PMM_YEAST
ID PMM_YEAST Reviewed; 254 AA.
AC P07283; D6VTI5; Q70D76; Q70D77;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Phosphomannomutase {ECO:0000303|PubMed:3288631};
DE Short=PMM;
DE EC=5.4.2.8 {ECO:0000269|PubMed:3288631};
DE AltName: Full=Asparagine-linked glycosylation protein 4 {ECO:0000303|PubMed:7037780};
GN Name=SEC53 {ECO:0000303|PubMed:3905826};
GN Synonyms=ALG4 {ECO:0000303|PubMed:7037780}; OrderedLocusNames=YFL045C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=3905826; DOI=10.1083/jcb.101.6.2374;
RA Bernstein M., Hoffmann W., Ammerer G., Schekman R.;
RT "Characterization of a gene product (Sec53p) required for protein assembly
RT in the yeast endoplasmic reticulum.";
RL J. Cell Biol. 101:2374-2382(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-234 AND ILE-249.
RC STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
RC CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
RX PubMed=15087486; DOI=10.1093/nar/gkh529;
RA Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA Souciet J.-L.;
RT "Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and
RT implication of recombination in phylogeny.";
RL Nucleic Acids Res. 32:2069-2078(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP GENE NAME.
RX PubMed=7037780; DOI=10.1016/s0021-9258(19)81096-7;
RA Huffaker T.C., Robbins P.W.;
RT "Temperature-sensitive yeast mutants deficient in asparagine-linked
RT glycosylation.";
RL J. Biol. Chem. 257:3203-3210(1982).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RX PubMed=3288631; DOI=10.1016/s0021-9258(19)76520-x;
RA Kepes F., Schekman R.;
RT "The yeast SEC53 gene encodes phosphomannomutase.";
RL J. Biol. Chem. 263:9155-9161(1988).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 such as folding and glycosylation of secretory proteins in
CC the ER lumen. {ECO:0000269|PubMed:3288631}.
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:3288631};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11142;
CC Evidence={ECO:0000305|PubMed:3288631};
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|PubMed:3288631}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:3288631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3905826}.
CC -!- MISCELLANEOUS: Present with 3500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR EMBL; X03213; CAA26957.1; -; Genomic_DNA.
DR EMBL; AJ585720; CAE52240.1; -; Genomic_DNA.
DR EMBL; AJ585721; CAE52241.1; -; Genomic_DNA.
DR EMBL; AJ585722; CAE52242.1; -; Genomic_DNA.
DR EMBL; AJ585723; CAE52243.1; -; Genomic_DNA.
DR EMBL; AJ585724; CAE52244.1; -; Genomic_DNA.
DR EMBL; AJ585725; CAE52245.1; -; Genomic_DNA.
DR EMBL; AJ585726; CAE52246.1; -; Genomic_DNA.
DR EMBL; AJ585727; CAE52247.1; -; Genomic_DNA.
DR EMBL; AJ585728; CAE52248.1; -; Genomic_DNA.
DR EMBL; AJ585729; CAE52249.1; -; Genomic_DNA.
DR EMBL; AJ585730; CAE52250.1; -; Genomic_DNA.
DR EMBL; AJ585731; CAE52251.1; -; Genomic_DNA.
DR EMBL; AJ585732; CAE52252.1; -; Genomic_DNA.
DR EMBL; AJ585733; CAE52253.1; -; Genomic_DNA.
DR EMBL; AJ585734; CAE52254.1; -; Genomic_DNA.
DR EMBL; AJ585735; CAE52255.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09196.1; -; Genomic_DNA.
DR EMBL; AY692959; AAT92978.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12395.1; -; Genomic_DNA.
DR PIR; S05874; BVBY53.
DR RefSeq; NP_116609.1; NM_001179922.1.
DR AlphaFoldDB; P07283; -.
DR SMR; P07283; -.
DR BioGRID; 31102; 290.
DR DIP; DIP-4312N; -.
DR IntAct; P07283; 28.
DR MINT; P07283; -.
DR STRING; 4932.YFL045C; -.
DR iPTMnet; P07283; -.
DR SWISS-2DPAGE; P07283; -.
DR MaxQB; P07283; -.
DR PaxDb; P07283; -.
DR PRIDE; P07283; -.
DR EnsemblFungi; YFL045C_mRNA; YFL045C; YFL045C.
DR GeneID; 850499; -.
DR KEGG; sce:YFL045C; -.
DR SGD; S000001849; SEC53.
DR VEuPathDB; FungiDB:YFL045C; -.
DR eggNOG; KOG3189; Eukaryota.
DR GeneTree; ENSGT00390000002918; -.
DR HOGENOM; CLU_065642_0_1_1; -.
DR InParanoid; P07283; -.
DR OMA; VCPIGRQ; -.
DR BioCyc; YEAST:YFL045C-MON; -.
DR Reactome; R-SCE-446205; Synthesis of GDP-mannose.
DR UniPathway; UPA00126; UER00424.
DR PRO; PR:P07283; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P07283; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IDA:SGD.
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 1: Evidence at protein level;
KW Cytoplasm; Isomerase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Phosphomannomutase"
FT /id="PRO_0000199703"
FT ACT_SITE 19
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT ACT_SITE 21
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT BINDING 28
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 130
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 148
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 186
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 188
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P31353"
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 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT VARIANT 234
FT /note="I -> T (in strain: CLIB 556 haplotype Ha1)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 249
FT /note="T -> I (in strain: R12 haplotype Ha1)"
FT /evidence="ECO:0000269|PubMed:15087486"
SQ SEQUENCE 254 AA; 29063 MW; B58C88A746368779 CRC64;
MSIAEFAYKE KPETLVLFDV DGTLTPARLT VSEEVRKTLA KLRNKCCIGF VGGSDLSKQL
EQLGPNVLDE FDYSFSENGL TAYRLGKELA SQSFINWLGE EKYNKLAVFI LRYLSEIDLP
KRRGTFLEFR NGMINVSPIG RNASTEERNE FERYDKEHQI RAKFVEALKK EFPDYGLTFS
IGGQISFDVF PAGWDKTYCL QHVEKDGFKE IHFFGDKTMV GGNDYEIFVD ERTIGHSVQS
PDDTVKILTE LFNL
