Reviewed, UniProtKB/Swiss-Prot P03962 (PYRF_YEAST)

Names and origin

Protein names

Recommended name:
    Orotidine 5'-phosphate decarboxylase
    EC=4.1.1.23
Alternative name(s):
    OMP decarboxylase
      Short name=OMPdecase
      Short name=OMPDCase
    Uridine 5'-monophosphate synthase
      Short name=UMP synthase

Gene names

Name:	URA3
Ordered Locus Names:	YEL021W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Orotidine 5'-phosphate = UMP + CO2.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Sequence similarities	Belongs to the OMP decarboxylase family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Molecular function	Decarboxylase Lyase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from mutant phenotype. Source: SGD UMP biosynthetic process Inferred from direct assay. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD soluble fraction Inferred from direct assay. Source: SGD
Molecular function	orotidine-5'-phosphate decarboxylase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RNQ1	P25367	1	EBI-14397,EBI-21708

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 267

267

Orotidine 5'-phosphate decarboxylase

PRO_0000134692

Regions

Region

59 – 61

3

Substrate binding

Region

91 – 100

10

Substrate binding

Sites

Active site

93

1

Proton donor

Binding site

37

1

Substrate

Binding site

217

1

Substrate

Binding site

235

1

Substrate

Amino acid modifications

Modified residue

219

1

Phosphothreonine Ref.8

Modified residue

228

1

Phosphoserine Ref.8

Cross-link

93

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Cross-link

209

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Cross-link

253

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Natural variations

Natural variant

160

1

A → S in strain: +D4.

Experimental info

Mutagenesis

59

1

K → A: Reduces Kcat 100-fold. Reduces substrate affinity 900-fold. Ref.6

Mutagenesis

91

1

D → A: Reduces activity over 100000-fold. Ref.6

Mutagenesis

93

1

K → A: Reduces activity over 100000-fold. Ref.6

Mutagenesis

96

1

D → A: Reduces Kcat over 100000-fold. Reduces substrate affinity 11-fold. Ref.6

Mutagenesis

215

1

Q → A: No effect. Ref.6

Sequence conflict

71 – 73

3

EGT → RIR in AAA35199. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

267

Helix Strand Turn

Details...

Helix

6 – 12

7

Helix

16 – 28

13

Beta strand

32 – 35

4

Helix

41 – 51

11

Helix

52 – 54

3

Beta strand

56 – 60

5

Helix

62 – 64

3

Turn

70 – 73

4

Helix

74 – 84

11

Beta strand

87 – 94

8

Helix

98 – 106

9

Turn

108 – 110

3

Helix

112 – 115

4

Beta strand

117 – 123

7

Helix

128 – 140

13

Beta strand

146 – 150

5

Helix

162 – 172

11

Turn

176 – 178

3

Beta strand

179 – 183

5

Turn

191 – 194

4

Beta strand

198 – 201

4

Turn

208 – 210

3

Turn

213 – 215

3

Helix

220 – 225

6

Beta strand

230 – 233

4

Helix

235 – 237

3

Helix

244 – 263

20

Sequences

	Sequence		Length	Mass (Da)
	P03962-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: D63EF9877BD0F984	FASTA	267	29,240
	10 20 30 40 50 60 MSKATYKERA ATHPSPVAAK LFNIMHEKQT NLCASLDVRT TKELLELVEA LGPKICLLKT 70 80 90 100 110 120 HVDILTDFSM EGTVKPLKAL SAKYNFLLFE DRKFADIGNT VKLQYSAGVY RIAEWADITN 130 140 150 160 170 180 AHGVVGPGIV SGLKQAAEEV TKEPRGLLML AELSCKGSLA TGEYTKGTVD IAKSDKDFVI 190 200 210 220 230 240 GFIAQRDMGG RDEGYDWLIM TPGVGLDDKG DALGQQYRTV DDVVSTGSDI IIVGRGLFAK 250 260 GRDAKVEGER YRKAGWEAYL RRCGQQN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and function of the yeast URA3 gene: expression in Escherichia coli." Rose M., Grisafi P., Botstein D. Gene 29:113-124(1984) [PubMed: 6092217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: +D4 and ATCC 28383 / FL100 / VTT C-80102.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Holtz A., Lou Y. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Transcription terminator-like element within a Saccharomyces cerevisiae promoter region." Yarger J.G., Armilei G., Gorman M.C. Mol. Cell. Biol. 6:1095-1101(1986) [PubMed: 3023868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
[5]	"Structure and function of the yeast URA3 gene. Differentially regulated expression of hybrid beta-galactosidase from overlapping coding sequences in yeast." Rose M., Botstein D. J. Mol. Biol. 170:883-904(1983) [PubMed: 6315953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
[6]	"Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase." Miller B.G., Snider M.J., Wolfenden R., Short S.A. J. Biol. Chem. 276:15174-15176(2001) [PubMed: 11278904] [Abstract] Cited for: MUTAGENESIS OF LYS-59; ASP-91; LYS-93; ASP-96 AND GLN-215.
[7]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-93; LYS-209 AND LYS-253, MASS SPECTROMETRY.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-219 AND SER-228, MASS SPECTROMETRY.
[9]	"Anatomy of a proficient enzyme: the structure of orotidine 5'-monophosphate decarboxylase in the presence and absence of a potential transition state analog." Miller B.G., Hassell A.M., Wolfenden R., Milburn M.V., Short S.A. Proc. Natl. Acad. Sci. U.S.A. 97:2011-2016(2000) [PubMed: 10681417] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH TRANSITION STATE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

K02206 Genomic DNA. Translation: AAA34824.1.
K02207 Genomic DNA. Translation: AAA34825.1.
U18530 Genomic DNA. Translation: AAB64498.1.
U89671 Genomic DNA. Translation: AAB49978.1.
M12926 Genomic DNA. Translation: AAA35199.1.
X00191 Genomic DNA. Translation: CAA25010.1. Different initiation.
U89927 Genomic DNA. Translation: AAB64383.1.
U63018 Genomic DNA. Translation: AAC53678.1.

PIR

DEBYOP. A01082.
DCBYOF. S05735.

RefSeq

NP_010893.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DQW	X-ray	2.10	A/B/C/D	3-266	[»]
1DQX	X-ray	2.40	A/B/C/D	3-266	[»]
3GDK	X-ray	2.00	A/B/C/D	1-267	[»]
3GDL	X-ray	1.65	A/B	1-267	[»]
3GDR	X-ray	1.90	A/B/C/D	1-267	[»]
3GDT	X-ray	1.60	A/B/C/D	1-267	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6576N.

IntAct

P03962. 2 interactions.

STRING

P03962.

Proteomic databases

PeptideAtlas

P03962.

PRIDE

P03962.

Genome annotation databases

Ensembl

YEL021W; YEL021W; YEL021W; Saccharomyces cerevisiae. [Genome view]

GeneID

856692.

KEGG

sce:YEL021W.

NMPDR

fig|4932.3.peg.1947.

Organism-specific databases

CYGD

YEL021w.

SGD

S000000747. URA3.

Phylogenomic databases

HOGENOM

HBG326699.

OMA

DITNAHG.

OrthoDB

EOG99S7Q4.

Enzyme and pathway databases

BRENDA

4.1.1.23. 250.

Gene expression databases

ArrayExpress

P03962.

Genevestigator

P03962.

GermOnline

YEL021W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR014732. OMPdecase_1_core.
IPR018089. OMPdecase_AS.
IPR001754. OMPdecase_core.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF00215. OMPdecase. 1 hit.
[Graphical view]

PROSITE

PS00156. OMPDECASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

982739.

Entry information

Entry name

PYRF_YEAST

Accession

Primary (citable) accession number: P03962

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	February 1, 1995
Last modified:	December 15, 2009
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)