Q043B0 (PYRC_LACGA) 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:	LGAS_1089

Organism

Lactobacillus gasseri (strain ATCC 33323 / DSM 20243) [Complete proteome] [HAMAP]

Taxonomic identifier

324831 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

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 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 – 425	425	Dihydroorotase HAMAP MF_00220_B		PRO_1000024089
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)
	Q043B0 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 6C2EBCDBB17D9C33	FASTA	425	46,019
	10 20 30 40 50 60 MATVIKNGTV YQNGRLIKAD VLIEGKKIKA IGTDLDAEKI IDAQGMLVSP GLVDVHVHYR 70 80 90 100 110 120 DPGQTYKEDI KTGSEAAARG GFTTVGAMPN VTPVPNTPEL MKKMVEENKH KGVVHIFQYG 130 140 150 160 170 180 PITNDETTDI IPDYAALKKA GAFALSNDGH GVQTAQTMYL AMQKAKENNL IIATHAQDDS 190 200 210 220 230 240 LFNKGIVNEG VAAKKLDLPP VTELAETTQI ARDLLLAQKT GVHYHICHVS TKTSVELVRL 250 260 270 280 290 300 AKARGINVTC EVAPHHILLT DSDIPKDNGY FKMNPPLRNK EDQAALLVGL LDGTIDLIAT 310 320 330 340 350 360 DHAPHAKSEK QGGMKNAAFG ITGSETAFST LYTKFVKEEK VLSLEQLLAL LSDKPAKVFG 370 380 390 400 410 420 IENAGVLEPG KNADVAIFDI EHKNEIKEAD FKSKGVNTPF TGQKVYGETV MTLVDGEVVY QRGTK

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: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33323 / DSM 20243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000413 Genomic DNA. Translation: ABJ60462.1.
RefSeq	YP_814900.1. NC_008530.1.
3D structure databases
ProteinModelPortal	Q043B0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q043B0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4439692.
GenomeReviews	Gene locus LGAS_1089 in contig CP000413_GR.
KEGG	lga:LGAS_1089.
NMPDR	fig|1596.1.peg.166.
PATRIC	22230342. VBILacGas62225_1078.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HBG724623.
OMA	CDVHPVG.
PhylomeDB	Q043B0.
ProtClustDB	PRK09357.
Enzyme and pathway databases
BioCyc	LGAS324831:LGAS_1089-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. False negative. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRC_LACGA

Accession

Primary (citable) accession number: Q043B0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program