ID   MPI_ECHMU               Reviewed;         433 AA.
AC   Q9GP38;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable mannose-6-phosphate isomerase;
DE            EC=5.3.1.8;
DE   AltName: Full=Phosphohexomutase;
DE   AltName: Full=Phosphomannose isomerase;
DE            Short=PMI;
GN   Name=PMIH;
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=H-95;
RX   PubMed=10973970; DOI=10.1074/jbc.m006091200;
RA   Brehm K., Jensen K., Frosch M.;
RT   "mRNA trans-splicing in the human parasitic cestode Echinococcus
RT   multilocularis.";
RL   J. Biol. Chem. 275:38311-38318(2000).
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}.
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; AJ292370; CAC18544.1; -; mRNA.
DR   AlphaFoldDB; Q9GP38; -.
DR   SMR; Q9GP38; -.
DR   eggNOG; KOG2757; Eukaryota.
DR   OMA; DIGLFCG; -.
DR   UniPathway; UPA00126; UER00423.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
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; PS00966; PMI_I_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Metal-binding; Zinc.
FT   CHAIN           1..433
FT                   /note="Probable mannose-6-phosphate isomerase"
FT                   /id="PRO_0000194234"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   433 AA;  47858 MW;  708C1268CECEB65D CRC64;
     MLRLKCASQR YDWGKVGVNS IVYKLQVASE NPDISHVDLP YAELWMGTHP SGSSCLWDNP
     HVTLAAHIQE NPASLGKPSL IYFGRRLPFL FKVLSVAKAL SIQAHPDKKM AVRLHAEQPD
     LYKDGSHKPE MAIALTDFEA LLGFRPLNQI LAFIQAFPEL AELTTLELPS PEEKRDVQPP
     SIKQLYSNLM RSSPEKVEST IKSLLNRFTT GSKSVCDPPL SILGVDLQEE DVQALVDLFL
     RLTQAFPGDV GCLSIFFLNY IRLKSGEAIF LKANTPHAYL SGDCVECMAN SDNVVRAGLT
     PKFKDVERLL EMLDYTPLTD SLRLGATQPI PTPEGISMKS FIPPVSEFAV DVIQFDAESR
     GFSLPSVPTA SILLFLHGQG TITCPSTGEA CSQETKFGPG FVYFVPADMI VNLVSKEDRK
     GSLHAFRAYV NRK