NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=N2-3-11;
DOI=10.1093/nar/15.19.8041; PubMed=3118332 [NCBI, ExPASy, EBI, Israel, Japan]
Distler J., Ebert A., Mansouri K., Pissowotzki K., Stockmann M., Piepersberg W.;
"Gene cluster for streptomycin biosynthesis in Streptomyces griseus: nucleotide sequence of three genes and analysis of transcriptional activity.";
Nucleic Acids Res. 15:8041-8056(1987).

Comments

FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis (By similarity).
FUNCTION: Involved in the biosynthesis of the streptose moiety of streptomycin.
CATALYTIC ACTIVITY: dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-glucose.
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
PATHWAY: Antibiotic biosynthesis; streptomycin biosynthesis .
SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y00459; CAA68514.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A26984; A26984.

3D structure databases

HSSP

Q9F7K6; 1IIN. [HSSP ENTRY / PDB]

ModBase

P08075.

Ontologies

GO:0008879;	Molecular function: glucose-1-phosphate thymidylyltransferase activity (inferred from electronic annotation from EC).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019872;	Biological process: streptomycin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005908; G1P_thy_trans_s.
IPR005835; NTP_transferase.
Graphical view of domain structure.

Pfam

PF00483; NTP_transferase; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01208; rmlA_long; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antibiotic biosynthesis; Magnesium; Metal-binding; Nucleotidyltransferase; Streptomycin biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 355`	`355`	`Glucose-1-phosphate thymidylyltransferase.`	`PRO_0000208005`
`METAL`	`107 107`		`Magnesium (By similarity).`
`METAL`	`220 220`		`Magnesium (By similarity).`

Sequence information

Length: 355 AA [This is the length of the unprocessed precursor]

Molecular weight: 38098 Da [This is the MW of the unprocessed precursor]

CRC64: ED136AEA854EB7DA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKALVLAGGT GTRLRPITHT SAKQLVPVAN KPVLFYGLEA IRAAGIIDVG IVVGDTADEI 

        70         80         90        100        110        120 
VAAVGDGSRF GLKVSYIPQS KPLGLAHCVL ISRDFLGEDD FIMYLGDNFV VGVVEDSVRE 

       130        140        150        160        170        180 
FRAARPDAHL MLTRVPEPRS FGVAELSDSG QVLGLEEKPA HPKSDLALVG VYLFSPAIHE 

       190        200        210        220        230        240 
AVAAITPSWR GELEITDAVQ WLIDAGRDVR STVISGYWKD TGNVTDMLEV NRLVLETTEP 

       250        260        270        280        290        300 
RCDGLVDERS DLIGRVLVEE GAEVRNSRVM GPTVIGAGTR VTNSYVGPFT SLAEDCVVED 

       310        320        330        340        350 
SEVEFSIVLR GASISGVRRI EASLIGRHVQ VTSAPEVPHA NRLVLGDHSR AQISS

P08075 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools