Q65JU9 (PYRC_BACLD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	BLi01770, BL02274

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220_B
Cofactor	Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220_B
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220_B
Subunit structure	Homodimer By similarity. HAMAP MF_00220_B
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: 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 – 428	428	Dihydroorotase HAMAP MF_00220_B		PRO_1000024078
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

Sequences

	Sequence		Length	Mass (Da)
	Q65JU9 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: A06BDBBBFDBB1F02	FASTA	428	46,684
	10 20 30 40 50 60 MSYLIKNGFM LDEKGEKVQR DIRVEGDAIS EIGSLEAASG ETVIDADGLF VSPGLVDLHV 70 80 90 100 110 120 HFREPGGEKK ETIETGAKAA ARGGFTTVAA MPNTRPVPDT KEQMEWLVNR IDETASVRVL 130 140 150 160 170 180 PYASITIRQT GREMTDFEGL KDAGAFAFTD DGVGVQTAGM MYEAMKKAAS INKAIVAHCE 190 200 210 220 230 240 DNSLIYGGSV HDGEFAKANG LNGIPSVCEA VHIARDVLLA EAAGCHYHVC HISTKESVRV 250 260 270 280 290 300 VRDAKKAGIR VTAEVTPHHL LLSDSDIPGL DTNYKMNPPL RSPEDREALL EGLRDGTIDF 310 320 330 340 350 360 IATDHAPHTE EEKQQTMSLA PFGIVGLETA FPLLYTHFVK TGKWTLKQLH DYMTVKPCEA 370 380 390 400 410 420 FGLPYGKLEA GRSADITLID LEREEKIDKS TFLSKGKNTP FDGISCFGWP AMTMAKGKLV YQEGRLVK

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU23305.1. AE017333 Genomic DNA. Translation: AAU40665.1.
RefSeq	YP_078943.1. NC_006270.3. YP_091358.1. NC_006322.1.
3D structure databases
HSSP	HSSP built from PDB template 1XRT based on UniProtKB O66990.
ProteinModelPortal	Q65JU9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65JU9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000054267; EBBACP00000052798; EBBACG00000054258. EBBACT00000061963; EBBACP00000060396; EBBACG00000061954.
GeneID	3030921. 3097653.
GenomeReviews	Gene locus BLi01770 in contig AE017333_GR. Gene locus BL02274 in contig CP000002_GR.
KEGG	bld:BLi01770. bli:BL02274.
NMPDR	fig|279010.5.peg.1712.
PATRIC	18949141. VBIBacLic203714_1774.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
GeneTree	EBGT00050000001626.
HOGENOM	HBG724623.
OMA	CDVHPVG.
PhylomeDB	Q65JU9.
ProtClustDB	CLSK887279.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI01770-MONOMER. BLIC279010:BL02274-MONOMER.
Family and domain databases
HAMAP	MF_00220_B. PyrC_type2_B. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR004722. DHOase. IPR002195. Dihydroorotase_CS. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
KO	K01465.
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
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_BACLD

Accession

Primary (citable) accession number: Q65JU9
Secondary accession number(s): Q62VA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program