ID   MPI_CRYNJ               Reviewed;         434 AA.
AC   Q9HFU4; Q5KBJ0;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   24-JAN-2024, entry version 129.
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=MAN1; OrderedLocusNames=CNI02370;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11359567; DOI=10.1046/j.1365-2958.2001.02401.x;
RA   Wills E.A., Roberts I.S., Del Poeta M., Rivera J., Casadevall A., Cox G.M.,
RA   Perfect J.R.;
RT   "Identification and characterization of the Cryptococcus neoformans
RT   phosphomannose isomerase-encoding gene, MAN1, and its impact on
RT   pathogenicity.";
RL   Mol. Microbiol. 40:610-620(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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=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; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF291701; AAG10203.1; -; Genomic_DNA.
DR   EMBL; AE017349; AAW45398.1; -; Genomic_DNA.
DR   RefSeq; XP_572705.1; XM_572705.1.
DR   AlphaFoldDB; Q9HFU4; -.
DR   SMR; Q9HFU4; -.
DR   STRING; 214684.Q9HFU4; -.
DR   PaxDb; 214684-Q9HFU4; -.
DR   EnsemblFungi; AAW45398; AAW45398; CNI02370.
DR   GeneID; 3259465; -.
DR   KEGG; cne:CNI02370; -.
DR   VEuPathDB; FungiDB:CNI02370; -.
DR   eggNOG; KOG2757; Eukaryota.
DR   HOGENOM; CLU_026967_0_0_1; -.
DR   InParanoid; Q9HFU4; -.
DR   OMA; DIGLFCG; -.
DR   OrthoDB; 1116301at2759; -.
DR   UniPathway; UPA00126; UER00423.
DR   PHI-base; PHI:220; -.
DR   Proteomes; UP000002149; Chromosome 9.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR   CDD; cd07011; cupin_PMI_type_I_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 1.10.441.10; Phosphomannose Isomerase, domain 2; 1.
DR   InterPro; IPR001250; Man6P_Isoase-1.
DR   InterPro; IPR016305; Mannose-6-P_Isomerase.
DR   InterPro; IPR018050; Pmannose_isomerase-type1_CS.
DR   InterPro; IPR046456; PMI_typeI_C.
DR   InterPro; IPR046457; PMI_typeI_cat.
DR   InterPro; IPR046458; PMI_typeI_hel.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   NCBIfam; TIGR00218; manA; 1.
DR   PANTHER; PTHR10309; MANNOSE-6-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR10309:SF0; MANNOSE-6-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF01238; PMI_typeI_C; 1.
DR   Pfam; PF20511; PMI_typeI_cat; 1.
DR   Pfam; PF20512; PMI_typeI_hel; 1.
DR   PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1.
DR   PRINTS; PR00714; MAN6PISMRASE.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   PROSITE; PS00965; PMI_I_1; 1.
DR   PROSITE; PS00966; PMI_I_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..434
FT                   /note="Mannose-6-phosphate isomerase"
FT                   /id="PRO_0000194243"
FT   REGION          181..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        310
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         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        38
FT                   /note="S -> A (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="K -> R (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="K -> R (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79..80
FT                   /note="SS -> TT (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="S -> P (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="G -> D (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="T -> S (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="L -> H (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="Q -> K (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="S -> D (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="P -> S (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        396
FT                   /note="N -> D (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400..401
FT                   /note="RS -> QT (in Ref. 1; AAG10203)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   434 AA;  47590 MW;  4C2541EEFE9793FF CRC64;
     MSPSVFKISP GINSYDWGKK GSASLAAQLA TTSIPDFSID EDKAYAELWM GTHPNNPSRL
     SDNTLLSEHL KSHPELIGSS VSSKFEDCKD GSLPFLFKVL SIGTALSIQA HPDKPLAKKL
     FDEKPDVYKD PNHKPEMAIA LTPFLAFLNF LPLSVLLLHL LTVPELQEFV DSSLTESLAS
     SLGLPTSQPP DTSLFKPTES PATAEQKDIL KQIFAALMSA DKKLVEEAIS KLIKRYQAKR
     DIKENEKSLV DLALRLNDQY PGDVGVLCVF LLNVVELKRG EAAFLGANEP HAYIEGDIIE
     CMATSDNVVR AGLTPKLRDV DTLVSMLTYE AAPGNKQLLQ PTPFQKGDDT TKLYDPPIAE
     FSVLRTELSK GMKTSHRPVE GPSLCVITEG EGVVRNGNDR SEFVRGDVIF VGAGKEVEWE
     AIKGLEMFRA YVEA
//