ID   MPI_EMENI               Reviewed;         461 AA.
AC   P29951; C8VRS9; Q5BFL3;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   24-JAN-2024, entry version 144.
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=manA; ORFNames=AN0667;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8307007; DOI=10.1111/j.1432-1033.1994.tb19954.x;
RA   Proudfoot A.E.I., Turcatti G., Wells T.N.C., Payton M.A., Smith D.J.;
RT   "Purification, cDNA cloning and heterologous expression of human
RT   phosphomannose isomerase.";
RL   Eur. J. Biochem. 219:415-423(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(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.
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:0000305}.
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; M85239; AAA33319.1; -; Genomic_DNA.
DR   EMBL; AACD01000010; EAA65443.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF89025.1; -; Genomic_DNA.
DR   PIR; A56239; A56239.
DR   RefSeq; XP_658271.1; XM_653179.1.
DR   AlphaFoldDB; P29951; -.
DR   SMR; P29951; -.
DR   STRING; 227321.P29951; -.
DR   EnsemblFungi; CBF89025; CBF89025; ANIA_00667.
DR   GeneID; 2876445; -.
DR   KEGG; ani:AN0667.2; -.
DR   eggNOG; KOG2757; Eukaryota.
DR   HOGENOM; CLU_026967_0_0_1; -.
DR   InParanoid; P29951; -.
DR   OMA; DIGLFCG; -.
DR   OrthoDB; 1116301at2759; -.
DR   UniPathway; UPA00126; UER00423.
DR   Proteomes; UP000000560; Chromosome VIII.
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:0000032; P:cell wall mannoprotein biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:EnsemblFungi.
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..461
FT                   /note="Mannose-6-phosphate isomerase"
FT                   /id="PRO_0000194244"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
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        19
FT                   /note="R -> K (in Ref. 1; AAA33319)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   461 AA;  50613 MW;  17E0D089A6656F79 CRC64;
     MQVPLLRLQC GVNSYDWGRV GPESAAAKYA AATAPSDFTI EADKPYAELW MGTHPSLPSK
     DVETQRTLLD MVQDNLALMS PEVSERYGGK LPFLFKVLSI RKALSIQAHP NKKLAEALHA
     RDPRNYPDDN HKPEMTIAIT PFEGLCGFRP LAEIVHFLKA VAPLRYLIGV QTATDFENAV
     RGFENTEDPE QTKKNKVALR TLFTSLMQSA SENIEQAARE LVAAAQSSPE TFASLVNAPD
     TNPTNAAELA SIIIRLNEQF PNDIGLFVFF FLNFVRLEPG EAMFLKADDI HAYISGDIIE
     CMASSDNVVR AGFTPKFKDV DTLTEMLTYS YAPIDEQKLQ PTDYPYTVLN AAAYSSASDS
     LLYDPPIEEF SVVKTSLRRT GAKATFDPLT GPSILICTGG TGKISVGHKT EEVKEGYVFF
     VGANAECIIE NTGTGSDEEN VFTTFKAFCD LTGKEDMANG H
//