A8FD15 (PYRC_BACP2) 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:	BPUM_1449

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]

Taxonomic identifier

315750 [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_1000058653
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)
	A8FD15 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: B50A9168280389E2	FASTA	428	46,993
	10 20 30 40 50 60 MSYLIKNGFI LTSTGEKVQQ DIRVEGEVIQ AIGHLEREDG EEVIDAKGLF VSPGLIDLHV 70 80 90 100 110 120 HLREPGGEKK ETIETGSKAA ARGGYTTIAA MPNTRPVPDT KEQMEWLMNR IEETSSVRVL 130 140 150 160 170 180 PYASITTRQI GEEMTDFAAL KEAGAFAFTD DGVGIQTAGM MYEAMKKAAS LDQAIVAHCE 190 200 210 220 230 240 DNSLIYGGCV HEGEFSKANG LNGIPSICES VHIARDVLLA EAANCHYHVC HISTKESVRV 250 260 270 280 290 300 VRDAKKAGIR VTAEVSPHHL LLCDADIPGL DTNYKMNPPL RGKEDREALI EGLLDGTIDF 310 320 330 340 350 360 IATDHAPHTE EEKNETMQRA PFGIVGLETA FPLLYTRFVK TGEWTLKELV DYMTIKPAEA 370 380 390 400 410 420 FSLPYGKLEK GQIADITLID LNKEMAIDKK SFLSKGQNTP FDKLTVSGWP VMTLASGKVV YEEGRLVK

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SAFR-032.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000813 Genomic DNA. Translation: ABV62132.1.
RefSeq	YP_001486692.1. NC_009848.1.
3D structure databases
ProteinModelPortal	A8FD15.
ModBase	Search...
Protein-protein interaction databases
STRING	A8FD15.
Protein family/group databases
MEROPS	M38.972.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000065762; EBBACP00000064095; EBBACG00000065753.
GeneID	5620716.
GenomeReviews	Gene locus BPUM_1449 in contig CP000813_GR.
KEGG	bpu:BPUM_1449.
PATRIC	18966735. VBIBacPum16546_1464.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
GeneTree	EBGT00050000001626.
HOGENOM	HBG724623.
OMA	CDVHPVG.
ProtClustDB	CLSK887279.
Enzyme and pathway databases
BioCyc	BPUM315750:BPUM_1449-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_BACP2

Accession

Primary (citable) accession number: A8FD15

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program