RT "Genome sequence and gene compaction of the eukaryote parasite RT Encephalitozoon cuniculi."; RL Nature 414:450-453(2001). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND RP DEVELOPMENTAL STAGE. RX PubMed=16691553; DOI=10.1002/pmic.200500796; RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.; RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi RT (microsporidia): a reference map for proteins expressed in late sporogonial RT stages."; RL Proteomics 6:3625-3635(2006). CC -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol- CC phosphate-mannose required for a number of critical mannosyl transfer CC reactions. {ECO:0000250}. 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; 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}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages. CC {ECO:0000269|PubMed:16691553}. 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; AL590445; CAD26542.1; -; Genomic_DNA. DR RefSeq; NP_597365.1; NM_001041231.1. DR AlphaFoldDB; Q8SVM5; -. DR SMR; Q8SVM5; -. DR STRING; 284813.Q8SVM5; -. DR GeneID; 859029; -. DR KEGG; ecu:ECU05_0260; -. DR VEuPathDB; MicrosporidiaDB:ECU05_0260; -. DR HOGENOM; CLU_065642_0_1_1; -. DR InParanoid; Q8SVM5; -. DR OMA; ISHRVYT; -. DR OrthoDB; 167037at2759; -. DR UniPathway; UPA00126; UER00424. DR Proteomes; UP000000819; Chromosome V. 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 1: Evidence at protein level; KW Cytoplasm; Isomerase; Magnesium; Metal-binding; Reference proteome. FT CHAIN 1..256 FT /note="Phosphomannomutase" FT /id="PRO_0000382908" FT ACT_SITE 12 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT ACT_SITE 14 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 12 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P31353" FT BINDING 14 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P31353" FT BINDING 21 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 123 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 134 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 141 FT /ligand="alpha-D-mannose 1-phosphate" FT /ligand_id="ChEBI:CHEBI:58409" FT /evidence="ECO:0000250|UniProtKB:Q92871" FT BINDING 179 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 209 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P31353" SQ SEQUENCE 256 AA; 29616 MW; DBDEFE2929D73D10 CRC64; MARDEKTIFL FDVDGTLSES RAKMPEKMGK MLESLRRKVR IGFVGGSDLA KQKEQVGDNI LEIFDYGFPE NGVSFYKNGT LESQEKIIDV LGEEFYKEFA NFVLRYLSDI DLPIKRGNFI EYRNSMINIS PIGRNCSREE RMKFFELDKK EKFREKMVTA MRDRFKDSCL VFSIGGQISI DCFPKGWDKT YCLRHIKKEG VENVYFFGDM TMEGGNDYEI YNHKDVHGIS VGNPDDTYRK VDQALKKIGL GGLEEN //