ID   MANA_ECOLI              Reviewed;         391 AA.
AC   P00946;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   10-JUN-2026, entry version 197.
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=b1613, JW1605;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=6397402; DOI=10.1016/0378-1119(84)90030-1;
RA   Miles J.S., Guest J.R.;
RT   "Nucleotide sequence and transcriptional start point of the phosphomannose
RT   isomerase gene (manA) of Escherichia coli.";
RL   Gene 32:41-48(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 378-391.
RC   STRAIN=K12 / EMG2;
RA   Robison K., O'Keeffe T., Church G.M.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
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   -!- INTERACTION:
CC       P00946; P18196: minC; NbExp=5; IntAct=EBI-554045, EBI-554060;
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; M15380; AAA24109.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74685.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15361.1; -; Genomic_DNA.
DR   EMBL; U35067; AAA79050.1; -; Genomic_DNA.
DR   PIR; A01172; ISECMP.
DR   RefSeq; NP_416130.3; NC_000913.3.
DR   RefSeq; WP_001170664.1; NZ_CP009789.1.
DR   AlphaFoldDB; P00946; -.
DR   SMR; P00946; -.
DR   BioGRID; 4260255; 328.
DR   BioGRID; 849240; 1.
DR   DIP; DIP-10153N; -.
DR   FunCoup; P00946; 746.
DR   IntAct; P00946; 19.
DR   STRING; 511145.b1613; -.
DR   BindingDB; P00946; -.
DR   ChEMBL; CHEMBL3309019; -.
DR   iPTMnet; P00946; -.
DR   jPOST; P00946; -.
DR   PaxDb; 511145-b1613; -.
DR   EnsemblBacteria; AAC74685; AAC74685; b1613.
DR   GeneID; 75204457; -.
DR   GeneID; 944840; -.
DR   KEGG; ecj:JW1605; -.
DR   KEGG; eco:b1613; -.
DR   KEGG; ecoc:C3026_09280; -.
DR   PATRIC; fig|1411691.4.peg.649; -.
DR   EchoBASE; EB0561; -.
DR   eggNOG; COG1482; Bacteria.
DR   HOGENOM; CLU_026967_1_0_6; -.
DR   InParanoid; P00946; -.
DR   OMA; DIGLFCG; -.
DR   OrthoDB; 9792649at2; -.
DR   PhylomeDB; P00946; -.
DR   BioCyc; EcoCyc:MANNPISOM-MONOMER; -.
DR   BioCyc; MetaCyc:MANNPISOM-MONOMER; -.
DR   BRENDA; 5.3.1.8; 2026.
DR   PRO; PR:P00946; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P00946; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IDA:EcoCyc.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009242; P:colanic acid biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0019309; P:mannose catabolic process; IMP:EcoCyc.
DR   CDD; cd07011; cupin_PMI_type_I_N; 1.
DR   FunFam; 2.60.120.10:FF:000076; Mannose-6-phosphate isomerase; 1.
DR   FunFam; 2.60.120.10:FF:000030; Mannose-6-phosphate isomerase ManA; 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   NCBIfam; NF011710; PRK15131.1; 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   Acetylation; Cytoplasm; Isomerase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..391
FT                   /note="Mannose-6-phosphate isomerase"
FT                   /id="PRO_0000194230"
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   MOD_RES         280
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
SQ   SEQUENCE   391 AA;  42850 MW;  669737512CADBCCD CRC64;
     MQKLINSVQN YAWGSKTALT ELYGMENPSS QPMAELWMGA HPKSSSRVQN AAGDIVSLRD
     VIESDKSTLL GEAVAKRFGE LPFLFKVLCA AQPLSIQVHP NKHNSEIGFA KENAAGIPMD
     AAERNYKDPN HKPELVFALT PFLAMNAFRE FSEIVSLLQP VAGAHPAIAH FLQQPDAERL
     SELFASLLNM QGEEKSRALA ILKSALDSQQ GEPWQTIRLI SEFYPEDSGL FSPLLLNVVK
     LNPGEAMFLF AETPHAYLQG VALEVMANSD NVLRAGLTPK YIDIPELVAN VKFEAKPANQ
     LLTQPVKQGA ELDFPIPVDD FAFSLHDLSD KETTISQQSA AILFCVEGDA TLWKGSQQLQ
     LKPGESAFIA ANESPVTVKG HGRLARVYNK L
//