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Protein

dTDP-glucose 4,6-dehydratase

Gene

rmlB

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 4 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. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage.1 Publication

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei81Substrate; via carbonyl oxygenBy similarity1
Binding sitei96NADBy similarity1
Active sitei121Proton donorBy similarity1
Active sitei122Proton acceptorBy similarity1
Active sitei147Proton acceptorBy similarity1
Binding sitei176SubstrateBy similarity1
Binding sitei177NAD; via amide nitrogenBy similarity1
Binding sitei211SubstrateBy similarity1
Binding sitei246SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 13NADSequence analysis7
Nucleotide bindingi33 – 36NADBy similarity4
Nucleotide bindingi57 – 58NADBy similarity2
Nucleotide bindingi147 – 151NADBy similarity5

GO - Molecular functioni

  • dTDP-glucose 4,6-dehydratase activity Source: UniProtKB

GO - Biological processi

  • dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
  • extracellular polysaccharide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00124.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydratase (EC:4.2.1.46)
Gene namesi
Name:rmlB
Synonyms:rfbB
Ordered Locus Names:MSMEG_1512, MSMEI_1476
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003998981 – 331dTDP-glucose 4,6-dehydrataseAdd BLAST331

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi246196.MSMEG_1512.

Structurei

3D structure databases

ProteinModelPortaliA0QSK6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni120 – 122Substrate bindingBy similarity3
Regioni186 – 187Substrate bindingBy similarity2
Regioni202 – 204Substrate bindingBy similarity3
Regioni270 – 273Substrate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
HOGENOMiHOG000168006.
KOiK01710.
OMAiYLENRAW.
OrthoDBiPOG091H044P.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

A0QSK6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLVTGGAG FIGANFVHLA LREARTSSIT VLDALTYAGS RESLAPVADR
60 70 80 90 100
IRLVQGDITD AALVGDLVAE SDAVVHFAAE THVDNALADP EPFLHSNVVG
110 120 130 140 150
TYTILEAVRR HNVRLHHVST DEVYGDLELD NPARFNETTP YNPSSPYSST
160 170 180 190 200
KAAADLLVRA WVRSYGVRAT ISNCSNNYGP YQHVEKFIPR QITNVLTGRR
210 220 230 240 250
PKLYGAGANV RDWIHVDDHN SAVWRILTDG TIGRTYLIGA ECERNNLTVM
260 270 280 290 300
RTILKLMGRD PDDFDHVTDR AGHDLRYAID PSTLQDELGW APKHTDFEAG
310 320 330
LTDTIDWYRA NESWWRPLKD TVEAKYQERG Q
Length:331
Mass (Da):36,967
Last modified:January 9, 2007 - v1
Checksum:i7DC0A0520677DDF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK70086.1.
CP001663 Genomic DNA. Translation: AFP37949.1.
RefSeqiWP_003892900.1. NZ_CP009494.1.
YP_885894.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK70086; ABK70086; MSMEG_1512.
AFP37949; AFP37949; MSMEI_1476.
GeneIDi4531259.
KEGGimsb:LJ00_07555.
msg:MSMEI_1476.
msm:MSMEG_1512.
PATRICi18075481. VBIMycSme59918_1497.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK70086.1.
CP001663 Genomic DNA. Translation: AFP37949.1.
RefSeqiWP_003892900.1. NZ_CP009494.1.
YP_885894.1. NC_008596.1.

3D structure databases

ProteinModelPortaliA0QSK6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_1512.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK70086; ABK70086; MSMEG_1512.
AFP37949; AFP37949; MSMEI_1476.
GeneIDi4531259.
KEGGimsb:LJ00_07555.
msg:MSMEI_1476.
msm:MSMEG_1512.
PATRICi18075481. VBIMycSme59918_1497.

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
HOGENOMiHOG000168006.
KOiK01710.
OMAiYLENRAW.
OrthoDBiPOG091H044P.

Enzyme and pathway databases

UniPathwayiUPA00124.

Family and domain databases

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

Entry informationi

Entry nameiRMLB_MYCS2
AccessioniPrimary (citable) accession number: A0QSK6
Secondary accession number(s): I7G5T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: January 9, 2007
Last modified: November 2, 2016
This is version 72 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.