MPI_CRYNJ
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 03-AUG-2022, entry version 124.
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; 5207.AAW45398; -.
DR PaxDb; 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; 1043197at2759; -.
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 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 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
