P09148 (GAL7_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Galactose-1-phosphate uridylyltransferase
Short name=Gal-1-P uridylyltransferase
EC=2.7.7.12

Alternative name(s):
UDP-glucose--hexose-1-phosphate uridylyltransferase

Gene names

Name:	galT
Synonyms:	galB
Ordered Locus Names:	b0758, JW0741

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose.
Cofactor	Binds 1 iron ion per subunit. Binds 1 zinc ion per subunit.
Pathway	Carbohydrate metabolism; galactose metabolism.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.
Biophysicochemical properties	Kinetic parameters: KM=0.200 mM for uridine 5'-diphosphate glucose Ref.9 KM=0.303 mM for galactose-1-phosphate KM=0.121 mM for uridine 5'-diphosphate galactose KM=0.157 mM for glucose-1-phosphate Vmax=180 µmol/min/mg enzyme

Ontologies

Keywords
Biological process	Carbohydrate metabolism Galactose metabolism
Ligand	Iron Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	galactose catabolic process via UDP-galactose Inferred from mutant phenotype PubMed 16590575. Source: EcoCyc
Molecular_function	UDP-glucose:hexose-1-phosphate uridylyltransferase activity Inferred from direct assay PubMed 5338129. Source: EcoCyc ferrous iron binding Inferred from direct assay PubMed 7727423. Source: EcoCyc zinc ion binding Inferred from direct assay PubMed 7727423. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-1120083,EBI-548960

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 348

348

Galactose-1-phosphate uridylyltransferase

PRO_0000169894

Sites

Active site

166

1

Tele-UMP-histidine intermediate Ref.8

Metal binding

52

1

Zinc

Metal binding

55

1

Zinc

Metal binding

115

1

Zinc

Metal binding

164

1

Zinc

Metal binding

182

1

Iron

Metal binding

281

1

Iron

Metal binding

296

1

Iron

Metal binding

298

1

Iron

Experimental info

Mutagenesis

160

1

C → S or A: Slight inhibition of enzymatic activity. Ref.9

Mutagenesis

161

1

S → A: 7000-fold reduction in specific activity. Ref.9

Mutagenesis

166

1

H → G: Abolishes enzymatic activity. Ref.11

Sequence conflict

29 – 31

3

AKR → LS in CAA29574. Ref.1

Secondary structure

1

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348

Helix Strand Turn

Details...

Turn

6 – 8

3

Beta strand

11 – 14

4

Turn

16 – 18

3

Beta strand

21 – 24

4

Helix

28 – 30

3

Beta strand

73 – 76

4

Beta strand

95 – 97

3

Beta strand

99 – 101

3

Beta strand

104 – 111

8

Helix

119 – 121

3

Helix

124 – 144

21

Beta strand

146 – 155

10

Helix

156 – 158

3

Beta strand

164 – 174

11

Helix

177 – 193

17

Helix

197 – 208

12

Beta strand

212 – 215

4

Beta strand

217 – 222

6

Beta strand

233 – 239

7

Helix

244 – 246

3

Helix

249 – 270

22

Beta strand

276 – 281

6

Beta strand

285 – 288

4

Beta strand

296 – 300

5

Beta strand

305 – 308

4

Helix

316 – 319

4

Beta strand

323 – 326

4

Helix

328 – 336

9

Helix

343 – 346

4

Sequences

	Sequence		Length	Mass (Da)
	P09148 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 3D55D2CB38D8C9A2	FASTA	348	39,646
	10 20 30 40 50 60 MTQFNPVDHP HRRYNPLTGQ WILVSPHRAK RPWQGAQETP AKQVLPAHDP DCFLCAGNVR 70 80 90 100 110 120 VTGDKNPDYT GTYVFTNDFA ALMSDTPDAP ESHDPLMRCQ SARGTSRVIC FSPDHSKTLP 130 140 150 160 170 180 ELSVAALTEI VKTWQEQTAE LGKTYPWVQV FENKGAAMGC SNPHPHGQIW ANSFLPNEAE 190 200 210 220 230 240 REDRLQKEYF AEQKSPMLVD YVQRELADGS RTVVETEHWL AVVPYWAAWP FETLLLPKAH 250 260 270 280 290 300 VLRITDLTDA QRSDLALALK KLTSRYDNLF QCSFPYSMGW HGAPFNGEEN QHWQLHAHFY 310 320 330 340 PPLLRSATVR KFMVGYEMLA ETQRDLTAEQ AAERLRAVSD IHFRESGV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequences of the gal E gene and the gal T gene of E. coli." Lemaire H.-G., Mueller-Hill B. Nucleic Acids Res. 14:7705-7711(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Structure of the galactokinase gene of Escherichia coli, the last (?) gene of the gal operon." Debouck C., Riccio A., Schumperli D., McKenney K., Jeffers J., Hughes C., Rosenberg M., Heusterspreute M., Brunel F., Davison J. Nucleic Acids Res. 13:1841-1853(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-348.
[6]	"The nucleotide sequence of the gal T gene of Escherichia coli." Cornwell T.L., Adhya S.L., Reznikoff W.S., Frey P.A. Nucleic Acids Res. 15:8116-8116(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-38.
[7]	"Galactose-1-phosphate uridylyltransferase: isolation and properties of a uridylyl-enzyme intermediate." Wong L.J., Sheu K.F., Lee S.L., Frey P.A. Biochemistry 16:1010-1016(1977) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer." Wedekind J.E., Frey P.A., Rayment I. Biochemistry 35:11560-11569(1996) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE HIS-166.
[9]	"Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine." Geeganage S., Ling V.W., Frey P.A. Biochemistry 39:5397-5404(2000) [PubMed] [Europe PMC] [Abstract] Cited for: KINETIC PARAMETERS, MUTAGENESIS OF CYS-160 AND SER-161.
[10]	"Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8-A resolution." Wedekind J.E., Frey P.A., Rayment I. Biochemistry 34:11049-11061(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[11]	"Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site." Thoden J.B., Ruzicka F.J., Frey P.A., Rayment I., Holden H.M. Biochemistry 36:1212-1222(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS OF HIS-166.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06226 Genomic DNA. Translation: CAA29574.1.
U00096 Genomic DNA. Translation: AAC73845.1.
AP009048 Genomic DNA. Translation: BAA35420.1.
X02306 Genomic DNA. Translation: CAA26171.1.

PIR

XNECUD. S00722.

RefSeq

NP_415279.1. NC_000913.2.
YP_489031.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GUP	X-ray	1.80	A/B/C/D	1-348	[»]
1GUQ	X-ray	1.80	A/B/C/D	1-348	[»]
1HXP	X-ray	1.80	A/B	1-348	[»]
1HXQ	X-ray	1.86	A/B	1-348	[»]

ProteinModelPortal

P09148.

SMR

P09148. Positions 2-348.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9735N.

IntAct

P09148. 1 interaction.

STRING

511145.b0758.

Proteomic databases

PaxDb

P09148.

PRIDE

P09148.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73845; AAC73845; b0758.
BAA35420; BAA35420; BAA35420.

GeneID

12932709.
945357.

KEGG

ecj:Y75_p0731.
eco:b0758.

PATRIC

32116717. VBIEscCol129921_0784.

Organism-specific databases

EchoBASE

EB0361.

EcoGene

EG10366. galT.

Phylogenomic databases

eggNOG

COG1085.

HOGENOM

HOG000230490.

KO

K00965.

OMA

PDYQGTY.

ProtClustDB

PRK11720.

Enzyme and pathway databases

BioCyc

EcoCyc:GALACTURIDYLYLTRANS-MONOMER.
ECOL316407:JW0741-MONOMER.
MetaCyc:GALACTURIDYLYLTRANS-MONOMER.

BRENDA

2.7.7.12. 2026.

SABIO-RK

P09148.

UniPathway

UPA00214.

Gene expression databases

Genevestigator

P09148.

Family and domain databases

Gene3D

3.30.428.10. 2 hits.

InterPro

IPR001937. GalP_UDPtransf1.
IPR019779. GalP_UDPtransf1_His-AS.
IPR005850. GalP_Utransf_C.
IPR005849. GalP_Utransf_N.
IPR011146. HIT-like.
[Graphical view]

PANTHER

PTHR11943. PTHR11943. 1 hit.

Pfam

PF02744. GalP_UDP_tr_C. 1 hit.
PF01087. GalP_UDP_transf. 1 hit.
[Graphical view]

PIRSF

PIRSF000808. GalT. 1 hit.

SUPFAM

SSF54197. His_triad-like_motif. 2 hits.

TIGRFAMs

TIGR00209. galT_1. 1 hit.

PROSITE

PS00117. GAL_P_UDP_TRANSF_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P09148.

Entry information

Entry name

GAL7_ECOLI

Accession

Primary (citable) accession number: P09148
Secondary accession number(s): P78270

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program