P0C7J4 (RMLA_XANCP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucose-1-phosphate thymidylyltransferase
EC=2.7.7.24

Alternative name(s):
dTDP-glucose pyrophosphorylase
dTDP-glucose synthase

Gene names

Name:	rmlA
Ordered Locus Names:	XCC0622

Organism

Xanthomonas campestris pv. campestris

Taxonomic identifier

340 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis By similarity.
Catalytic activity	dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-glucose.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the glucose-1-phosphate thymidylyltransferase family.
Sequence caution	The sequence AAM39938.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	extracellular polysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glucose-1-phosphate thymidylyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 295	295	Glucose-1-phosphate thymidylyltransferase		PRO_0000208001
Sites
	Metal binding	111	1	Magnesium By similarity
	Metal binding	226	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C7J4 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: 585D239B6EAF4554	FASTA	295	32,508
	10 20 30 40 50 60 MTQRKGIILA GGSGTRLYPI TKGVSKQLLP VYDKPMIYYP LSVLMLAGIR DILIINTPHE 70 80 90 100 110 120 QALFQSLLGD GAQWGVNIQY AVQPSPDGLA QAYLIGRDFV GGKPSCLVLG DNIFHGHGLT 130 140 150 160 170 180 DTLRRADARE QGATVFGYWV NDPERYGVAE FDQHGKVIDI AEKPEKPRSN YAVTGLYFYD 190 200 210 220 230 240 GKASDYAAAL KPSPRGELEI TDLNRCYLDA GDLHLEPLGR GYAWLDTGTH QSLHEAANFI 250 260 270 280 290 ETIQMRQGLQ VCCPEEIAFG QGWIDAEQLE RLAAPLLKND YGKYLTALAK RGAVH

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM39938.1. Different initiation.
RefSeq	NP_636014.1. NC_003902.1.
3D structure databases
ProteinModelPortal	P0C7J4.
SMR	P0C7J4. Positions 4-290.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1001156.
GenomeReviews	Gene locus XCC0622 in contig AE008922_GR.
KEGG	xcc:XCC0622.
PATRIC	24071894. VBIXanCam115730_0682.
Phylogenomic databases
HOGENOM	HBG688195.
OMA	EDNASFK.
ProtClustDB	CLSK2518014.
Family and domain databases
InterPro	IPR005907. G1P_thy_trans_s. IPR005835. NTP_transferase. [Graphical view]
KO	K00973.
PANTHER	PTHR22572:SF13. PTHR22572:SF13. 1 hit.
Pfam	PF00483. NTP_transferase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01207. RmlA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RMLA_XANCP

Accession

Primary (citable) accession number: P0C7J4
Secondary accession number(s): P55256

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program