Reviewed, UniProtKB/Swiss-Prot Q8NQ39 (PYRC_CORGL)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	Cgl1611, cg1815

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	447 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 By similarity.
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 – 447	447	Dihydroorotase HAMAP MF_00220		PRO_0000147232
Sites
	Metal binding	73	1	Zinc 1 By similarity
	Metal binding	75	1	Zinc 1 By similarity
	Metal binding	194	1	Zinc 2 By similarity
	Metal binding	247	1	Zinc 2 By similarity
	Metal binding	320	1	Zinc 1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NQ39-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 5AAD2377CF5F6572	FASTA	447	47,827
	10 20 30 40 50 60 MVDSNTQYPE TGALAPAPAD SLLISNVLVY GEGEPTNVFV KDGVIAAIGG THEADRTIDG 70 80 90 100 110 120 NGGVLLPGFV DMHVHLREPG REDTETIATG SAAAAKGGFT AVFTMANTTP VMDQPVIAES 130 140 150 160 170 180 VWFKGQNIGL CDVHPVGSIT KGLEGKELTE FGMMARSEAK VRMFSDDGKC VDDPQVMRRA 190 200 210 220 230 240 LEYAKGMDVL IAQHAEDHRL TEGASAHEGE NAARLGLRGW PRVAEESIVV RDAIMARDYG 250 260 270 280 290 300 NRVHICHAST EGTVELLRWA KSQGIPITAE VTPHHLTLTD ERLETYDAVN KVNPPLRESR 310 320 330 340 350 360 DAEALKKALL DGTIDVVATD HAPHGSEDKC CEFENAKPGM LGLETSLSII VDTFVATGLA 370 380 390 400 410 420 DWRFVARVMS ERPAEITRLP GQGRPIAEGE PANLAIVDPG KTWTASGADF ASKAENTPFE 430 440 GQEFSAKVTH TVLRGKVTCA DGVAQNA

References

[1]

"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000036 Genomic DNA. Translation: BAB99004.1. BX927152 Genomic DNA. Translation: CAF21620.1.
RefSeq	NP_600825.1. YP_225896.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1019579. 3343550.
GenomeReviews	Gene locus Cgl1611 in contig BA000036_GR. Gene locus cg1815 in contig BX927147_GR.
KEGG	cgb:cg1815. cgl:NCgl1549.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8NQ39.
OMA	Q8NQ39. CDVHPVG.
Enzyme and pathway databases
BioCyc	CGLU196627-1:CG1815-MON.
BRENDA	3.5.2.3. 812.
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_CORGL

Accession

Primary (citable) accession number: Q8NQ39

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2003
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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