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UniProtKB/Swiss-Prot entry P24174


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MANC_ECOLI
Primary accession number P24174
Secondary accession number P78084
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on July 19, 2003 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 77)
Name and origin of the protein
Protein name Mannose-1-phosphate guanylyltransferase
Synonyms EC 2.7.7.13
GDP-mannose pyrophosphorylase
GMPP
GMP
Gene name
Name: manC
Synonyms: cpsB, rfbM
OrderedLocusNames: b2049, JW2034
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=7815923 [NCBI, ExPASy, EBI, Israel, Japan]
Aoyama K., Haase A.M., Reeves P.R.;
"Evidence for effect of random genetic drift on G+C content after lateral transfer of fucose pathway genes to Escherichia coli K-12.";
Mol. Biol. Evol. 11:829-838(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8759852 [NCBI, ExPASy, EBI, Israel, Japan]
Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R.;
"Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid.";
J. Bacteriol. 178:4885-4893(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 327-478.
Tal R., Eichinger G., Emerick A., Wong H.C.;
"The nucleotide sequence of the phosphoglucomutase gene in E. coli.";
Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U38473; AAC77846.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75110.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15905.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77127; AAA02893.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H64970; H64970.
RefSeq AP_002649.1; -.
NP_416553.1; -.
3D structure databases
ModBase P24174.
Enzyme and pathway databases
BioCyc EcoCyc:MANNPGUANYLTRANGDP-MON; -.
MetaCyc:MANNPGUANYLTRANGDP-MON; -.
Organism-specific databases
EchoBASE EB0159; -.
EcoGene EG10161; manC.
Ontologies
GO
GO:0004475; Molecular function: mannose-1-phosphate guanylyltransferase activity (inferred from electronic annotation from EC).
GO:0009103; Biological process: lipopolysaccharide biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006375; Man1P_GuanlTrfase/Man6P_Isoase.
IPR001538; Man6P_isomerase-2_C.
IPR005835; NTP_transferase.
IPR014710; RmlC-like_jellyroll.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
Pfam PF01050; MannoseP_isomer; 1.
PF00483; NTP_transferase; 1.
Pfam graphical view of domain structure.
ProDom PD002664; Man6P_isomerII; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01479; GMP_PMI; 1.
BLOCKS P24174.
ProtoNet P24174.
Genome annotation databases
GeneID 946580; -.
GenomeReviews U00096_GR; b2049.
AP009048_GR; JW2034.
KEGG ecj:JW2034; -.
eco:b2049; -.
Phylogenomic databases
HOGENOM P24174; -.
Genome annotation databases
CMR P24174; b2049.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Capsule biogenesis/degradation; Complete proteome; Lipopolysaccharide biosynthesis; Nucleotidyltransferase; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   478  478     Mannose-1-phosphate guanylyltransferase. PRO_0000194253
CONFLICT   325   325        V -> L (in Ref. 1 and 2). 
Sequence information
Length: 478 AA [This is the length of the unprocessed precursor] Molecular weight: 53016 Da [This is the MW of the unprocessed precursor] CRC64: 675C0EEA050B4186 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQSKLYPVV MAGGSGSRLW PLSRVLYPKQ FLCLKGDLTM LQTTICRLNG VECESPVVIC 

        70         80         90        100        110        120 
NEQHRFIVAE QLRQLNKLTE NIILEPAGRN TAPAIALAAL AAKRHSPESD PLMLVLAADH 

       130        140        150        160        170        180 
VIADEDAFRA AVRNAMPYAE AGKLVTFGIV PDLPETGYGY IRRGEVSAGE QDMVAFEVAQ 

       190        200        210        220        230        240 
FVEKPNLETA QAYVASGEYY WNSGMFLFRA GRYLEELKKY RPDILDACEK AMSAVDPDLN 

       250        260        270        280        290        300 
FIRVDEEAFL ACPEESVDYA VMERTADAVV VPMDAGWSDV GSWSSLWEIS AHTAEGNVCH 

       310        320        330        340        350        360 
GDVINHKTEN SYVYAESGLV TTVGVKDLVV VQTKDAVLIA DRNAVQDVKK VVEQIKADGR 

       370        380        390        400        410        420 
HEHRVHREVY RPWGKYDSID AGDRYQVKRI TVKPGEGLSV QMHHHRAEHW VVVAGTAKVT 

       430        440        450        460        470 
IDGDIKLLGE NESIYIPLGA THCLENPGKI PLDLIEVRSG SYLEEDDVVR FADRYGRV 

P24174 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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