Q81WF6 (PYRE_BACAN) Reviewed, UniProtKB/Swiss-Prot

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:	BA_4021, GBAA_4021, BAS3733

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
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. HAMAP MF_01208
Catalytic activity	Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01208
Cofactor	Magnesium By similarity. HAMAP MF_01208
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP MF_01208
Subunit structure	Homodimer By similarity. HAMAP MF_01208
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 Reference proteome
Gene Ontology (GO)
Biological process	nucleoside metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	orotate phosphoribosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 210

210

Orotate phosphoribosyltransferase HAMAP MF_01208

PRO_0000110665

Regions

Region

120 – 128

9

5-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site

94

1

5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity

Binding site

98

1

5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity

Binding site

100

1

5-phosphoribose 1-diphosphate; shared with dimeric partner By similarity

Binding site

124

1

Orotate By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

210

Helix Strand Turn

Details...

Helix

1 – 11

11

Beta strand

15 – 17

3

Beta strand

30 – 35

6

Helix

37 – 42

6

Helix

44 – 51

8

Helix

55 – 61

7

Beta strand

67 – 69

3

Helix

77 – 86

10

Beta strand

115 – 123

9

Helix

129 – 138

10

Beta strand

147 – 151

5

Helix

159 – 163

5

Beta strand

169 – 172

4

Helix

174 – 183

10

Helix

190 – 200

11

Helix

205 – 209

5

Sequences

	Sequence		Length	Mass (Da)
	Q81WF6 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 0FB8FABEBB5E54B6	FASTA	210	22,714
	10 20 30 40 50 60 MKKEIASHLL EIGAVFLQPN DPFTWSSGMK SPIYCDNRLT LSYPKVRQTI AAGLEELIKE 70 80 90 100 110 120 HFPTVEVIAG TATAGIAHAA WVSDRMDLPM CYVRSKAKGH GKGNQIEGKA EKGQKVVVVE 130 140 150 160 170 180 DLISTGGSAI TCVEALREAG CEVLGIVSIF TYELEAGKEK LEAANVASYS LSDYSALTEV 190 200 210 AAEKGIIGQA ETKKLQEWRK NPADEAWITA

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE016879 Genomic DNA. Translation: AAP27748.1.
AE017334 Genomic DNA. Translation: AAT33138.1.
AE017225 Genomic DNA. Translation: AAT56035.1.

RefSeq

NP_846262.1. NC_003997.3.
YP_020663.1. NC_007530.2.
YP_029984.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3M3H	X-ray	1.75	A	1-210	[»]
3OSC	X-ray	2.65	A/B/C	1-210	[»]

ProteinModelPortal

Q81WF6.

SMR

Q81WF6. Positions 1-204.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000008120; EBBACP00000007876; EBBACG00000008112.
EBBACT00000014908; EBBACP00000014529; EBBACG00000014900.
EBBACT00000022989; EBBACP00000022474; EBBACG00000022980.

GeneID

1086652.
2815305.
2853071.

GenomeReviews

Gene locus BA_4021 in contig AE016879_GR.
Gene locus BAS3733 in contig AE017225_GR.
Gene locus GBAA_4021 in contig AE017334_GR.

KEGG

ban:BA_4021.
bar:GBAA_4021.
bat:BAS3733.

TIGR

BA_4021.
GBAA_4021.

Phylogenomic databases

GeneTree

EBGT00050000002725.

HOGENOM

HBG404341.

OMA

LPMTYVR.

ProtClustDB

PRK00455.

Enzyme and pathway databases

BioCyc

BANT260799:BAS3733-MONOMER.
BANT261594:GBAA4021-MONOMER.

Family and domain databases

HAMAP

MF_01208. PyrE.
[Tree]

InterPro

IPR004467. Or_phspho_trans_clade-1.
IPR023031. Orotate_PribosylTferase.
IPR000836. PRibTrfase.
[Graphical view]

KO

K00762.

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_BACAN

Accession

Primary (citable) accession number: Q81WF6
Secondary accession number(s): Q6HUK4, Q6KNT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	November 16, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program