MANC_ECOLI
ID MANC_ECOLI Reviewed; 478 AA.
AC P24174; P78084;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Mannose-1-phosphate guanylyltransferase;
DE EC=2.7.7.13;
DE AltName: Full=GDP-mannose pyrophosphorylase;
DE Short=GMP;
DE Short=GMPP;
GN Name=manC; Synonyms=cpsB, rfbM; OrderedLocusNames=b2049, JW2034;
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=7815923; DOI=10.1093/oxfordjournals.molbev.a040166;
RA Aoyama K., Haase A.M., Reeves P.R.;
RT "Evidence for effect of random genetic drift on G+C content after lateral
RT transfer of fucose pathway genes to Escherichia coli K-12.";
RL Mol. Biol. Evol. 11:829-838(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8759852; DOI=10.1128/jb.178.16.4885-4893.1996;
RA Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R.;
RT "Organization of the Escherichia coli K-12 gene cluster responsible for
RT production of the extracellular polysaccharide colanic acid.";
RL J. Bacteriol. 178:4885-4893(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 327-478.
RA Tal R., Eichinger G., Emerick A., Wong H.C.;
RT "The nucleotide sequence of the phosphoglucomutase gene in E. coli.";
RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of the capsular polysaccharide
CC colanic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58409; EC=2.7.7.13;
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC route): step 1/1.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC {ECO:0000305}.
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DR EMBL; U38473; AAC77846.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75110.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15905.1; -; Genomic_DNA.
DR EMBL; M77127; AAA02893.1; -; Genomic_DNA.
DR PIR; H64970; H64970.
DR RefSeq; NP_416553.1; NC_000913.3.
DR RefSeq; WP_000079274.1; NZ_LN832404.1.
DR AlphaFoldDB; P24174; -.
DR SMR; P24174; -.
DR BioGRID; 4263312; 190.
DR IntAct; P24174; 5.
DR STRING; 511145.b2049; -.
DR PaxDb; P24174; -.
DR PRIDE; P24174; -.
DR EnsemblBacteria; AAC75110; AAC75110; b2049.
DR EnsemblBacteria; BAA15905; BAA15905; BAA15905.
DR GeneID; 946580; -.
DR KEGG; ecj:JW2034; -.
DR KEGG; eco:b2049; -.
DR PATRIC; fig|1411691.4.peg.202; -.
DR EchoBASE; EB0159; -.
DR eggNOG; COG0662; Bacteria.
DR eggNOG; COG0836; Bacteria.
DR HOGENOM; CLU_035527_1_0_6; -.
DR InParanoid; P24174; -.
DR OMA; LIVCNEK; -.
DR PhylomeDB; P24174; -.
DR BioCyc; EcoCyc:MANNPGUANYLTRANGDP-MON; -.
DR BioCyc; MetaCyc:MANNPGUANYLTRANGDP-MON; -.
DR UniPathway; UPA00126; UER00930.
DR PRO; PR:P24174; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0009242; P:colanic acid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IEP:EcoCyc.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR006375; Man1P_GuaTrfase/Man6P_Isoase.
DR InterPro; IPR001538; Man6P_isomerase-2_C.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF01050; MannoseP_isomer; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01479; GMP_PMI; 1.
PE 3: Inferred from homology;
KW Capsule biogenesis/degradation; GTP-binding;
KW Lipopolysaccharide biosynthesis; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..478
FT /note="Mannose-1-phosphate guanylyltransferase"
FT /id="PRO_0000194253"
FT CONFLICT 325
FT /note="V -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 53016 MW; 675C0EEA050B4186 CRC64;
MAQSKLYPVV MAGGSGSRLW PLSRVLYPKQ FLCLKGDLTM LQTTICRLNG VECESPVVIC
NEQHRFIVAE QLRQLNKLTE NIILEPAGRN TAPAIALAAL AAKRHSPESD PLMLVLAADH
VIADEDAFRA AVRNAMPYAE AGKLVTFGIV PDLPETGYGY IRRGEVSAGE QDMVAFEVAQ
FVEKPNLETA QAYVASGEYY WNSGMFLFRA GRYLEELKKY RPDILDACEK AMSAVDPDLN
FIRVDEEAFL ACPEESVDYA VMERTADAVV VPMDAGWSDV GSWSSLWEIS AHTAEGNVCH
GDVINHKTEN SYVYAESGLV TTVGVKDLVV VQTKDAVLIA DRNAVQDVKK VVEQIKADGR
HEHRVHREVY RPWGKYDSID AGDRYQVKRI TVKPGEGLSV QMHHHRAEHW VVVAGTAKVT
IDGDIKLLGE NESIYIPLGA THCLENPGKI PLDLIEVRSG SYLEEDDVVR FADRYGRV
