Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P26391

- RMLB_SALTY

UniProt

P26391 - RMLB_SALTY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

dTDP-glucose 4,6-dehydratase

Gene

rfbB

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

NAD(+)2 PublicationsNote: Binds 1 NAD(+) per subunit.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801NAD; via carbonyl oxygen2 Publications
Binding sitei84 – 841Substrate; via carbonyl oxygen1 Publication
Binding sitei99 – 991NAD2 Publications
Active sitei134 – 1341Proton donor1 Publication
Active sitei135 – 1351Proton acceptor1 Publication
Active sitei167 – 1671Proton acceptor1 Publication
Binding sitei196 – 1961Substrate1 Publication
Binding sitei197 – 1971NAD; via amide nitrogen2 Publications
Binding sitei231 – 2311Substrate1 Publication
Binding sitei266 – 2661Substrate1 Publication
Binding sitei357 – 3571Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 123NAD2 Publications
Nucleotide bindingi32 – 354NAD2 Publications
Nucleotide bindingi58 – 592NAD2 Publications
Nucleotide bindingi167 – 1715NAD2 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
  2. extracellular polysaccharide biosynthetic process Source: UniProtKB
  3. lipopolysaccharide biosynthetic process Source: UniProtKB
  4. O antigen biosynthetic process Source: UniProtKB-UniPathway
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-dehydratasePRO_0000183243Add
BLAST

Proteomic databases

PaxDbiP26391.
PRIDEiP26391.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi99287.STM2097.

Structurei

Secondary structure

1
361
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi11 – 2313Combined sources
Beta strandi27 – 326Combined sources
Helixi40 – 434Combined sources
Turni44 – 485Combined sources
Beta strandi52 – 565Combined sources
Helixi62 – 7211Combined sources
Beta strandi75 – 795Combined sources
Helixi86 – 916Combined sources
Helixi94 – 1007Combined sources
Helixi102 – 11615Combined sources
Helixi120 – 1256Combined sources
Beta strandi127 – 1337Combined sources
Helixi134 – 1374Combined sources
Helixi143 – 1453Combined sources
Helixi166 – 18520Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi196 – 1994Combined sources
Helixi207 – 21711Combined sources
Beta strandi221 – 2244Combined sources
Beta strandi230 – 2356Combined sources
Helixi236 – 24914Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi263 – 2653Combined sources
Helixi266 – 28015Combined sources
Helixi287 – 2904Combined sources
Beta strandi291 – 2944Combined sources
Helixi309 – 3157Combined sources
Helixi323 – 33614Combined sources
Helixi338 – 3436Combined sources
Helixi347 – 35711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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_N.
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

        10         20         30         40         50
MKILITGGAG FIGSAVVRHI IKNTQDTVVN IDKLTYAGNL ESLSDISESN
60 70 80 90 100
RYNFEHADIC DSAEITRIFE QYQPDAVMHL AAESHVDRSI TGPAAFIETN
110 120 130 140 150
IVGTYALLEV ARKYWSALGE DKKNNFRFHH ISTDEVYGDL PHPDEVENSV
160 170 180 190 200
TLPLFTETTA YAPSSPYSAS KASSDHLVRA WRRTYGLPTI VTNCSNNYGP
210 220 230 240 250
YHFPEKLIPL VILNALEGKP LPIYGKGDQI RDWLYVEDHA RALHMVVTEG
260 270 280 290 300
KAGETYNIGG HNEKKNLDVV FTICDLLDEI VPKATSYREQ ITYVADRPGH
310 320 330 340 350
DRRYAIDAGK ISRELGWKPL ETFESGIRKT VEWYLANTQW VNNVKSGAYQ
360
SWIEQNYEGR Q
Length:361
Mass (Da):40,719
Last modified:August 1, 1992 - v1
Checksum:i3A574B4D917EBC57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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_N.
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: November 26, 2014
This is version 114 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