P31301 (PYRC_USTMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3

Gene names

Name:	PYR3
ORF Names:	UM01521

Organism

Ustilago maydis (strain 521 / FGSC 9021) (Smut fungus)

Taxonomic identifier

237631 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago

Protein attributes

Sequence length	394 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.
Induction	By N-carbamoyl-L-aspartate.
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 electronic annotation. Source: UniProtKB-KW
Molecular function	dihydroorotase activity Inferred from electronic annotation. Source: EC 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 – 394	394	Dihydroorotase		PRO_0000147291
Sites
	Metal binding	15	1	Zinc 1 By similarity
	Metal binding	17	1	Zinc 1 By similarity
	Metal binding	98	1	Zinc 1; via carbamate group By similarity
	Metal binding	98	1	Zinc 2; via carbamate group By similarity
	Metal binding	135	1	Zinc 2 By similarity
	Metal binding	175	1	Zinc 2 By similarity
	Metal binding	245	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	98	1	N6-carboxylysine By similarity
Experimental info
	Sequence conflict	12	1	A → G in CAA44866. Ref.1
	Sequence conflict	63 – 65	3	RAL → AAV in CAA44866. Ref.1
	Sequence conflict	88 – 89	2	KA → EG in CAA44866. Ref.1
	Sequence conflict	162	1	I → M in CAA44866. Ref.1
	Sequence conflict	270	1	A → D in CAA44866. Ref.1
	Sequence conflict	289	1	G → A in CAA44866. Ref.1
	Sequence conflict	300 – 301	2	CA → WP in CAA44866. Ref.1
	Sequence conflict	348	1	S → C in CAA44866. Ref.1
	Sequence conflict	373	1	A → R in CAA44866. Ref.1
	Sequence conflict	384 – 390	7	GKCLGWE → VSAG in CAA44866. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P31301 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: 400DFA2BE435DFB8	FASTA	394	42,837
	10 20 30 40 50 60 MSVQEITIPA PADFHVHLRQ GKMSELVTPH VAEGGVSLAY VMPNLVPPIT STQQAMEYLE 70 80 90 100 110 120 RLRALAPQTM FVGTLYLSPD LTPAEIAKAA QNGVRGVKSY PRGVTTNSDS GIEDYETYYP 130 140 150 160 170 180 IFEEMQKHDM VLNLHGELPS NADAGICVLN AEEKFLTHLF KIHGEFPKLK IVLEHATTRK 190 200 210 220 230 240 AVEAVKQCGD TVGCTITPHH LELIVDDWAG KPLNFCKPVA KYPDDRQALR DVIRQGHPRF 250 260 270 280 290 300 FLGSDSAPHP LANKYPSAVT HGAPGTKASA SGSDHLEATG VVSCGCAAGV YTSSILVPLC 310 320 330 340 350 360 ATLLEAFGAL DQLANYVSIN GRNFYGYNDD QHAKHGSIKL RKVRSRSSIS PAAATVPAVY 370 380 390 VHPEFREVPD SDASKVQVVP FWAGKCLGWE IVRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Ustilago maydis pyr3 gene: sequence and transcriptional analysis." Spanos A., Kanuga N., Holden D.W., Banks G.R. Gene 117:73-79(1992) [PubMed: 1353740] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 521 / FGSC 9021.
[2]	"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W. Nature 444:97-101(2006) [PubMed: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521 / FGSC 9021.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X63181 Genomic DNA. Translation: CAA44866.1. AACP01000056 Genomic DNA. Translation: EAK82576.1.
PIR	DEUSO. JQ1667.
RefSeq	XP_757668.1. XM_752575.1.
3D structure databases
ProteinModelPortal	P31301.
ModBase	Search...
Protein-protein interaction databases
STRING	P31301.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	UM01521T0; UM01521P0; UM01521.
GeneID	3629607.
KEGG	uma:UM01521.1.
Phylogenomic databases
eggNOG	fuNOG04770.
HOGENOM	HBG628648.
OMA	CLPVAKR.
OrthoDB	EOG4HTD20.
Enzyme and pathway databases
BRENDA	3.5.2.3. 6587.
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. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRC_USTMA

Accession

Primary (citable) accession number: P31301
Secondary accession number(s): Q4PEE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	December 12, 2006
Last modified:	December 14, 2011
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program