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P26391

- RMLB_SALTY

UniProt

P26391 - RMLB_SALTY

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Protein
dTDP-glucose 4,6-dehydratase
Gene
rfbB, STM2097
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O.1 Publication

Cofactori

Binds 1 NAD per subunit.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801NAD; via carbonyl oxygen
Binding sitei84 – 841Substrate; via carbonyl oxygen
Binding sitei99 – 991NAD
Active sitei134 – 1341Proton donor1 Publication
Active sitei135 – 1351Proton acceptor1 Publication
Active sitei167 – 1671Proton acceptor1 Publication
Binding sitei196 – 1961Substrate
Binding sitei197 – 1971NAD; via amide nitrogen
Binding sitei231 – 2311Substrate
Binding sitei266 – 2661Substrate
Binding sitei357 – 3571Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 123NAD
Nucleotide bindingi32 – 354NAD
Nucleotide bindingi58 – 592NAD
Nucleotide bindingi167 – 1715NAD

GO - Molecular functioni

  1. NADH binding Source: UniProtKB
  2. dTDP-glucose 4,6-dehydratase activity Source: UniProtKB

GO - Biological processi

  1. O antigen biosynthetic process Source: UniProtKB-UniPathway
  2. dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
  3. extracellular polysaccharide biosynthetic process Source: UniProtKB
  4. lipopolysaccharide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2109-MONOMER.
UniPathwayiUPA00124.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydratase (EC:4.2.1.46)
Gene namesi
Name:rfbB
Ordered Locus Names:STM2097
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361dTDP-glucose 4,6-dehydratase
PRO_0000183243Add
BLAST

Proteomic databases

PaxDbiP26391.
PRIDEiP26391.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi99287.STM2097.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76
Helixi11 – 2313
Beta strandi27 – 326
Helixi40 – 434
Turni44 – 485
Beta strandi52 – 565
Helixi62 – 7211
Beta strandi75 – 795
Helixi86 – 916
Helixi94 – 1007
Helixi102 – 11615
Helixi120 – 1256
Beta strandi127 – 1337
Helixi134 – 1374
Helixi143 – 1453
Helixi166 – 18520
Beta strandi189 – 1946
Beta strandi196 – 1994
Helixi207 – 21711
Beta strandi221 – 2244
Beta strandi230 – 2356
Helixi236 – 24914
Beta strandi255 – 2584
Beta strandi263 – 2653
Helixi266 – 28015
Helixi287 – 2904
Beta strandi291 – 2944
Helixi309 – 3157
Helixi323 – 33614
Helixi338 – 3436
Helixi347 – 35711

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G1AX-ray2.47A/B/C/D1-361[»]
1KEUX-ray2.40A/B1-361[»]
1KEWX-ray1.80A/B1-361[»]
ProteinModelPortaliP26391.
SMRiP26391. Positions 1-361.

Miscellaneous databases

EvolutionaryTraceiP26391.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 1353Substrate binding
Regioni206 – 2072Substrate binding
Regioni222 – 2243Substrate binding
Regioni297 – 3004Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1088.
HOGENOMiHOG000168006.
KOiK01710.
OMAiDSERYAF.
OrthoDBiEOG6PZXCX.
PhylomeDBiP26391.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.

Sequencei

Sequence statusi: Complete.

P26391-1 [UniParc]FASTAAdd to Basket

« Hide

MKILITGGAG FIGSAVVRHI IKNTQDTVVN IDKLTYAGNL ESLSDISESN    50
RYNFEHADIC DSAEITRIFE QYQPDAVMHL AAESHVDRSI TGPAAFIETN 100
IVGTYALLEV ARKYWSALGE DKKNNFRFHH ISTDEVYGDL PHPDEVENSV 150
TLPLFTETTA YAPSSPYSAS KASSDHLVRA WRRTYGLPTI VTNCSNNYGP 200
YHFPEKLIPL VILNALEGKP LPIYGKGDQI RDWLYVEDHA RALHMVVTEG 250
KAGETYNIGG HNEKKNLDVV FTICDLLDEI VPKATSYREQ ITYVADRPGH 300
DRRYAIDAGK ISRELGWKPL ETFESGIRKT VEWYLANTQW VNNVKSGAYQ 350
SWIEQNYEGR Q 361
Length:361
Mass (Da):40,719
Last modified:August 1, 1992 - v1
Checksum:i3A574B4D917EBC57
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56793 Genomic DNA. Translation: CAA40115.1.
AE006468 Genomic DNA. Translation: AAL21001.1.
PIRiS15299.
RefSeqiNP_461042.1. NC_003197.1.
WP_000697840.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21001; AAL21001; STM2097.
GeneIDi1253618.
KEGGistm:STM2097.
PATRICi32382777. VBISalEnt20916_2219.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56793 Genomic DNA. Translation: CAA40115.1 .
AE006468 Genomic DNA. Translation: AAL21001.1 .
PIRi S15299.
RefSeqi NP_461042.1. NC_003197.1.
WP_000697840.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G1A X-ray 2.47 A/B/C/D 1-361 [» ]
1KEU X-ray 2.40 A/B 1-361 [» ]
1KEW X-ray 1.80 A/B 1-361 [» ]
ProteinModelPortali P26391.
SMRi P26391. Positions 1-361.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM2097.

Proteomic databases

PaxDbi P26391.
PRIDEi P26391.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL21001 ; AAL21001 ; STM2097 .
GeneIDi 1253618.
KEGGi stm:STM2097.
PATRICi 32382777. VBISalEnt20916_2219.

Phylogenomic databases

eggNOGi COG1088.
HOGENOMi HOG000168006.
KOi K01710.
OMAi DSERYAF.
OrthoDBi EOG6PZXCX.
PhylomeDBi P26391.

Enzyme and pathway databases

UniPathwayi UPA00124 .
UPA00281 .
BioCyci SENT99287:GCTI-2109-MONOMER.

Miscellaneous databases

EvolutionaryTracei P26391.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR005888. dTDP_Gluc_deHydtase.
IPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR10366:SF41. PTHR10366:SF41. 1 hit.
Pfami PF01370. Epimerase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01181. dTDP_gluc_dehyt. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) IN COMPLEX WITH NAD, COFACTOR, SUBUNIT.
  4. 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.

Entry informationi

Entry nameiRMLB_SALTY
AccessioniPrimary (citable) accession number: P26391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 3, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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