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P96871 (RMLD_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:strL
Ordered Locus Names:Rv3266c, MT3366
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length304 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.3

Catalytic activity

dTDP-6-deoxy-beta-L-mannose + NADP+ = dTDP-4-dehydro-6-deoxy-beta-L-mannose + NADPH. Ref.3

Pathway

Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.

Miscellaneous

Was identified as a high-confidence drug target.

Sequence similarities

Belongs to the dTDP-4-dehydrorhamnose reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 304304dTDP-4-dehydrorhamnose reductase
PRO_0000395352

Regions

Nucleotide binding12 – 165NAD By similarity
Nucleotide binding16 – 172NADP By similarity
Nucleotide binding35 – 362NAD By similarity
Nucleotide binding41 – 422NAD/NADP By similarity
Nucleotide binding62 – 654NAD By similarity
Nucleotide binding63 – 653NADP By similarity
Nucleotide binding132 – 1365NAD/NADP By similarity
Region104 – 1052Substrate binding By similarity

Sites

Binding site1571Substrate; via amide nitrogen By similarity
Binding site1581NAD; via amide nitrogen By similarity
Binding site2561Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P96871 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: F8D73C1674599E09

FASTA30432,045
        10         20         30         40         50         60 
MAGRSERLVI TGAGGQLGSH LTAQAAREGR DMLALTSSQW DITDPAAAER IIRHGDVVIN 

        70         80         90        100        110        120 
CAAYTDVDGA ESNEAVAYAV NATGPQHLAR ACARVGARLI HVSTDYVFDG DFGGAEPRPY 

       130        140        150        160        170        180 
EPTDETAPQG VYARSKLAGE QAVLAAFPEA AVVRTAWVYT GGTGKDFVAV MRRLAAGHGR 

       190        200        210        220        230        240 
VDVVDDQTGS PTYVADLAEA LLALADAGVR GRVLHAANEG VVSRFGQARA VFEECGADPQ 

       250        260        270        280        290        300 
RVRPVSSAQF PRPAPRSSYS ALSSRQWALA GLTPLRHWRS ALATALAAPA NSTSIDRRLP 


STRD 

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"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, CATALYTIC ACTIVITY.
Strain: ATCC 25618 / H37Rv.
[4]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842582 Genomic DNA. Translation: CAB07093.1.
AE000516 Genomic DNA. Translation: AAK47707.1.
AL123456 Genomic DNA. Translation: CCP46085.1.
PIRC70978.
RefSeqNP_217783.1. NC_000962.3.
NP_337893.1. NC_002755.2.
YP_006516743.1. NC_018143.1.

3D structure databases

HSSPHSSP built from PDB template 1N2S based on UniProtKB P26392.
ProteinModelPortalP96871.
SMRP96871. Positions 7-282.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv3266c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK47707; AAK47707; MT3366.
GeneID13318089.
888704.
922434.
KEGGmtc:MT3366.
mtu:Rv3266c.
mtv:RVBD_3266c.
PATRIC18129154. VBIMycTub22151_3673.

Organism-specific databases

TubercuListRv3266c.

Phylogenomic databases

eggNOGCOG1091.
HOGENOMHOG000227711.
KOK00067.
OMAGSPTYVG.
ProtClustDBCLSK792390.

Enzyme and pathway databases

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...

Other

BindingDBP96871.
ChEMBLCHEMBL1938225.

Entry information

Entry nameRMLD_MYCTU
AccessionPrimary (citable) accession number: P96871
Secondary accession number(s): L0TEU1, Q7D5T1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: May 1, 1997
Last modified: May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families