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Reviewed, UniProtKB/Swiss-Prot P37753 (MANC9_ECOLX)

Last modified September 22, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mannose-1-phosphate guanylyltransferase
    EC=2.7.7.13
Alternative name(s):
    GDP-mannose pyrophosphorylase
      Short name=GMPP
      Short name=GMP
Gene names
Name: manC
Synonyms: rfbM, rfbM1
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS O9 antigen.

Catalytic activity

GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.

Pathway

Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.

Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.

Miscellaneous

There are two duplicated genes for manB and manC in this E.coli strain.

Sequence similarities

Belongs to the mannose-6-phosphate isomerase type 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Mannose-1-phosphate guanylyltransferase
PRO_0000194259

Natural variations

Natural variant1611V → L

Sequences

Sequence LengthMass (Da)Tools
P37753-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: F3A8394550384F79

FASTA47152,628
        10         20         30         40         50         60 
MLLPVIMAGG TGSRLWPMSR ELYPKQFLRL FGQNSMLQET ITRLSGLEVH EPMVICNEEH 

        70         80         90        100        110        120 
RFLVAEQLRQ LNKLSSNIIL EPVGRNTAPA IALAALQATR HGDDPLMLVL AADHIINNQP 

       130        140        150        160        170        180 
VFHDAIRVAE QYADEGHLVT FGIVPNAPET GYGYIQRGVA VTDSAHTPYQ VARFVEKPDR 

       190        200        210        220        230        240 
ERAGAYLASG EYYWNSGMFM FRAKKYLSEL AKFRPDILEA CQAAVNAADN GSDFISIPHD 

       250        260        270        280        290        300 
IFCECPDESV DYAVMEKTAD AVVVGLDADW SDVGSWSALW EVSPKDGQGN VLSGDAWVHN 

       310        320        330        340        350        360 
SENCYINSDE KLVAAIGVEN LVIVSTKDAV LVMNRERSQD VKKAVEFLKQ NQRTEYKRHR 

       370        380        390        400        410        420 
EIYRPWGRCD VVVQTPRFNV NRITVKPGGA FSMQMHHHRA EHWVILAGTG QVTVNGKQFL 

       430        440        450        460        470 
LSENQSTFIP IGAEHCLENP GCIPLEVLEI QSGSYLGEDD IIRIKDQYGR C 

« Hide

References

[1]"Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli O9:K30 and participation of rfb genes in the synthesis of the group I K30 capsular polysaccharide."
Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., Whitfield C.
J. Bacteriol. 176:3126-3139(1994) [PubMed: 7515042] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O9:K30:H12 / E69.
[2]"Bacterial polysaccharide synthesis and gene nomenclature."
Reeves P.R., Hobbs M., Valvano M.A., Skurnik M., Whitfield C., Coplin D., Kido N., Klena J., Maskell D., Raetz C.R.H., Rick P.D.
Trends Microbiol. 4:495-503(1996) [PubMed: 9004408] [Abstract]
Cited for: GENE NAME.

Cross-references

Sequence databases

L27632 Genomic DNA. Translation: AAA21139.1.
L27646 Genomic DNA. Translation: AAA21137.1.
PIRI41251.
I84556.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.7.22. 246.

Family and domain databases

InterProIPR006375. Man1P_GuaTrfase/Man6P_Isoase.
IPR001538. Man6P_isomerase-2_C.
IPR005835. NTP_transferase.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
PfamPF01050. MannoseP_isomer. 1 hit.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
ProDomPD002664. Man6P_isomerII. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01479. GMP_PMI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANC9_ECOLX
AccessionPrimary (citable) accession number: P37753
Secondary accession number(s): P82273
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: September 22, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents