Q047M6 (PYRC_LACDB) 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:	LBUL_1952

Organism

Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365) [Complete proteome] [HAMAP]

Taxonomic identifier

321956 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus delbrueckii › Lactobacillus delbrueckii subsp. bulgaricus

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP-Rule MF_00220
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP-Rule 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	'de novo' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 425	425	Dihydroorotase HAMAP-Rule MF_00220		PRO_1000024088
Sites
	Metal binding	56	1	Zinc 1 By similarity
	Metal binding	58	1	Zinc 1 By similarity
	Metal binding	138	1	Zinc 1; via carbamate group By similarity
	Metal binding	138	1	Zinc 2; via carbamate group By similarity
	Metal binding	175	1	Zinc 2 By similarity
	Metal binding	228	1	Zinc 2 By similarity
	Metal binding	301	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	138	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q047M6 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: C9EF52A40DE91371	FASTA	425	46,301
	10 20 30 40 50 60 MQTVIKNGTV YQNGRLIHAD VLIEDQKIKA IGTDLTGDKV IDATGKLVSP GLVDVHVHYR 70 80 90 100 110 120 DPGQTYKEDI ETGSKAAAHG GFTTVGAMPN VTPVPDTPDL MKKMVQENKQ KGIVHIFQYG 130 140 150 160 170 180 PITKNETTDE LPDYAALKKA GAFALSNDGH GVQTAQTMYL AMQEAKKNDL IVAAHAQDDS 190 200 210 220 230 240 LFNHGIVNEG EKAKELNLPP VTELAETTQI ARDLLLAEKT GVHYHICHVS TKTSVELVRI 250 260 270 280 290 300 AKACGINVTC EAAPHHLLLT EDDIPKDNGY YKMNPPLRSK EDQVALLVGL LDGTIDLIAT 310 320 330 340 350 360 DHAPHAKQEK QGGMQNAAFG ITGSETAFST LYTKFVKEDK VFTLEQLLSW LSDQPAKVFG 370 380 390 400 410 420 LKKAGVLEPG CPADVAIFDL EHETELKEKN YQSKGINTPF TGQKIYGATV MTMVDGEVVY QRGEK

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-365.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000412 Genomic DNA. Translation: ABJ59346.1.
RefSeq	YP_813784.1. NC_008529.1.
3D structure databases
ProteinModelPortal	Q047M6.
ModBase	Search...
Protein-protein interaction databases
STRING	321956.LBUL_1952.
Protein family/group databases
MEROPS	M38.972.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABJ59346; ABJ59346; LBUL_1952.
GeneID	4434751.
KEGG	lbu:LBUL_1952.
PATRIC	22223769. VBILacDel70259_1868.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HOG000219142.
KO	K01465.
OMA	GINTPFT.
ProtClustDB	PRK09357.
Enzyme and pathway databases
BioCyc	LDEL321956:GI15-1958-MONOMER.
UniPathway	UPA00070; UER00117.
Family and domain databases
HAMAP	MF_00220_B. PyrC_type2_B.
InterPro	IPR006680. Amidohydro_1. IPR004722. DHOase. IPR002195. Dihydroorotase_CS. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR00857. pyrC_multi. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. False negative. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRC_LACDB

Accession

Primary (citable) accession number: Q047M6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program