Q92AH1 (PYRC_LISIN) 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:	lin1951

Organism

Listeria innocua [Complete proteome] [HAMAP]

Taxonomic identifier

1642 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	426 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 – 426	426	Dihydroorotase HAMAP MF_00220_B		PRO_0000147239
Sites
	Metal binding	58	1	Zinc 1 By similarity
	Metal binding	60	1	Zinc 1 By similarity
	Metal binding	140	1	Zinc 1; via carbamate group By similarity
	Metal binding	140	1	Zinc 2; via carbamate group By similarity
	Metal binding	177	1	Zinc 2 By similarity
	Metal binding	230	1	Zinc 2 By similarity
	Metal binding	303	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	140	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92AH1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: D8591D40D111FED3	FASTA	426	46,201
	10 20 30 40 50 60 MYVLKNGQVL NESGELENKD VLIQNGKVNL IADSIEVTSG EEFDATGKLI APGFIDVHVH 70 80 90 100 110 120 LREPGGEHKE TILTGTKAAA RGGYTTICSM PNTKPVPDSK EVMNSLQAKI KETAEVRVLP 130 140 150 160 170 180 YASITTSLGT DELVDFEALK EAGAFAFTDD GVGVQLAGTM YEAMKRAAAL DMAIVAHCED 190 200 210 220 230 240 NSLIYGGVVH DGIFAEKEGL KGIPNIAESV QIARDVLLAE AAGCHYHVCH ISTKESVRVV 250 260 270 280 290 300 RDAKRAGIRV TAEVSPHHLI LDEEDIPGND GNWKMNPPLR SKEDRAALLE GLLDGTIDFI 310 320 330 340 350 360 ATDHAPHAAE EKNVPMEQAA FGIVGLETAF PLLYTHFVKT NEWTLKQLID WMTVKPAECF 370 380 390 400 410 420 KLPYGKLEEG AVADIVVLDL EKEATIDPAT FYSKGKNTPF VGETCIGWPV ATFAEGELVY NEGENK

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIP 11262 / Serovar 6a.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL596170 Genomic DNA. Translation: CAC97181.1.
PIR	AE1676.
RefSeq	NP_471285.1. NC_003212.1.
3D structure databases
ProteinModelPortal	Q92AH1.
ModBase	Search...
Protein family/group databases
MEROPS	M38.972.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1130647.
GenomeReviews	Gene locus lin1951 in contig AL592022_GR.
KEGG	lin:lin1951.
NMPDR	fig|272626.1.peg.1938.
PATRIC	20300713. VBILisInn102668_1995.
Organism-specific databases
GenoList	LIN1951.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG724623.
OMA	GIFAEKE.
ProtClustDB	PRK09357.
Enzyme and pathway databases
BioCyc	LINN272626:LIN1951-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_LISIN

Accession

Primary (citable) accession number: Q92AH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program