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   27-MAR-2024, entry version 201.
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; 302.
DR   DIP; DIP-4312N; -.
DR   IntAct; P07283; 28.
DR   MINT; P07283; -.
DR   STRING; 4932.YFL045C; -.
DR   iPTMnet; P07283; -.
DR   MaxQB; P07283; -.
DR   PaxDb; 4932-YFL045C; -.
DR   PeptideAtlas; P07283; -.
DR   EnsemblFungi; YFL045C_mRNA; YFL045C; YFL045C.
DR   GeneID; 850499; -.
DR   KEGG; sce:YFL045C; -.
DR   AGR; SGD:S000001849; -.
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; ISHRVYT; -.
DR   OrthoDB; 167037at2759; -.
DR   BioCyc; YEAST:YFL045C-MONOMER; -.
DR   Reactome; R-SCE-446205; Synthesis of GDP-mannose.
DR   UniPathway; UPA00126; UER00424.
DR   BioGRID-ORCS; 850499; 1 hit in 10 CRISPR screens.
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; 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; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SWISS-2DPAGE; P07283; -.
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
//