Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

dTDP-4-dehydrorhamnose reductase

Gene

strL

Organism
Streptomyces griseus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the streptose moiety of streptomycin. Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. RmlD uses NADH and NADPH nearly equally well (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per monomer.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei157 – 1571Substrate; via amide nitrogenBy similarity
Binding sitei227 – 2271SubstrateBy similarity
Binding sitei259 – 2591SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 197NADPSequence Analysis
Nucleotide bindingi13 – 175NADBy similarity
Nucleotide bindingi17 – 182NADPBy similarity
Nucleotide bindingi36 – 372NADBy similarity
Nucleotide bindingi42 – 432NAD/NADPBy similarity
Nucleotide bindingi65 – 684NADBy similarity
Nucleotide bindingi66 – 683NADPBy similarity
Nucleotide bindingi131 – 1355NAD/NADPBy similarity

GO - Molecular functioni

  1. dTDP-4-dehydrorhamnose reductase activity Source: UniProtKB

GO - Biological processi

  1. dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
  2. extracellular polysaccharide biosynthetic process Source: UniProtKB
  3. streptomycin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis, Streptomycin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00066.
UPA00124.

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:strL
OrganismiStreptomyces griseus
Taxonomic identifieri1911 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304dTDP-4-dehydrorhamnose reductasePRO_0000207989Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP29781.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1082Substrate bindingBy similarity

Sequence similaritiesi

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.

P29781-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPYPRPRWL VTGASGMLGR ELTPLLDRRG AAVTALGRGH LDITDGAAVR
60 70 80 90 100
SAVAEHRPAV VVNCAAWTAV DEAESEPALA MAVNGEGPRH LAQACRAVGA
110 120 130 140 150
VLLQLSTDYV FPGSGGRPYR EDHPTGPRTV YGCTKRAGER AVLEVLPDTG
160 170 180 190 200
YIVRTAWLYG AGGPNFVAKM IRLEADEDTV LVVDDQHGQP TWTADLADRL
210 220 230 240 250
AALGAAALAG TAPAGIYHAT NTGGTTWNAL APETFRLLGA DPARVRPTTS
260 270 280 290 300
LALARPAVRP RYSVLDQSRW KAAGLEPLRH WRAALTESFP ALCGRAGRPV

PGPR
Length:304
Mass (Da):32,215
Last modified:April 1, 1993 - v1
Checksum:i7594F25D3F7ED0CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62567 Genomic DNA. Translation: CAA44443.1.
PIRiS18618. SYSMPG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62567 Genomic DNA. Translation: CAA44443.1.
PIRiS18618. SYSMPG.

3D structure databases

ProteinModelPortaliP29781.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00066.
UPA00124.

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

  1. "Genetics of streptomycin production in Streptomyces griseus: molecular structure and putative function of genes strELMB2N."
    Pissowotzki K., Mansouri K., Piepersberg W.
    Mol. Gen. Genet. 231:113-123(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BIOSYNTHESIS OF THE STREPTOSE MOIETY OF STREPTOMYCIN.
    Strain: N2-3-11.

Entry informationi

Entry nameiRMLD_STRGR
AccessioniPrimary (citable) accession number: P29781
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 1, 2015
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

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.