Q9UTI0 (PYRC_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable dihydroorotase
Short name=DHOase
EC=3.5.2.3

Gene names

Name:	ura2
ORF Names:	SPAC16.03c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Sequence similarities	Belongs to the DHOase family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Molecular function	dihydroorotase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 337	337	Probable dihydroorotase		PRO_0000147290
Sites
	Metal binding	12	1	Zinc 1 By similarity
	Metal binding	14	1	Zinc 1 By similarity
	Metal binding	95	1	Zinc 1; via carbamate group By similarity
	Metal binding	95	1	Zinc 2; via carbamate group By similarity
	Metal binding	132	1	Zinc 2 By similarity
	Metal binding	170	1	Zinc 2 By similarity
	Metal binding	240	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	95	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9UTI0 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 1E0D00F457A6FA02	FASTA	337	37,552
	10 20 30 40 50 60 MSLKIPGLAD MHVHLRQDNM LKAVVPTVAE GGVSVAYVMP NLIPPITTVD ACLQYKKEIE 70 80 90 100 110 120 QLDSKTTYLM SLYLSPETTP EVIYEAAKKG IRGVKSYPKG ATTNSESGVE SYEPFYPTFA 130 140 150 160 170 180 AMQETGMILN IHGEVPPSKD NTVFTAEPKF LPTLLDLHQR FPKLKIVLEH CTTADAVEAV 190 200 210 220 230 240 KACGESVAGT ITAHHLYLTQ KDWQDDPYCF CKPVAKTERD RRALIEAATS KNPKFFFGSD 250 260 270 280 290 300 SAPHPRSSKL KTPPAAGVFT QPFAASYLAE VFDKEGRLDA LKDFACIFGR KFYCIPLDFK 310 320 330 ESNIVLKKES FRVPESVAND LVPFHPNEVL QWHCSWE

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB57401.1.
PIR	T37731.
RefSeq	NP_594571.1. NM_001020000.1.
3D structure databases
ProteinModelPortal	Q9UTI0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UTI0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC16.03c.1; SPAC16.03c.1:pep; SPAC16.03c.
GeneID	2542745.
GenomeReviews	Gene locus ura2 in contig CU329670_GR.
KEGG	spo:SPAC16.03c.
NMPDR	fig|4896.1.peg.4541.
Organism-specific databases
GeneDB_Spombe	SPAC16.03c.
Phylogenomic databases
eggNOG	fuNOG04770.
GeneTree	EFGT00050000006781.
HOGENOM	HBG628648.
OMA	CLPVAKR.
OrthoDB	EOG4HTD20.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002667-MONOMER.
Gene expression databases
ArrayExpress	Q9UTI0.
Family and domain databases
InterPro	IPR006992. Amidohydro_2. IPR004721. DHOdimr. IPR002195. Dihydroorotase_CS. [Graphical view]
KO	K01465.
Pfam	PF04909. Amidohydro_2. 1 hit. [Graphical view]
PIRSF	PIRSF001237. DHOdimr. 1 hit.
TIGRFAMs	TIGR00856. PyrC_dimer. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. False negative. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRC_SCHPO

Accession

Primary (citable) accession number: Q9UTI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program