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A0QTF8 (RMLD_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
dTDP-4-dehydrorhamnose reductase

EC=1.1.1.133
Alternative name(s):
dTDP-4-keto-L-rhamnose reductase
dTDP-6-deoxy-L-lyxo-4-hexulose reductase
dTDP-6-deoxy-L-mannose dehydrogenase
dTDP-L-rhamnose synthase
Gene names
Name:rmlD
Synonyms:rfbD
Ordered Locus Names:MSMEG_1825, MSMEI_1782
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. 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. Ref.4

Catalytic activity

dTDP-beta-L-rhamnose + NADP+ = dTDP-4-dehydro-beta-L-rhamnose + NADPH.

Pathway

Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.

Sequence similarities

Belongs to the dTDP-4-dehydrorhamnose reductase family.

Sequence caution

The sequence AFP38254.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327dTDP-4-dehydrorhamnose reductase
PRO_0000399900

Regions

Nucleotide binding40 – 445NAD By similarity
Nucleotide binding44 – 452NADP By similarity
Nucleotide binding63 – 642NAD By similarity
Nucleotide binding69 – 702NAD/NADP By similarity
Nucleotide binding90 – 934NAD By similarity
Nucleotide binding91 – 933NADP By similarity
Nucleotide binding157 – 1615NAD/NADP By similarity
Region132 – 1332Substrate binding By similarity

Sites

Binding site1821Substrate; via amide nitrogen By similarity
Binding site1831NAD; via amide nitrogen By similarity
Binding site2811Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QTF8 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 5AD5A5F7337A7276

FASTA32734,254
        10         20         30         40         50         60 
MDLINGMGTS PGYWRTPREP GNDHRRARLD VMAQRIVITG AGGMVGRVLA DQAAAKGHTV 

        70         80         90        100        110        120 
LALTSSQCDI TDEDAVRRFV ANGDVVINCA AYTQVDKAED EPERAHAVNA VGPGNLAKAC 

       130        140        150        160        170        180 
AAVDAGLIHI STDYVFGAVD RDTPYEVDDE TGPVNIYGRT KLAGEQAVLA AKPDAYVVRT 

       190        200        210        220        230        240 
AWVYRGGDGS DFVATMRRLA AGDGAIDVVA DQVGSPTYTG DLVGALLQIV DGGVEPGILH 

       250        260        270        280        290        300 
AANAGVASRF DQARATFEAV GADPERVRPC GSDRHPRPAP RPSYTVLSSQ RSAQAGLTPL 

       310        320 
RDWREALQDA VAAVVGATTD GPLPSTP 

« Hide

References

« Hide 'large scale' references
[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"Formation of dTDP-rhamnose is essential for growth of mycobacteria."
Ma Y., Pan F., McNeil M.
J. Bacteriol. 184:3392-3395(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000480 Genomic DNA. Translation: ABK74972.1.
CP001663 Genomic DNA. Translation: AFP38254.1. Different initiation.
RefSeqYP_006566549.1. NC_018289.1.
YP_886196.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0QTF8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_1825.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK74972; ABK74972; MSMEG_1825.
AFP38254; AFP38254; MSMEI_1782.
GeneID4533132.
KEGGmsg:MSMEI_1782.
msm:MSMEG_1825.
PATRIC18076099. VBIMycSme59918_1807.

Phylogenomic databases

eggNOGCOG1091.
HOGENOMHOG000227711.
KOK00067.
OMALTNAGSP.
OrthoDBEOG6HTP2V.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-1825-MONOMER.
UniPathwayUPA00124.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
TIGRFAMsTIGR01214. rmlD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRMLD_MYCS2
AccessionPrimary (citable) accession number: A0QTF8
Secondary accession number(s): I7G6I9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways