PMM_CAEEL
ID PMM_CAEEL Reviewed; 254 AA.
AC Q9XUE6; E3W758;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable phosphomannomutase;
DE Short=PMM;
DE EC=5.4.2.8;
GN ORFNames=F52B11.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q9XUE6-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q9XUE6-2; Sequence=VSP_041635;
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR EMBL; Z82268; CAB05198.3; -; Genomic_DNA.
DR EMBL; Z82268; CBX53327.1; -; Genomic_DNA.
DR PIR; T22485; T22485.
DR RefSeq; NP_001255786.1; NM_001268857.1. [Q9XUE6-1]
DR RefSeq; NP_001255787.1; NM_001268858.1. [Q9XUE6-2]
DR AlphaFoldDB; Q9XUE6; -.
DR SMR; Q9XUE6; -.
DR BioGRID; 43448; 4.
DR IntAct; Q9XUE6; 1.
DR STRING; 6239.F52B11.2a; -.
DR EPD; Q9XUE6; -.
DR PaxDb; Q9XUE6; -.
DR PeptideAtlas; Q9XUE6; -.
DR EnsemblMetazoa; F52B11.2a.1; F52B11.2a.1; WBGene00009925. [Q9XUE6-1]
DR EnsemblMetazoa; F52B11.2b.1; F52B11.2b.1; WBGene00009925. [Q9XUE6-2]
DR GeneID; 178364; -.
DR KEGG; cel:CELE_F52B11.2; -.
DR UCSC; F52B11.2; c. elegans. [Q9XUE6-1]
DR CTD; 178364; -.
DR WormBase; F52B11.2a; CE44567; WBGene00009925; -. [Q9XUE6-1]
DR WormBase; F52B11.2b; CE36163; WBGene00009925; -. [Q9XUE6-2]
DR eggNOG; KOG3189; Eukaryota.
DR GeneTree; ENSGT00390000002918; -.
DR HOGENOM; CLU_065642_0_1_1; -.
DR InParanoid; Q9XUE6; -.
DR OMA; VCPIGRQ; -.
DR OrthoDB; 1038583at2759; -.
DR PhylomeDB; Q9XUE6; -.
DR Reactome; R-CEL-446205; Synthesis of GDP-mannose.
DR UniPathway; UPA00126; UER00424.
DR PRO; PR:Q9XUE6; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00009925; Expressed in adult organism and 4 other tissues.
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; -; 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 3: Inferred from homology;
KW Alternative splicing; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Probable phosphomannomutase"
FT /id="PRO_0000199698"
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 129
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 140
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 147
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 185
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 187
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_041635"
SQ SEQUENCE 254 AA; 28839 MW; F4E0339B8C7DD8A8 CRC64;
MTSPASSRTI LVFDVDGTLT AARQTITPEM REFLIEARKR VPLAIVGGSD FKKITEQLAD
HDKDLLLSLF DYTFSENGLY GFKGTEPYPV QSIQKAIGDA KLQELINFAL RYMSDIQLPV
KRGNFVEFRN GMINLSPIGR SCSQEERMQF VEFDKKHGIR QKFTEQLREK FGQYGLQFAI
GGQISVDVFP TGWDKTFCLQ YLVPDFDTIH FFGDKTAPGG NDHEIFADER TVGHTVEGPE
DTRKHVENVL KELD
