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Protein

dTDP-4-dehydrorhamnose reductase

Gene

rmlD

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 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.1 Publication

Catalytic activityi

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

Pathway:idTDP-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei182 – 1821Substrate; via amide nitrogenBy similarity
Binding sitei183 – 1831NAD; via amide nitrogenBy similarity
Binding sitei281 – 2811SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 445NADBy similarity
Nucleotide bindingi44 – 452NADPBy similarity
Nucleotide bindingi63 – 642NADBy similarity
Nucleotide bindingi69 – 702NAD/NADPBy similarity
Nucleotide bindingi90 – 934NADBy similarity
Nucleotide bindingi91 – 933NADPBy similarity
Nucleotide bindingi157 – 1615NAD/NADPBy similarity

GO - Molecular functioni

  • dTDP-4-dehydrorhamnose reductase 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

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-1825-MONOMER.
UniPathwayiUPA00124.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:rmlD
Synonyms:rfbD
Ordered Locus Names:MSMEG_1825, MSMEI_1782
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
ProteomesiUP000006158 Componenti: Chromosome UP000000757 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327dTDP-4-dehydrorhamnose reductasePRO_0000399900Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi246196.MSMEG_1825.

Structurei

3D structure databases

ProteinModelPortaliA0QTF8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni132 – 1332Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1091.
HOGENOMiHOG000227711.
KOiK00067.
OMAiRSPDICE.
OrthoDBiEOG6HTP2V.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
IPR029900. RmlD.
IPR029903. RmlD-like-bd.
[Graphical view]
PANTHERiPTHR10491. PTHR10491. 1 hit.
PTHR10491:SF5. PTHR10491:SF5. 1 hit.
PfamiPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01214. rmlD. 1 hit.

Sequencei

Sequence statusi: Complete.

A0QTF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLINGMGTS PGYWRTPREP GNDHRRARLD VMAQRIVITG AGGMVGRVLA
60 70 80 90 100
DQAAAKGHTV LALTSSQCDI TDEDAVRRFV ANGDVVINCA AYTQVDKAED
110 120 130 140 150
EPERAHAVNA VGPGNLAKAC AAVDAGLIHI STDYVFGAVD RDTPYEVDDE
160 170 180 190 200
TGPVNIYGRT KLAGEQAVLA AKPDAYVVRT AWVYRGGDGS DFVATMRRLA
210 220 230 240 250
AGDGAIDVVA DQVGSPTYTG DLVGALLQIV DGGVEPGILH AANAGVASRF
260 270 280 290 300
DQARATFEAV GADPERVRPC GSDRHPRPAP RPSYTVLSSQ RSAQAGLTPL
310 320
RDWREALQDA VAAVVGATTD GPLPSTP
Length:327
Mass (Da):34,254
Last modified:January 9, 2007 - v1
Checksum:i5AD5A5F7337A7276
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74972.1.
CP001663 Genomic DNA. Translation: AFP38254.1. Different initiation.
RefSeqiWP_011727934.1. NC_008596.1.
YP_886196.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK74972; ABK74972; MSMEG_1825.
AFP38254; AFP38254; MSMEI_1782.
GeneIDi4533132.
KEGGimsg:MSMEI_1782.
msm:MSMEG_1825.
PATRICi18076099. VBIMycSme59918_1807.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74972.1.
CP001663 Genomic DNA. Translation: AFP38254.1. Different initiation.
RefSeqiWP_011727934.1. NC_008596.1.
YP_886196.1. NC_008596.1.

3D structure databases

ProteinModelPortaliA0QTF8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_1825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK74972; ABK74972; MSMEG_1825.
AFP38254; AFP38254; MSMEI_1782.
GeneIDi4533132.
KEGGimsg:MSMEI_1782.
msm:MSMEG_1825.
PATRICi18076099. VBIMycSme59918_1807.

Phylogenomic databases

eggNOGiCOG1091.
HOGENOMiHOG000227711.
KOiK00067.
OMAiRSPDICE.
OrthoDBiEOG6HTP2V.

Enzyme and pathway databases

UniPathwayiUPA00124.
BioCyciMSME246196:GJ4Y-1825-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
IPR029900. RmlD.
IPR029903. RmlD-like-bd.
[Graphical view]
PANTHERiPTHR10491. PTHR10491. 1 hit.
PTHR10491:SF5. PTHR10491:SF5. 1 hit.
PfamiPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01214. rmlD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiRMLD_MYCS2
AccessioniPrimary (citable) accession number: A0QTF8
Secondary accession number(s): I7G6I9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: January 9, 2007
Last modified: July 22, 2015
This is version 67 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

External Data

Dasty 3

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 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.