P29781 (RMLD_STRGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

strL

Organism

Streptomyces griseus

Taxonomic identifier

1911 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces griseus group

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1
Catalytic activity	dTDP-6-deoxy-beta-L-mannose + NADP+ = dTDP-4-dehydro-6-deoxy-beta-L-mannose + NADPH.
Cofactor	Binds 1 magnesium ion per monomer By similarity.
Pathway	Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Antibiotic biosynthesis; streptomycin biosynthesis.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the dTDP-4-dehydrorhamnose reductase family.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis Streptomycin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	dTDP-rhamnose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway extracellular polysaccharide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB streptomycin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	dTDP-4-dehydrorhamnose reductase activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 304	304	dTDP-4-dehydrorhamnose reductase		PRO_0000207989
Regions
	Nucleotide binding	13 – 19	7	NADP Potential
	Nucleotide binding	13 – 17	5	NAD By similarity
	Nucleotide binding	17 – 18	2	NADP By similarity
	Nucleotide binding	36 – 37	2	NAD By similarity
	Nucleotide binding	42 – 43	2	NAD/NADP By similarity
	Nucleotide binding	65 – 68	4	NAD By similarity
	Nucleotide binding	66 – 68	3	NADP By similarity
	Nucleotide binding	131 – 135	5	NAD/NADP By similarity
	Region	107 – 108	2	Substrate binding By similarity
Sites
	Binding site	157	1	Substrate; via amide nitrogen By similarity
	Binding site	227	1	Substrate By similarity
	Binding site	259	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29781 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 7594F25D3F7ED0CB	FASTA	304	32,215
	10 20 30 40 50 60 MSPYPRPRWL VTGASGMLGR ELTPLLDRRG AAVTALGRGH LDITDGAAVR SAVAEHRPAV 70 80 90 100 110 120 VVNCAAWTAV DEAESEPALA MAVNGEGPRH LAQACRAVGA VLLQLSTDYV FPGSGGRPYR 130 140 150 160 170 180 EDHPTGPRTV YGCTKRAGER AVLEVLPDTG YIVRTAWLYG AGGPNFVAKM IRLEADEDTV 190 200 210 220 230 240 LVVDDQHGQP TWTADLADRL AALGAAALAG TAPAGIYHAT NTGGTTWNAL APETFRLLGA 250 260 270 280 290 300 DPARVRPTTS LALARPAVRP RYSVLDQSRW KAAGLEPLRH WRAALTESFP ALCGRAGRPV PGPR

References

[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(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BIOSYNTHESIS OF THE STREPTOSE MOIETY OF STREPTOMYCIN. Strain: N2-3-11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X62567 Genomic DNA. Translation: CAA44443.1.
PIR	SYSMPG. S18618.
3D structure databases
ProteinModelPortal	P29781.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00066. UPA00124.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR005913. dTDP_dehydrorham_reduct. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF04321. RmlD_sub_bind. 1 hit. [Graphical view]
TIGRFAMs	TIGR01214. rmlD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RMLD_STRGR

Accession

Primary (citable) accession number: P29781

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program