ID   MPI_BOVIN               Reviewed;         423 AA.
AC   Q3SZI0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 107.
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=MPI;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; BC102844; AAI02845.1; -; mRNA.
DR   RefSeq; NP_001030361.1; NM_001035284.1.
DR   AlphaFoldDB; Q3SZI0; -.
DR   SMR; Q3SZI0; -.
DR   STRING; 9913.ENSBTAP00000007684; -.
DR   PRIDE; Q3SZI0; -.
DR   Ensembl; ENSBTAT00000007684; ENSBTAP00000007684; ENSBTAG00000005845.
DR   GeneID; 513586; -.
DR   KEGG; bta:513586; -.
DR   CTD; 4351; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005845; -.
DR   VGNC; VGNC:50218; MPI.
DR   eggNOG; KOG2757; Eukaryota.
DR   GeneTree; ENSGT00390000016075; -.
DR   InParanoid; Q3SZI0; -.
DR   OMA; DIGLFCG; -.
DR   OrthoDB; 1043197at2759; -.
DR   UniPathway; UPA00126; UER00423.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000005845; Expressed in biceps femoris and 107 other tissues.
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:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR   GO; GO:0061611; P:mannose to fructose-6-phosphate metabolic process; IEA:Ensembl.
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   Acetylation; Cytoplasm; Isomerase; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P34949"
FT   CHAIN           2..423
FT                   /note="Mannose-6-phosphate isomerase"
FT                   /id="PRO_0000245030"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P34949"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34949"
FT   MOD_RES         108
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34949"
SQ   SEQUENCE   423 AA;  46369 MW;  9BE8AB8D3B8B37E5 CRC64;
     MAAQRVFPLS CVVQQYAWGK MGSNSEVARL LASSDPLAQI SEDRPYAELW MGTHPRGDAK
     ILDNRISQKT LGQWIADNQD SLGSKVKDTF NGKLPFLFKV LSVETALSIQ AHPNKELAEK
     LHLQAPQHYP DANHKPEMAI ALTPFQGLCG FRPVEEIVTF LTKVPEFQFL IGDNAAAQLK
     QSLSQDSEAV TSALRSCFSH LMKSEKKVVV EQLNLLVKRI SQQVAAGNNM EDICGELLLQ
     LHQQYPGDIG CFAIYFLNLL TLKPGEAMFL EANVPHAYLK GDCVECMACS DNTVRAGLTP
     KFIDVPTLCE MLSYTPSPSQ DRLFPPARSP EDPYLSIYDP PVPDFTVMKV EVPGSVTEYK
     VLALDSASIL LVVQGTVTAS SPTAQAAIPL KRGGVLFIGA NESVSLKLTV PKDLLMFRAC
     CLL