Q2GH90 (PYRC_EHRCR) 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:	ECH_0373

Organism

Ehrlichia chaffeensis (strain Arkansas) [Complete proteome] [HAMAP]

Taxonomic identifier

205920 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

Protein attributes

Sequence length	447 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 – 447	447	Dihydroorotase HAMAP MF_00220_B		PRO_0000325593
Sites
	Metal binding	81	1	Zinc 1 By similarity
	Metal binding	83	1	Zinc 1 By similarity
	Metal binding	161	1	Zinc 1; via carbamate group By similarity
	Metal binding	161	1	Zinc 2; via carbamate group By similarity
	Metal binding	198	1	Zinc 2 By similarity
	Metal binding	252	1	Zinc 2 By similarity
	Metal binding	325	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	161	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2GH90 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: A077FA4FA5361C26	FASTA	447	49,167
	10 20 30 40 50 60 MYKQSWELLG NGQHADLTVA YINARIIDPE SKLDIRGSLL TKGDKIIDFG PDLFANGIPS 70 80 90 100 110 120 TIDEVIDCNN NILLPGLIDI HVHFREPGQE HKETINTGSK SAAAGGITTV VCQPNTIPTI 130 140 150 160 170 180 SSVITAKYIK MRALESAYVN IEFYASITKS DNSLSDMALL KEVGAVGFTD DGMPVMNALT 190 200 210 220 230 240 MRQALSYSSM LDTVIAQHAE DLNISNNGCI NEGIISYELG LKGIPDISES IIVNRDIALM 250 260 270 280 290 300 KNIKNVHYHI LHVSSQESLH IIKQAKSQGL KVTCEVTPHH FTLTERDIMT HGSLAKMNPP 310 320 330 340 350 360 LRTENDRLSM IEGLKSGIID CIATDHAPHD INAKELPLDT AAFGIVGLET MLPISLELYH 370 380 390 400 410 420 NGTMPLIDLL ATLTYKPADI IKVPRGRIKK DYVADLIILD LDHEWVVDIS KFASKSKNSP 430 440 FHNRKVKGKV LRTIVSGKTT YKAEIII

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Arkansas.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000236 Genomic DNA. Translation: ABD45465.1.
RefSeq	YP_507193.1. NC_007799.1.
3D structure databases
ProteinModelPortal	Q2GH90.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2GH90.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3927284.
GenomeReviews	Gene locus ECH_0373 in contig CP000236_GR.
KEGG	ech:ECH_0373.
PATRIC	20576233. VBIEhrCha103583_0317.
TIGR	ECH_0373.
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HBG724623.
OMA	ILGFNEH.
PhylomeDB	Q2GH90.
ProtClustDB	CLSK749639.
Enzyme and pathway databases
BioCyc	ECHA205920:ECH_0373-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_EHRCR

Accession

Primary (citable) accession number: Q2GH90

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 21, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program