[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 33. STRAIN=N2-3-11; Ahlert J., Distler J., Mansouri K., Roggel M., Altenbach H.J., Piepersberg W.; Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83. STRAIN=N2-3-11; DOI=10.1007/BF00293829; PubMed=1661369 [NCBI, ExPASy, EBI, Israel, Japan] Pissowotzki K., Mansouri K., Piepersberg W.; "Genetics of streptomycin production in Streptomyces griseus: molecular structure and putative function of genes strELMB2N."; Mol. Gen. Genet. 231:113-123(1991).

Comments

CATALYTIC ACTIVITY: dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-glucose.
PATHWAY: Antibiotic biosynthesis; streptomycin biosynthesis .

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

Y08763; CAA70009.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X62567; CAA44446.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S19785; S19785.

3D structure databases

ModBase

P29785.

Ontologies

GO:0008879;	Molecular function: glucose-1-phosphate thymidylyltransferase activity (inferred from electronic annotation from EC).
GO:0004437;	Molecular function: inositol or phosphatidylinositol phosphatase activity (inferred from electronic annotation from InterPro).
GO:0019872;	Biological process: streptomycin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000760; Inositol_P.
Graphical view of domain structure.

PANTHER

PTHR20854; Inositol_P; 1.

Pfam

PF00459; Inositol_P; 1.
Pfam graphical view of domain structure.

PRINTS

PR00378; INOSPHPHTASE.

ProDom

PD023420; Inositol_P; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Other

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

Keywords

Antibiotic biosynthesis; Streptomycin biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 259`	`259`		`Glucose-1-phosphate thymidylyltransferase.`	`PRO_0000072287`

Sequence information

Length: 259 AA [This is the length of the unprocessed precursor]

Molecular weight: 27858 Da [This is the MW of the unprocessed precursor]

CRC64: D2DA6E0E75AFF28A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDNDSDVRL AHRLAEIADT LAWEFFGGAP AVRHKSDGSP VSEADLAVEK ALLAVLAAER 

        70         80         90        100        110        120 
PGDAVLTEES GSLGTRSSRR RWILDPIDGT IPFLAGERGW GTHVALEVDE ELRTAVLSRP 

       130        140        150        160        170        180 
TERSRWWAVR GRGAFTSVRG EPLSAARPLR IPSAPLPLEA ARVGGFLMPD SPVEPVRDRM 

       190        200        210        220        230        240 
RWVESSVCLV GDLLEGRVDA VIDEGGHVWD RAPAALLVHE AGGRVDDLRG GGRLDERWLV 

       250 
YAADGVADGL AGLLRDVGA

P29785 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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