ID   MPI_ASPFU               Reviewed;         457 AA.
AC   Q66WM4; Q4WSC2; Q6MYF6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 113.
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=pmi1; Synonyms=manA; ORFNames=AfA6E3.135c, AFUA_1G13280;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=YJ-407;
RA   Yu X., Jin C.;
RT   "Aspergillus fumigatus strain YJ-407 phosphomannose isomerase (pmi) mRNA.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA   Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA   Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S.,
RA   O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A.,
RA   Salzberg S.L., Saunders D., Seeger K., Sharp S., Warren T., Denning D.W.,
RA   Barrell B.G., Hall N.;
RT   "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT   region encompassing the nitrate assimilation gene cluster.";
RL   Fungal Genet. Biol. 41:443-453(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AY700212; AAU06585.1; -; mRNA.
DR   EMBL; BX649606; CAF32047.1; -; Genomic_DNA.
DR   EMBL; AAHF01000004; EAL90660.1; -; Genomic_DNA.
DR   RefSeq; XP_752698.1; XM_747605.1.
DR   AlphaFoldDB; Q66WM4; -.
DR   SMR; Q66WM4; -.
DR   STRING; 746128.CADAFUBP00001256; -.
DR   EnsemblFungi; EAL90660; EAL90660; AFUA_1G13280.
DR   GeneID; 3510576; -.
DR   KEGG; afm:AFUA_1G13280; -.
DR   VEuPathDB; FungiDB:Afu1g13280; -.
DR   eggNOG; KOG2757; Eukaryota.
DR   HOGENOM; CLU_026967_0_0_1; -.
DR   InParanoid; Q66WM4; -.
DR   OMA; DIGLFCG; -.
DR   OrthoDB; 1043197at2759; -.
DR   BRENDA; 5.3.1.8; 508.
DR   UniPathway; UPA00126; UER00423.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IDA:AspGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006013; P:mannose metabolic process; IMP:AspGD.
DR   GO; GO:0006486; P:protein glycosylation; IEA:EnsemblFungi.
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   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..457
FT                   /note="Mannose-6-phosphate isomerase"
FT                   /id="PRO_0000194240"
FT   ACT_SITE        311
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        80
FT                   /note="I -> V (in Ref. 1; AAU06585)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   457 AA;  49930 MW;  27C3E5F425BAA224 CRC64;
     MPPVPLLRLQ CGVNSYDWGK VGHESAAAKY AATTAASDFS IQSDKPYAEL WMGTHPSLPS
     KDLETQRTLL DMVQDNQALI SQEVSERYGG KLPFLFKVLS IRKALSIQAH PNKKLAEKLH
     ARDPRNYPDD NHKPEMTIAI TPFEGLCGFR PLVEIIHFLK AVAPLRQLVG ERAASEFENT
     VKGSEESEDP AVTEKNKQAL RTLFTSLMRS SPESIEAATK ELVAIAQNSP ETFTTSSSTP
     ETNPTNPAEL AAITVRLNGQ FPNDIGSFVF FFLNFVKLEP GEAMFLKADD IHAYISGDII
     ECMASSDNVV RAGFTPKFKD VDTLVDMLTY SYAPIAEQKL EPTDYPYAVL NAPAYSSGSS
     CILYDPPIEE FSVVKTDLKR QGAKATFDGI SGPSIVICTA GAGKITVGPK TEEVNEGYVF
     FVGANAECII ESTGEDTFTT FKAFCDLTGK EDMVNGN