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Protein

dTDP-glucose 4,6-dehydratase

Gene

rffG

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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.

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.
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.
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 sitei81NAD; via carbonyl oxygenBy similarity1
Binding sitei85Substrate; via carbonyl oxygenBy similarity1
Binding sitei100NADBy similarity1
Active sitei135Proton donorBy similarity1
Active sitei136Proton acceptorBy similarity1
Active sitei160Proton acceptorBy similarity1
Binding sitei189SubstrateBy similarity1
Binding sitei190NAD; via amide nitrogenBy similarity1
Binding sitei224SubstrateBy similarity1
Binding sitei259SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi8 – 14NADSequence analysis7
Nucleotide bindingi33 – 36NADBy similarity4
Nucleotide bindingi59 – 60NADBy similarity2
Nucleotide bindingi160 – 164NADBy similarity5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00124.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydratase (EC:4.2.1.46)
Gene namesi
Name:rffG
Ordered Locus Names:HI_0873
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001832371 – 338dTDP-glucose 4,6-dehydrataseAdd BLAST338

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi71421.HI0873.

Structurei

3D structure databases

ProteinModelPortaliP44914.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni134 – 136Substrate bindingBy similarity3
Regioni199 – 200Substrate bindingBy similarity2
Regioni215 – 217Substrate bindingBy similarity3
Regioni294 – 297Substrate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
KOiK01710.
OMAiHNDNSLH.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.

Sequencei

Sequence statusi: Complete.

P44914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMNILVTGGS GFIGSALIRY IINHTQDFVI NIDKLTYAAN QSALREVENN
60 70 80 90 100
PRYVFEKVDI CDLNVIENIF EKYQPDAVMH LAAESHVDRS ISGAADFVQT
110 120 130 140 150
NIVGTYTLLE VAKNYWHTLD EAKKTTFRFH HISTDEVYGD LSLSEPAFTE
160 170 180 190 200
QSPYHPSSPY SASKAASNHL VQAWHRTYGL PVIITNSSNN YGAYQHAEKL
210 220 230 240 250
IPLMISNAVM GKPLPIYGDG QQIRDWLFVE DHVQASYLVL TKGRVGENYN
260 270 280 290 300
IGGNCEKTNL EVVKRICQLL EELAPSKPNH IKYYEDLMTF VKDRPGHDVR
310 320 330
YSLDCSKIHA ELGWQPQITF EQGLRQTVKW YLFNSSSS
Length:338
Mass (Da):38,329
Last modified:November 1, 1995 - v1
Checksum:iB44BCC29D6C7D04B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22531.1.
PIRiC64099.
RefSeqiNP_439034.2. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22531; AAC22531; HI_0873.
GeneIDi949510.
KEGGihin:HI0873.
PATRICi20190401. VBIHaeInf48452_0914.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22531.1.
PIRiC64099.
RefSeqiNP_439034.2. NC_000907.1.

3D structure databases

ProteinModelPortaliP44914.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22531; AAC22531; HI_0873.
GeneIDi949510.
KEGGihin:HI0873.
PATRICi20190401. VBIHaeInf48452_0914.

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
KOiK01710.
OMAiHNDNSLH.

Enzyme and pathway databases

UniPathwayiUPA00124.
UPA00281.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRMLB_HAEIN
AccessioniPrimary (citable) accession number: P44914
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 5, 2016
This is version 106 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

Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.