ID MANA_SALTY Reviewed; 391 AA. AC P25081; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 157. 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; Synonyms=pmi; OrderedLocusNames=STM1467; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C5; RX PubMed=1879695; DOI=10.1016/0378-1119(91)90406-2; RA Collins L.V., Hackett J.; RT "Sequence of the phosphomannose isomerase-encoding gene of Salmonella RT typhimurium."; RL Gene 103:135-136(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). CC -!- FUNCTION: Involved in the conversion of glucose to GDP-L-fucose, which CC can be converted to L-fucose, a capsular polysaccharide. 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 -!- 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; X57117; CAA40399.1; -; Genomic_DNA. DR EMBL; AE006468; AAL20387.1; -; Genomic_DNA. DR PIR; JQ1192; JQ1192. DR RefSeq; NP_460428.1; NC_003197.2. DR RefSeq; WP_001170627.1; NC_003197.2. DR PDB; 2WFP; X-ray; 1.67 A; A=1-391. DR PDB; 3H1M; X-ray; 2.50 A; A=1-391. DR PDB; 3H1W; X-ray; 1.94 A; A=1-391. DR PDB; 3H1Y; X-ray; 2.04 A; A=1-391. DR PDB; 5ZT4; X-ray; 1.70 A; A=1-391. DR PDB; 5ZT5; X-ray; 1.90 A; A=1-391. DR PDB; 5ZT6; X-ray; 2.50 A; A=1-391. DR PDB; 5ZUW; X-ray; 2.10 A; A=1-391. DR PDB; 5ZUY; X-ray; 2.00 A; A=1-391. DR PDB; 5ZV0; X-ray; 2.10 A; A=1-391. DR PDB; 5ZVR; X-ray; 1.93 A; A=1-391. DR PDB; 5ZVU; X-ray; 2.20 A; A=1-391. DR PDB; 5ZVX; X-ray; 1.70 A; A=1-391. DR PDBsum; 2WFP; -. DR PDBsum; 3H1M; -. DR PDBsum; 3H1W; -. DR PDBsum; 3H1Y; -. DR PDBsum; 5ZT4; -. DR PDBsum; 5ZT5; -. DR PDBsum; 5ZT6; -. DR PDBsum; 5ZUW; -. DR PDBsum; 5ZUY; -. DR PDBsum; 5ZV0; -. DR PDBsum; 5ZVR; -. DR PDBsum; 5ZVU; -. DR PDBsum; 5ZVX; -. DR AlphaFoldDB; P25081; -. DR SMR; P25081; -. DR STRING; 99287.STM1467; -. DR PaxDb; 99287-STM1467; -. DR GeneID; 1252985; -. DR KEGG; stm:STM1467; -. DR PATRIC; fig|99287.12.peg.1549; -. DR HOGENOM; CLU_026967_1_0_6; -. DR OMA; DIGLFCG; -. DR PhylomeDB; P25081; -. DR BioCyc; SENT99287:STM1467-MONOMER; -. DR BRENDA; 5.3.1.8; 5542. DR EvolutionaryTrace; P25081; -. DR PHI-base; PHI:8136; -. DR Proteomes; UP000001014; Chromosome. 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:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central. 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; IPR049071; MPI_cupin_dom. 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; PF21621; MPI_cupin_dom; 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Isomerase; Metal-binding; Reference proteome; KW Zinc. FT CHAIN 1..391 FT /note="Mannose-6-phosphate isomerase" FT /id="PRO_0000194231" FT ACT_SITE 274 FT /evidence="ECO:0000250" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 99 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 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT CONFLICT 92 FT /note="Q -> K (in Ref. 1; CAA40399)" FT /evidence="ECO:0000305" FT STRAND 1..3 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 14..17 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 18..23 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:5ZUY" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:5ZT4" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:5ZT4" FT HELIX 58..64 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 66..70 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 72..77 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 84..92 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:5ZVU" FT HELIX 102..114 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:5ZT5" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:5ZT4" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 142..148 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 151..158 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 159..164 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 166..173 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 177..188 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 192..208 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 214..223 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 228..231 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 236..241 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 246..249 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 255..266 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 276..280 FT /evidence="ECO:0007829|PDB:5ZT4" FT HELIX 284..289 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 311..313 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 317..320 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 322..327 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 341..354 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 357..361 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 366..369 FT /evidence="ECO:0007829|PDB:2WFP" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:2WFP" FT STRAND 376..388 FT /evidence="ECO:0007829|PDB:2WFP" SQ SEQUENCE 391 AA; 42591 MW; 61E7355146DBEF5A CRC64; MQKLINSVQN YAWGSKTALT ELYGIANPQQ QPMAELWMGA HPKSSSRITT ANGETVSLRD AIEKNKTAML GEAVANRFGE LPFLFKVLCA AQPLSIQVHP NKRNSEIGFA KENAAGIPMD AAERNYKDPN HKPELVFALT PFLAMNAFRE FSDIVSLLQP VAGAHSAIAH FLQVPNAERL SQLFASLLNM QGEEKSRALA VLKAALNSQQ GEPWQTIRVI SEYYPDDSGL FSPLLLNVVK LNPGEAMFLF AETPHAYLQG VALEVMANSD NVLRAGLTPK YIDIPELVAN VKFEPKPAGE LLTAPVKSGA ELDFPIPVDD FAFSLHDLAL QETSIGQHSA AILFCVEGEA VLRKDEQRLV LKPGESAFIG ADESPVNASG TGRLARVYNK L //