ID PMM2_MACFA Reviewed; 246 AA. AC Q60HD6; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 24-JAN-2024, entry version 81. DE RecName: Full=Phosphomannomutase 2; DE Short=PMM 2; DE EC=5.4.2.8; GN Name=PMM2; ORFNames=QtrA-14736; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Temporal cortex; RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.; RT "Isolation and characterization of cDNA for macaque neurological disease RT genes."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AB125191; BAD51979.1; -; mRNA. DR RefSeq; NP_001272027.1; NM_001285098.1. DR RefSeq; XP_015297658.1; XM_015442172.1. DR AlphaFoldDB; Q60HD6; -. DR SMR; Q60HD6; -. DR STRING; 9541.ENSMFAP00000017019; -. DR GeneID; 102146519; -. DR KEGG; mcf:102146519; -. DR CTD; 5373; -. DR eggNOG; KOG3189; Eukaryota. DR OrthoDB; 167037at2759; -. DR UniPathway; UPA00126; UER00424. DR Proteomes; UP000233100; Unplaced. 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:SF2; PHOSPHOMANNOMUTASE 2; 1. DR Pfam; PF03332; PMM; 1. DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Isomerase; Magnesium; Metal-binding; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:O15305" FT CHAIN 2..246 FT /note="Phosphomannomutase 2" FT /id="PRO_0000199695" 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 /ligand_label="1" 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 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 /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 223 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" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:O15305" FT MOD_RES 149 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9Z2M7" SQ SEQUENCE 246 AA; 28024 MW; 39F129672C141EB2 CRC64; MAAPGPALCL FDVDGTLTAP RQKITKEMDD FLQKLRQKIK IGVVGGSDFE KVQEQLGNDV VEKYDYVFPE NGLVAYKDGK LLCKQNIQSH LGEALIQDLI NYCLSYIAKV KLPKKRGTFI EFRNGMLNVS PIGRSCSQEE RIEFYELDKK ENIRQKFVAD LRKEFAGKGL TFSIGGQISF DVFPDGWDKR YCLRHVENDG YKTIYFFGDK TMPGGNDHEI FTDPRTVGYS VTAPEDTRRI CEELFS //