MANA_ECOLI
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 03-AUG-2022, entry version 184.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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_SSZK01000001.1.
DR AlphaFoldDB; P00946; -.
DR SMR; P00946; -.
DR BioGRID; 4260255; 312.
DR BioGRID; 849240; 1.
DR DIP; DIP-10153N; -.
DR IntAct; P00946; 19.
DR STRING; 511145.b1613; -.
DR BindingDB; P00946; -.
DR ChEMBL; CHEMBL3309019; -.
DR iPTMnet; P00946; -.
DR SWISS-2DPAGE; P00946; -.
DR jPOST; P00946; -.
DR PaxDb; P00946; -.
DR PRIDE; P00946; -.
DR EnsemblBacteria; AAC74685; AAC74685; b1613.
DR EnsemblBacteria; BAA15361; BAA15361; BAA15361.
DR GeneID; 944840; -.
DR KEGG; ecj:JW1605; -.
DR KEGG; eco:b1613; -.
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 PhylomeDB; P00946; -.
DR BioCyc; EcoCyc:MANNPISOM-MON; -.
DR BioCyc; MetaCyc:MANNPISOM-MON; -.
DR BRENDA; 5.3.1.8; 2026.
DR PRO; PR:P00946; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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 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 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
