MANA_SALTY
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 03-AUG-2022, entry version 149.
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; Proteobacteria; 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}.
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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; P25081; -.
DR EnsemblBacteria; AAL20387; AAL20387; 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-MON; -.
DR BRENDA; 5.3.1.8; 5542.
DR EvolutionaryTrace; P25081; -.
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 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 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
