ID MPI_DICDI Reviewed; 452 AA. AC Q54PA0; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 24-JAN-2024, entry version 113. 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=mpi; ORFNames=DDB_G0284685; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(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: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; AAFI02000070; EAL65112.1; -; Genomic_DNA. DR RefSeq; XP_638475.1; XM_633383.1. DR AlphaFoldDB; Q54PA0; -. DR SMR; Q54PA0; -. DR STRING; 44689.Q54PA0; -. DR PaxDb; 44689-DDB0231659; -. DR EnsemblProtists; EAL65112; EAL65112; DDB_G0284685. DR GeneID; 8624726; -. DR KEGG; ddi:DDB_G0284685; -. DR dictyBase; DDB_G0284685; mpi. DR eggNOG; KOG2757; Eukaryota. DR HOGENOM; CLU_026967_2_1_1; -. DR InParanoid; Q54PA0; -. DR OMA; DIGLFCG; -. DR PhylomeDB; Q54PA0; -. DR Reactome; R-DDI-446205; Synthesis of GDP-mannose. DR UniPathway; UPA00126; UER00423. DR PRO; PR:Q54PA0; -. DR Proteomes; UP000002195; Chromosome 4. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; ISS:dictyBase. 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; ISS:dictyBase. 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; 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; 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; PS00966; PMI_I_2; 1. PE 3: Inferred from homology; KW Cytoplasm; Isomerase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..452 FT /note="Probable mannose-6-phosphate isomerase" FT /id="PRO_0000327494" FT ACT_SITE 314 FT /evidence="ECO:0000250" FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 143 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 168 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 295 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" SQ SEQUENCE 452 AA; 51091 MW; FBD259EF215E6D47 CRC64; MENNNNNNNN NNNNNNNNNN IVLLKCVSQN YEWGKYGSNS TVAKLLKGYA KECSDIIKET IPYAELWMGD HVSAPSKVEY KNKELKLREY IDTVQKEINE KSSTSSSSSS SIRGEIVEKR FGNDFPFLFK VLSIRTALSI QAHPDSQLAQ VLFKKYPNIY KDPYHKPEIA IATTPFEALC SFRPLSEIQS FIDTIPEFKN SLPNNLIKLD DCKEYLKSIV TSLLKADGLL ISNNLKELNN RLNEKREEER DDLDRLVLKL YSQYPGDVGV FFAYILNYIV LKPGEALFLG AGEPHAYISG DCVECMAPSD NVVRAGLTPK LKDVDTLGDM LTYRTGRPDL VVPQQRPDLS LTNYRCYQPP VDEFQVEYYH LDDCCKNINV YSSKGPSIVL VYSGNLSIEN KSNQSTLNNL HTGSILFVPA NTDYQFIQSD SSIPVSIYVA SVSNRIFNKN NL //