MPI_YEAST
ID MPI_YEAST Reviewed; 429 AA.
AC P29952; D3DLP9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Mannose-6-phosphate isomerase;
DE EC=5.3.1.8;
DE AltName: Full=Phosphohexomutase;
DE AltName: Full=Phosphomannose isomerase;
DE Short=PMI;
GN Name=PMI40; OrderedLocusNames=YER003C;
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], PARTIAL PROTEIN SEQUENCE, CLEAVAGE OF
RP INITIATOR METHIONINE, AND ACETYLATION AT SER-2.
RX PubMed=1377774; DOI=10.1128/mcb.12.7.2924-2930.1992;
RA Smith D.J., Proudfoot A.E.I., Friedli L., Klig L.S., Paravicini G.,
RA Payton M.A.;
RT "PMI40, an intron-containing gene required for early steps in yeast
RT mannosylation.";
RL Mol. Cell. Biol. 12:2924-2930(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
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 [4]
RP INHIBITION BY ZINC.
RX PubMed=8448139; DOI=10.1021/bi00056a014;
RA Wells T.N.C., Coulin F., Payton M.A., Proudfoot A.E.I.;
RT "Phosphomannose isomerase from Saccharomyces cerevisiae contains two
RT inhibitory metal ion binding sites.";
RL Biochemistry 32:1294-1301(1993).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC EC=5.3.1.8;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- ACTIVITY REGULATION: Can be inhibited by an excess of zinc.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 1/2.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By D-mannose.
CC -!- MISCELLANEOUS: Present with 5220 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC {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; M85238; AAA34872.1; -; Genomic_DNA.
DR EMBL; U18778; AAB64536.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07653.1; -; Genomic_DNA.
DR PIR; S50461; S50461.
DR RefSeq; NP_010918.1; NM_001178894.1.
DR AlphaFoldDB; P29952; -.
DR SMR; P29952; -.
DR BioGRID; 36733; 392.
DR DIP; DIP-6619N; -.
DR IntAct; P29952; 2.
DR MINT; P29952; -.
DR STRING; 4932.YER003C; -.
DR BindingDB; P29952; -.
DR ChEMBL; CHEMBL3308954; -.
DR CarbonylDB; P29952; -.
DR iPTMnet; P29952; -.
DR UCD-2DPAGE; P29952; -.
DR MaxQB; P29952; -.
DR PaxDb; P29952; -.
DR PRIDE; P29952; -.
DR EnsemblFungi; YER003C_mRNA; YER003C; YER003C.
DR GeneID; 856720; -.
DR KEGG; sce:YER003C; -.
DR SGD; S000000805; PMI40.
DR VEuPathDB; FungiDB:YER003C; -.
DR eggNOG; KOG2757; Eukaryota.
DR GeneTree; ENSGT00390000016075; -.
DR HOGENOM; CLU_026967_0_0_1; -.
DR InParanoid; P29952; -.
DR OMA; DIGLFCG; -.
DR BioCyc; YEAST:YER003C-MON; -.
DR Reactome; R-SCE-446205; Synthesis of GDP-mannose.
DR SABIO-RK; P29952; -.
DR UniPathway; UPA00126; UER00423.
DR PRO; PR:P29952; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P29952; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:SGD.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IMP:SGD.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR001250; Man6P_Isoase-1.
DR InterPro; IPR016305; Mannose-6-P_Isomerase.
DR InterPro; IPR018050; Pmannose_isomerase-type1_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR10309; PTHR10309; 1.
DR Pfam; PF01238; PMI_typeI; 1.
DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1.
DR PRINTS; PR00714; MAN6PISMRASE.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR00218; manA; 1.
DR PROSITE; PS00965; PMI_I_1; 1.
DR PROSITE; PS00966; PMI_I_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Isomerase;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1377774"
FT CHAIN 2..429
FT /note="Mannose-6-phosphate isomerase"
FT /id="PRO_0000194247"
FT ACT_SITE 300
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:1377774"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 25
FT /note="A -> R (in Ref. 1; AAA34872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 48189 MW; C95E7C06B348A02F CRC64;
MSNKLFRLDA GYQQYDWGKI GSSSAVAQFA AHSDPSVQIE QDKPYAELWM GTHSKMPSYN
HESKESLRDI ISKNPSAMLG KDIIDKFHAT NELPFLFKVL SIEKVLSIQA HPDKALGKIL
HAQDPKNYPD DNHKPEMAIA VTDFEGFCGF KPLQEIADEL KRIPELRNIV GEETSRNFIE
NIQPSAQKGS PEDEQNKKLL QAVFSRVMNA SDDKIKIQAR SLVERSKNSP SDFNKPDLPE
LIQRLNKQFP DDVGLFCGCL LLNHCRLNAG EAIFLRAKDP HAYISGDIME CMAASDNVVR
AGFTPKFKDV KNLVSMLTYT YDPVEKQKMQ PLKFDRSSGN GKSVLYNPPI EEFAVLETTF
DEKLGQRHFE GVDGPSILIT TKGNGYIKAD GQKLKAEPGF VFFIAPHLPV DLEAEDEAFT
TYRAFVEPN
