Reviewed, UniProtKB/Swiss-Prot P0AEP3 (GALU_ECOLI)

Names and origin

Protein names

Recommended name:
    UTP--glucose-1-phosphate uridylyltransferase
    EC=2.7.7.9
Alternative name(s):
    UDP-glucose pyrophosphorylase
      Short name=UDPGP
    Alpha-D-glucosyl-1-phosphate uridylyltransferase
    Uridine diphosphoglucose pyrophosphorylase

Gene names

Name:	galU
Synonyms:	ychD
Ordered Locus Names:	b1236, JW1224

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a role in stationary phase survival.
Catalytic activity	UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose.
Cofactor	Magnesium.
Subunit structure	Homotetramer or homopentamer.
Sequence similarities	Belongs to the UDPGP type 2 family.

Ontologies

Keywords
Ligand	Magnesium
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	UDP-glucose metabolic process Inferred from electronic annotation. Source: InterPro biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	UTP:glucose-1-phosphate uridylyltransferase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
purU	P37051	1	EBI-909038,EBI-1122931

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2 Ref.7

Chain

2 – 302

301

UTP--glucose-1-phosphate uridylyltransferase

PRO_0000201354

Secondary structure

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302

Helix Strand Turn

Details...

Beta strand

10 – 14

5

Helix

20 – 22

3

Turn

23 – 26

4

Beta strand

27 – 29

3

Helix

31 – 33

3

Helix

41 – 51

11

Beta strand

56 – 61

6

Helix

63 – 65

3

Helix

66 – 72

7

Helix

76 – 82

7

Helix

89 – 96

8

Beta strand

103 – 108

6

Helix

115 – 121

7

Helix

123 – 126

4

Beta strand

131 – 134

4

Beta strand

138 – 140

3

Turn

147 – 149

3

Helix

152 – 162

11

Beta strand

165 – 171

7

Helix

175 – 177

3

Beta strand

178 – 182

5

Beta strand

193 – 196

4

Beta strand

198 – 202

5

Turn

205 – 207

3

Beta strand

211 – 220

10

Helix

224 – 228

5

Helix

241 – 251

11

Beta strand

254 – 258

5

Beta strand

263 – 265

3

Helix

269 – 282

14

Turn

284 – 286

3

Helix

287 – 297

11

Sequences

	Sequence		Length	Mass (Da)
	P0AEP3-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: ADEAEB3F6A1194CB	FASTA	302	32,942
	10 20 30 40 50 60 MAAINTKVKK AVIPVAGLGT RMLPATKAIP KEMLPLVDKP LIQYVVNECI AAGITEIVLV 70 80 90 100 110 120 THSSKNSIEN HFDTSFELEA MLEKRVKRQL LDEVQSICPP HVTIMQVRQG LAKGLGHAVL 130 140 150 160 170 180 CAHPVVGDEP VAVILPDVIL DEYESDLSQD NLAEMIRRFD ETGHSQIMVE PVADVTAYGV 190 200 210 220 230 240 VDCKGVELAP GESVPMVGVV EKPKADVAPS NLAIVGRYVL SADIWPLLAK TPPGAGDEIQ 250 260 270 280 290 300 LTDAIDMLIE KETVEAYHMK GKSHDCGNKL GYMQAFVEYG IRHNTLGTEF KAWLEEEMGI KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multicopy suppression: an approach to understanding intracellular functioning of the protein export system." Ueguchi C., Ito K. J. Bacteriol. 174:1454-1461(1992) [PubMed: 1537791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"UTP: alpha-D-glucose-1-phosphate uridylyltransferase of Escherichia coli: isolation and DNA sequence of the galU gene and purification of the enzyme." Weissborn A.C., Liu Q., Rumley M.K., Kennedy E.P. J. Bacteriol. 176:2611-2618(1994) [PubMed: 8169209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, CHARACTERIZATION. Strain: K12.
[3]	"Overproduction and characterization of recombinant UDP-glucose pyrophosphorylase from Escherichia coli K-12." Hossain S.A., Tanizawa K., Kazuta Y., Fukui T. J. Biochem. 115:965-972(1994) [PubMed: 7961613] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[4]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 2-18. Strain: K12 / EMG2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59940 Genomic DNA. Translation: CAA42564.1.
M98830 Unassigned DNA. Translation: AAA20118.1.
U00096 Genomic DNA. Translation: AAC74318.1.
AP009048 Genomic DNA. Translation: BAA36104.1.

PIR

JC2265. G64870.

RefSeq

AP_001862.1.
NP_415752.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E3D	X-ray	1.95	A/B/C/D	1-302	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AEP3. 3 interactions.

STRING

P0AEP3.

Genome annotation databases

GeneID

945730.

GenomeReviews

Gene locus JW1224 in contig AP009048_GR.
Gene locus b1236 in contig U00096_GR.

KEGG

ecj:JW1224.
eco:b1236.

Organism-specific databases

EchoBASE

EB1295.

EcoGene

EG11319. galU.

CMR

Search...

Phylogenomic databases

eggNOG

COG1210.

HOGENOM

HBG688195.

OMA

CIEDHFD.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUC1PURIDYLTRANS-MONOMER.
ECOL168927:B1236-MONOMER.
MetaCyc:GLUC1PURIDYLTRANS-MONOMER.

Gene expression databases

Genevestigator

P0AEP3.

Family and domain databases

InterPro

IPR005771. GalU_uridylyltTrfase_bac/arc.
IPR005835. NTP_transferase.
[Graphical view]

Pfam

PF00483. NTP_transferase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01099. galU. 1 hit.

ProtoNet

Search...

Entry information

Entry name

GALU_ECOLI

Accession

Primary (citable) accession number: P0AEP3
Secondary accession number(s): P25520

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)