Reviewed, UniProtKB/Swiss-Prot P25995 (PYRC_BACSU)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	BSU15500

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6. HAMAP MF_00220
Subunit structure	Homodimer. HAMAP MF_00220
Sequence similarities	Belongs to the DHOase family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	dihydroorotase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 428	428	Dihydroorotase HAMAP MF_00220		PRO_0000147229
Sites
	Metal binding	59	1	Zinc 1 By similarity
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	141	1	Zinc 1; via carbamate group By similarity
	Metal binding	141	1	Zinc 2; via carbamate group By similarity
	Metal binding	178	1	Zinc 2 By similarity
	Metal binding	231	1	Zinc 2 By similarity
	Metal binding	304	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	141	1	N6-carboxylysine By similarity
Experimental info
	Sequence conflict	81	1	A → G in AAA21268. Ref.1
	Sequence conflict	220 – 222	3	AEA → LG in AAA21268. Ref.1
	Sequence conflict	323 – 351	29	GIVGL…KQLID → RNCRLRNSIPASLHTLCQKW QLVTEAADLT in AAA21268. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25995-1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 86739BFB81D395AB	FASTA	428	46,533
	10 20 30 40 50 60 MSYLIKNGWI LNENGEKTQA DIRVTGETIT AIGKLDATDN ETVIDAKGLL VSPGFVDLHV 70 80 90 100 110 120 HFREPGGEKK ETIETGAKAA ARGGYTTVAA MPNTRPVPDT KEQMEWVQNR IKETSCVRVL 130 140 150 160 170 180 PYASITIRQI GDEMTNFEAL KEAGAFAFTD DGVGIQTAGM MYEAMKRAAA IDKAIVAHCE 190 200 210 220 230 240 DNSLIYGGSV HEGTFSKANG LNGIPSVCES VHIARDVLLA EAANCHYHVC HISTKESVRV 250 260 270 280 290 300 VRDAKKAGIR VTAEVSPHHL LLCDEDIPGL DTNYKMNPPL RSPEDRAALI EGLLDGTIDF 310 320 330 340 350 360 IATDHAPHTE EEKNTEMKLA PFGIVGLETA FPLLYTHFVK NGSWSLKQLI DYMTIKPCEA 370 380 390 400 410 420 FGLPYGTLQT GQAADITLID LEKEAVIDKE TFLSKGKNTP FNGISCTGWP VATIAAGKLA YEEGRLVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon." Quinn C.L., Stephenson B.T., Switzer R.L. J. Biol. Chem. 266:9113-9127(1991) [PubMed: 1709162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 0:0-0(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M59757 Genomic DNA. Translation: AAA21268.1. AL009126 Genomic DNA. Translation: CAB13424.2.
PIR	DEBSO. D39845.
RefSeq	NP_389433.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M38.972.
Genome annotation databases
GeneID	937095.
GenomeReviews	Gene locus BSU15500 in contig AL009126_GR.
KEGG	bsu:BSU15500.
NMPDR	fig|224308.1.peg.1552.
Organism-specific databases
SubtiList	BG10714. pyrC. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P25995.
OMA	P25995. ERANFTI.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1552-MON.
BRENDA	3.5.2.3. 150.
Family and domain databases
HAMAP	MF_00220. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR004722. DHOmult. IPR002195. Dihydroorotase_CS. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
ProDom	PD000518. DHOase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00857. pyrC_multi. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRC_BACSU

Accession

Primary (citable) accession number: P25995

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	June 16, 2009
Last modified:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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