Galactose-1-phosphate uridylyltransferase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P09148 (GAL7_ECOLI)

Last modified June 16, 2009. Version 97. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-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: K_M=0.200 mM for uridine 5'-diphosphate glucose Ref.9 K_M=0.303 mM for galactose-1-phosphate K_M=0.121 mM for uridine 5'-diphosphate galactose K_M=0.157 mM for glucose-1-phosphate V_max=180 µmol/min/mg enzyme

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Ontologies

Keywords
Biological process	Carbohydrate metabolism Galactose metabolism
Ligand	Iron Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	galactose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	UDP-glucose:hexose-1-phosphate uridylyltransferase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

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

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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

Tele-UMP-histidine intermediate Ref.8

Metal binding

Zinc

Metal binding

Zinc

Metal binding

115

Zinc

Metal binding

164

Zinc

Metal binding

182

Iron

Metal binding

281

Iron

Metal binding

296

Iron

Metal binding

298

Iron

Experimental info

Mutagenesis

160

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

Mutagenesis

161

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

Mutagenesis

166

H → G: Abolishes enzymatic activity. Ref.11

Sequence conflict

29 – 31

AKR → LS in CAA29574. Ref.1

Secondary structure

348

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P09148-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 3D55D2CB38D8C9A2
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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

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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: 3022232] [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. 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.
[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: 9278503] [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: 16738553] [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: 3158881] [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: 2823224] [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: 321007] [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: 8794735] [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: 10820011] [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: 7669762] [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: 9063869] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS OF HIS-166.

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Cross-references

Sequence databases

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

AP_001389.1.
NP_415279.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9735N.

IntAct

P09148. 1 interaction.

Genome annotation databases

GeneID

945357.

GenomeReviews

Gene locus JW0741 in contig AP009048_GR.
Gene locus b0758 in contig U00096_GR.

KEGG

ecj:JW0741.
eco:b0758.

Organism-specific databases

EchoBASE

EB0361.

EcoGene

EG10366. galT.

CMR

Search...

Phylogenomic databases

HOGENOM

P09148.

OMA

P09148. DHWQLHA.

Enzyme and pathway databases

BioCyc

EcoCyc:GALACTURIDYLYLTRANS-MON.
MetaCyc:GALACTURIDYLYLTRANS-MON.

BRENDA

2.7.7.12. 246.

Family and domain databases

InterPro

IPR001937. GalP_UDPtransf1.
IPR019779. GalP_UDPtransf1_His-AS.
IPR005850. GalP_Utransf_C.
IPR005849. GalP_Utransf_N.
IPR011151. His_triad_motif.
[Graphical view]

Gene3D

G3DSA:3.30.428.10. His_triad_motif. 2 hits.

PANTHER

PTHR11943. GalP_UDPtransf1. 1 hit.

Pfam

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

PIRSF

PIRSF000808. GalT. 1 hit.

ProDom

PD005051. GalP_Utransf. 2 hits.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00209. galT_1. 1 hit.

PROSITE

PS00117. GAL_P_UDP_TRANSF_I. 1 hit.
[Graphical view]

ProtoNet

Search...

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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:	June 16, 2009
This is version 97 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)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents