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P26391 (RMLB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
dTDP-glucose 4,6-dehydratase
EC=4.2.1.46
Gene names
Name:rfbB
Ordered Locus Names:STM2097
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

dTDP-glucose = dTDP-4-dehydro-6-deoxy-D-glucose + H2O. Ref.4

Cofactor

Binds 1 NAD ion per monomer. Ref.3 Ref.4

Pathway

Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.

Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.

Subunit structure

Homodimer. Ref.3 Ref.4

Sequence similarities

Belongs to the sugar epimerase family. dTDP-glucose dehydratase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361dTDP-glucose 4,6-dehydratase
PRO_0000183243

Regions

Nucleotide binding10 – 123NAD
Nucleotide binding32 – 354NAD
Nucleotide binding58 – 592NAD
Nucleotide binding167 – 1715NAD
Region133 – 1353Substrate binding
Region206 – 2072Substrate binding
Region222 – 2243Substrate binding
Region297 – 3004Substrate binding

Sites

Active site1341Proton donor Ref.4
Active site1351Proton acceptor Ref.4
Active site1671Proton acceptor Ref.4
Binding site801NAD; via carbonyl oxygen
Binding site841Substrate; via carbonyl oxygen
Binding site991NAD
Binding site1961Substrate
Binding site1971NAD; via amide nitrogen
Binding site2311Substrate
Binding site2661Substrate
Binding site3571Substrate

Secondary structure

1 ........................................................... 361
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26391 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 3A574B4D917EBC57

FASTA36140,719
        10         20         30         40         50         60 
MKILITGGAG FIGSAVVRHI IKNTQDTVVN IDKLTYAGNL ESLSDISESN RYNFEHADIC 

        70         80         90        100        110        120 
DSAEITRIFE QYQPDAVMHL AAESHVDRSI TGPAAFIETN IVGTYALLEV ARKYWSALGE 

       130        140        150        160        170        180 
DKKNNFRFHH ISTDEVYGDL PHPDEVENSV TLPLFTETTA YAPSSPYSAS KASSDHLVRA 

       190        200        210        220        230        240 
WRRTYGLPTI VTNCSNNYGP YHFPEKLIPL VILNALEGKP LPIYGKGDQI RDWLYVEDHA 

       250        260        270        280        290        300 
RALHMVVTEG KAGETYNIGG HNEKKNLDVV FTICDLLDEI VPKATSYREQ ITYVADRPGH 

       310        320        330        340        350        360 
DRRYAIDAGK ISRELGWKPL ETFESGIRKT VEWYLANTQW VNNVKSGAYQ SWIEQNYEGR 


Q

« Hide

References

« Hide 'large scale' references
[1]"Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2)."
Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.
Mol. Microbiol. 5:695-713(1991) [PubMed: 1710759] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"The crystal structure of dTDP-D-Glucose 4,6-dehydratase (RmlB) from Salmonella enterica serovar Typhimurium, the second enzyme in the dTDP-l-rhamnose pathway."
Allard S.T., Giraud M.F., Whitfield C., Graninger M., Messner P., Naismith J.H.
J. Mol. Biol. 307:283-295(2001) [PubMed: 11243820] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) IN COMPLEX WITH NAD, COFACTOR, SUBUNIT.
[4]"Toward a structural understanding of the dehydratase mechanism."
Allard S.T., Beis K., Giraud M.-F., Hegeman A.D., Gross J.W., Wilmouth R.C., Whitfield C., Graninger M., Messner P., Allen A.G., Maskell D.J., Naismith J.H.
Structure 10:81-92(2002) [PubMed: 11796113] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD, FUNCTION AS A DEHYDRATASE, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, REACTION MECHANISM, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X56793 Genomic DNA. Translation: CAA40115.1.
AE006468 Genomic DNA. Translation: AAL21001.1.
PIRS15299.
RefSeqNP_461042.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G1AX-ray2.47A/B/C/D1-361[»]
1KEUX-ray2.40A/B1-361[»]
1KEWX-ray1.80A/B1-361[»]
ProteinModelPortalP26391.
SMRP26391. Positions 1-361.
ModBaseSearch...

Proteomic databases

PRIDEP26391.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1253618.
GenomeReviewsGene locus STM2097 in contig AE006468_GR.
KEGGstm:STM2097.
NMPDRfig|99287.1.peg.2022.
PATRIC32382777. VBISalEnt20916_2219.

Phylogenomic databases

HOGENOMHBG755066.
OMAWSALDGD.
ProtClustDBPRK10084.

Enzyme and pathway databases

BioCycSTYP99287:STM2097-MONOMER.

Family and domain databases

InterProIPR005888. dTDP_Gluc_deHydtase.
IPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK01710.
PANTHERPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01181. DTDP_gluc_dehyt. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRMLB_SALTY
AccessionPrimary (citable) accession number: P26391
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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