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Protein

dTDP-glucose 4,6-dehydratase

Gene

rfbB

Organism
Xanthomonas campestris pv. campestris (strain B100)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction.By similarity

Catalytic activityi

dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O.By similarity

Cofactori

NAD+By similarityNote: Binds 1 NAD+ per subunit.By similarity

Pathwayi: dTDP-L-rhamnose biosynthesis

This protein is involved in the pathway dTDP-L-rhamnose biosynthesis, which is part of Carbohydrate biosynthesis.By similarity
View all proteins of this organism that are known to be involved in the pathway dTDP-L-rhamnose biosynthesis and in Carbohydrate biosynthesis.

Pathwayi: LPS O-antigen biosynthesis

This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.By similarity
View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei84Substrate; via carbonyl oxygenBy similarity1
Binding sitei99NADBy similarity1
Binding sitei133SubstrateBy similarity1
Active sitei134Proton donorBy similarity1
Active sitei135Proton acceptorBy similarity1
Active sitei158Proton acceptorBy similarity1
Binding sitei187SubstrateBy similarity1
Binding sitei188NAD; via amide nitrogenBy similarity1
Binding sitei222SubstrateBy similarity1
Binding sitei257SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 13NADBy similarity2
Nucleotide bindingi32 – 35NADBy similarity4
Nucleotide bindingi58 – 59NADBy similarity2
Nucleotide bindingi80 – 84NADBy similarity5
Nucleotide bindingi158 – 162NADBy similarity5

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processLipopolysaccharide biosynthesis
LigandNAD

Enzyme and pathway databases

UniPathwayi
UPA00124

UPA00281

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydrataseBy similarity (EC:4.2.1.46By similarity)
Gene namesi
Name:rfbB
Synonyms:rmlB
Ordered Locus Names:xcc-b100_3734
OrganismiXanthomonas campestris pv. campestris (strain B100)
Taxonomic identifieri509169 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
Proteomesi
  • UP000001188 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003331841 – 351dTDP-glucose 4,6-dehydrataseAdd BLAST351

Proteomic databases

PRIDEiB0RVL0

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliB0RVL0
SMRiB0RVL0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni197 – 198Substrate bindingBy similarity2
Regioni213 – 215Substrate bindingBy similarity3
Regioni289 – 293Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.By similarity

Phylogenomic databases

KOiK01710
OMAiEWCQHVQ

Family and domain databases

InterProiView protein in InterPro
IPR005888 dTDP_Gluc_deHydtase
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01181 dTDP_gluc_dehyt, 1 hit

Sequencei

Sequence statusi: Complete.

B0RVL0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATWLVTGGA GFIGGNFVLE AVSRGIRVVN LDALTYAGNL NTLASLEGNA
60 70 80 90 100
DHIFVKGDIG DGALVTRLLQ EHQPDAVLNF AAESHVDRSI EGPGAFIQTN
110 120 130 140 150
VVGTLALLEA VRDYWKALPD TRRDAFRFLH VSTDEVYGTL GETGKFTETT
160 170 180 190 200
PYAPNSPYSA SKAASDHLVR AFHHTYGLPV LTTNCSNNYG PYHFPEKLIP
210 220 230 240 250
LVIAKALAGE PLPVYGDGKQ VRDWLFVSDH CEAIRTVLAK GRVGETYNVG
260 270 280 290 300
GNSERQNIEV VQAICALLDQ HRPREDGKPR ESQIAYVTDR PGHDRRYAID
310 320 330 340 350
ASKLKDELGW EPAYTFEQGI ALTVDWYLTN QTWVQGVLDG SYRLERIGAT

V
Length:351
Mass (Da):38,558
Last modified:April 8, 2008 - v1
Checksum:iF1B393B1A2EA0F3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF204145 Genomic DNA Translation: AAK53466.1
AM920689 Genomic DNA Translation: CAP53101.1

Genome annotation databases

EnsemblBacteriaiCAP53101; CAP53101; xcc-b100_3734
KEGGixca:xcc-b100_3734

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF204145 Genomic DNA Translation: AAK53466.1
AM920689 Genomic DNA Translation: CAP53101.1

3D structure databases

ProteinModelPortaliB0RVL0
SMRiB0RVL0
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB0RVL0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAP53101; CAP53101; xcc-b100_3734
KEGGixca:xcc-b100_3734

Phylogenomic databases

KOiK01710
OMAiEWCQHVQ

Enzyme and pathway databases

UniPathwayi
UPA00124

UPA00281

Family and domain databases

InterProiView protein in InterPro
IPR005888 dTDP_Gluc_deHydtase
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01181 dTDP_gluc_dehyt, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRMLB_XANCB
AccessioniPrimary (citable) accession number: B0RVL0
Secondary accession number(s): P55295
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: May 23, 2018
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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