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B0RVK6 (XANB_XANCB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xanthan biosynthesis protein XanB

Including the following 2 domains:

  1. Mannose-6-phosphate isomerase
    EC=5.3.1.8
    Alternative name(s):
    Phosphohexomutase
    Phosphomannose isomerase
    Short name=PMI
  2. Mannose-1-phosphate guanylyl transferase
    EC=2.7.7.13
    Alternative name(s):
    GDP-mannose pyrophosphorylase
    Short name=GMP
    Short name=GMPP
Gene names
Name:xanB
Ordered Locus Names:xcc-b100_3730
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in xanthan production.

Catalytic activity

D-mannose 6-phosphate = D-fructose 6-phosphate.

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.

Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Xanthan biosynthesis protein XanB
PRO_0000333187

Sequences

Sequence LengthMass (Da)Tools
B0RVK6 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 596DEEFFA93FC78A

FASTA46750,934
        10         20         30         40         50         60 
MSDVLPIILS GGSGTRLWPL SRETYPKQFL PLVGEHSMLQ ATWLRSAPVA AHAPIVVANE 

        70         80         90        100        110        120 
EHRFMAAEQL QQLGVKPSAI LLEPKGRNTA PAIAVAALEA TRNGGDPLLL VLPSDHVIRD 

       130        140        150        160        170        180 
EAAFQAAVTV AAAAAEQGKL VTFGIKPTAP ETGYGYIKAG AGTGATAVER FVEKPDLATA 

       190        200        210        220        230        240 
QGYLASGEYY WNSGMFLFRA SRYLEELRKF QPAIADACQK AWEGGKRDAD FTRLDKDAFA 

       250        260        270        280        290        300 
SSPSDSIDYA VMEKTADAVV VPLDAGWNDV GSWSSLLDVS EQDGQGNAHH GDVIQLDCKN 

       310        320        330        340        350        360 
TYAYGSRLIA MVGLENVVVV ETDDAVLVGH RDRIQEVKEV VSQIKSAGRS EATWHRKVYR 

       370        380        390        400        410        420 
PWGAYDSIDM GQRFQVKRIT VKPGATLSLQ MHHHRAEHWI VVSGTAEVTR GDEVLLLTEN 

       430        440        450        460 
QSTYIPLGVT HRLKNPGKLP LELIEVQSGS YLGEDDIVRF EDTYGRT 

« Hide

References

« Hide 'large scale' references
[1]"Genetics of xanthan production in Xanthomonas campestris: the xanA and xanB genes are involved in UDP-glucose and GDP-mannose biosynthesis."
Koeplin R., Arnold W., Hoette B., Simon R., Wang G., Puehler A.
J. Bacteriol. 174:191-199(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Lipopolysaccharide biosynthesis in Xanthomonas campestris pv. campestris: a cluster of 15 genes is involved in the biosynthesis of the LPS O-antigen and the LPS core."
Vorhoelter F.-J., Niehaus K., Puehler A.
Mol. Genet. Genomics 266:79-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 164.
[3]"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF204145 Genomic DNA. Translation: AAK53463.1.
AM920689 Genomic DNA. Translation: CAP53097.1.
PIRB43304.
RefSeqYP_001905135.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RVK6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509169.xccb100_3730.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP53097; CAP53097; xcc-b100_3730.
GeneID6325210.
KEGGxca:xccb100_3730.
PATRIC24087412. VBIXanCam108527_3767.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0662.
KOK16011.
OMAIYAACEQ.
OrthoDBEOG6X3W6T.
ProtClustDBCLSK445961.

Enzyme and pathway databases

BioCycXCAM509169:GHW4-3816-MONOMER.
UniPathwayUPA00126; UER00423.
UPA00126; UER00930.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR006375. Man1P_GuaTrfase/Man6P_Isoase.
IPR001538. Man6P_isomerase-2_C.
IPR005835. NTP_transferase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF01050. MannoseP_isomer. 1 hit.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
TIGRFAMsTIGR01479. GMP_PMI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXANB_XANCB
AccessionPrimary (citable) accession number: B0RVK6
Secondary accession number(s): P29956, Q93S98
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: November 13, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways