Reviewed, UniProtKB/Swiss-Prot P08870 (PYRE_SALTY)

Names and origin

Protein names

Recommended name:
    Orotate phosphoribosyltransferase
      Short name=OPRT
      Short name=OPRTase
    EC=2.4.2.10

Gene names

Name:	pyrE
Ordered Locus Names:	STM3733

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	213 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	Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) By similarity.
Catalytic activity	Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01208
Cofactor	Magnesium. Manganese can replace magnesium as the divalent metal. The role of the metal is to bind 5-phosphoribose 1-diphosphate and form a Mg-5-phosphoribose 1-diphosphate complex which then serves as substrate for OPRTase. Ref.5
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP MF_01208
Subunit structure	Homodimer. Ref.8
Sequence similarities	Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Magnesium
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nucleoside metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP orotate phosphoribosyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 213

212

Orotate phosphoribosyltransferase HAMAP MF_01208

PRO_0000110734

Regions

Region

34 – 35

2

Orotate binding HAMAP MF_01208

Region

72 – 73

2

5-phosphoribose 1-diphosphate binding HAMAP MF_01208

Region

124 – 132

9

5-phosphoribose 1-diphosphate binding HAMAP MF_01208

Sites

Binding site

26

1

5-phosphoribose 1-diphosphate HAMAP MF_01208

Binding site

99

1

5-phosphoribose 1-diphosphate; shared with dimeric partner HAMAP MF_01208

Binding site

100

1

5-phosphoribose 1-diphosphate HAMAP MF_01208

Binding site

103

1

5-phosphoribose 1-diphosphate; shared with dimeric partner HAMAP MF_01208

Binding site

105

1

5-phosphoribose 1-diphosphate; shared with dimeric partner HAMAP MF_01208

Binding site

128

1

Orotate HAMAP MF_01208

Binding site

156

1

Orotate HAMAP MF_01208

Experimental info

Mutagenesis

19

1

K → Q: No loss of activity.

Mutagenesis

26

1

K → A or Q: Reduced activity.

Mutagenesis

73

1

K → A or Q: Significant loss of activity.

Mutagenesis

100

1

K → A: Reduced activity.

Mutagenesis

103

1

K → A or Q: Drastically reduced activity.

Mutagenesis

124

1

D → N: Loss of activity.

Mutagenesis

125

1

D → N: Loss of activity.

Secondary structure

1

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213

Helix Strand Turn

Details...

Helix

3 – 14

12

Beta strand

17 – 24

8

Beta strand

30 – 35

6

Helix

37 – 39

3

Helix

43 – 60

18

Beta strand

65 – 68

4

Turn

71 – 73

3

Helix

74 – 89

16

Beta strand

94 – 98

5

Beta strand

109 – 114

6

Beta strand

118 – 123

6

Beta strand

128 – 130

3

Helix

132 – 142

11

Beta strand

146 – 155

10

Beta strand

161 – 165

5

Helix

166 – 174

9

Beta strand

177 – 183

7

Helix

184 – 193

10

Helix

195 – 197

3

Helix

198 – 211

14

Sequences

	Sequence		Length	Mass (Da)
	P08870-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 963A8BE3DD9113B0	FASTA	213	23,562
	10 20 30 40 50 60 MKPYQRQFIE FALNKQVLKF GEFTLKSGRK SPYFFNAGLF NTGRDLALLG RFYAEALVDS 70 80 90 100 110 120 GIEFDLLFGP AYKGIPIATT TAVALAEHHD KDLPYCFNRK EAKDHGEGGS LVGSALQGRV 130 140 150 160 170 180 MLVDDVITAG TAIRESMEII QAHGATLAGV LISLDRQERG RGEISAIQEV ERDYGCKVIS 190 200 210 IITLKDLIAY LEEKPDMAEH LAAVRAYREE FGV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure and crystallization of orotate phosphoribosyltransferase from Salmonella typhimurium." Scapin G., Sacchettini J.C., Dessen A., Bhatia M., Grubmeyer C. J. Mol. Biol. 230:1304-1308(1993) [PubMed: 8487307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"Cloning and characterization of the pyrE gene and of PyrE::Mud1 (Ap lac) fusions from Salmonella typhimurium." Neuhard J., Stauning E., Kelln R.A. Eur. J. Biochem. 146:597-603(1985) [PubMed: 3882417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
[4]	"Kinetic mechanism of orotate phosphoribosyltransferase from Salmonella typhimurium." Bhatia M.B., Vinitsky A., Grubmeyer C. Biochemistry 29:10480-10487(1990) [PubMed: 2271660] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-17, FUNCTION, KINETIC MECHANISM.
[5]	"The role of divalent magnesium in activating the reaction catalyzed by orotate phosphoribosyltransferase." Bhatia M.B., Grubmeyer C. Arch. Biochem. Biophys. 303:321-325(1993) [PubMed: 7685580] [Abstract] Cited for: COFACTOR.
[6]	"Active site lysines in orotate phosphoribosyltransferase." Grubmeyer C., Segura E., Dorfman R.H. J. Biol. Chem. 268:20299-20304(1993) [PubMed: 8376388] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-29 AND 100-108.
[7]	"Locations and functional roles of conserved lysine residues in Salmonella typhimurium orotate phosphoribosyltransferase." Ozturk D.H., Dorfman R.H., Scapin G., Sacchettini J.C., Grubmeyer C. Biochemistry 34:10755-10763(1995) [PubMed: 7545005] [Abstract] Cited for: MUTAGENESIS, PARTIAL PROTEIN SEQUENCE.
[8]	"Structure and function of Salmonella typhimurium orotate phosphoribosyltransferase: protein complementation reveals shared active sites." Ozturk D.H., Dorfman R.H., Scapin G., Sacchettini J.C., Grubmeyer C. Biochemistry 34:10764-10770(1995) [PubMed: 7545006] [Abstract] Cited for: SUBUNIT, BINDING SITES.
[9]	"Crystal structure of orotate phosphoribosyltransferase." Scapin G., Grubmeyer C., Sacchettini J.C. Biochemistry 33:1287-1294(1994) [PubMed: 8312245] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH OMP.
[10]	"The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate." Scapin G., Ozturk D.H., Grubmeyer C., Sacchettini J.C. Biochemistry 34:10744-10754(1995) [PubMed: 7545004] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH OROTATE AND PRPP.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z19547 Genomic DNA. Translation: CAA79607.1.
AE006468 Genomic DNA. Translation: AAL22592.1.

PIR

S32801.

RefSeq

NP_462633.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LH0	X-ray	2.00	A/B	1-213	[»]
1OPR	X-ray	2.30	A	1-213	[»]
1STO	X-ray	2.60	A	1-213	[»]

ModBase

Search...

Proteomic databases

PRIDE

P08870.

Genome annotation databases

GeneID

1255257.

GenomeReviews

Gene locus STM3733 in contig AE006468_GR.

KEGG

stm:STM3733.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P08870.

OMA

YKGITLA.

Enzyme and pathway databases

BioCyc

STYP99287:STM3733-MON.

BRENDA

2.4.2.10. 2.

Family and domain databases

HAMAP

MF_01208.
[Tree]

InterPro

IPR004467. Or_phspho_trans.
IPR002375. Pr/py_Pribosyl_transf_CS.
IPR000836. PRibTrfase.
[Graphical view]

Pfam

PF00156. Pribosyltran. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00336. pyrE. 1 hit.

PROSITE

PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PYRE_SALTY

Accession

Primary (citable) accession number: P08870

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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