Reviewed, UniProtKB/Swiss-Prot Q2GL89 (PYRC_ANAPZ)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	APH_0245

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

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 + H(2)O = N-carbamoyl-L-aspartate.
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.
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		PRO_0000325581
Sites
	Metal binding	84	1	Zinc 1 By similarity
	Metal binding	86	1	Zinc 1 By similarity
	Metal binding	164	1	Zinc 1; via carbamate group By similarity
	Metal binding	164	1	Zinc 2; via carbamate group By similarity
	Metal binding	201	1	Zinc 2 By similarity
	Metal binding	255	1	Zinc 2 By similarity
	Metal binding	328	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	164	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2GL89-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: B09D15AE95C66DC9	FASTA	447	48,529
	10 20 30 40 50 60 MVSERQTWSL LQGGQCNEYT VAYINARIID PASGTDYKGY LLTRGKEILD FGPGFFDPNG 70 80 90 100 110 120 AAFAASEVVD CNGHVLMPGI VDLHVHLREP GGEHKETVDT GSRAAAAGGV TTVVCQPNTI 130 140 150 160 170 180 PRLENVLVAK YLKMRALESS CVNIEFYGAV TKSDGELCDM ASLKDAGALG FTDDGLPVMN 190 200 210 220 230 240 ALYMKRAFEY AQDLDVVVAQ HAEDCNLSDG GCINEGLVSR ELGLKGIPDI SESIMVSRDI 250 260 270 280 290 300 QLLREVPGAH YHVLHISTKK ALDIVRAAKR EGLRVTCEVT PHHFLLNESA VLEHGTMAKM 310 320 330 340 350 360 NPPLRTEEDR LSMISGLEDG TIDCIATDHA PHAAQEKTRP ISCCAFGIVG LETLLPLSLE 370 380 390 400 410 420 LYHNAGMSLM DVLSKLTSKP AEIVRLPRGK IAKGLVADLV IFDLEHVWTI DTAKFSSKSK 430 440 NSPFQGRKVK GKVLRTVVSG KTVYRAE

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000235 Genomic DNA. Translation: ABD43938.1.
RefSeq	YP_504862.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3931083.
GenomeReviews	Gene locus APH_0245 in contig CP000235_GR.
KEGG	aph:APH_0245.
NMPDR	fig|212042.5.peg.233.
TIGR	APH_0245.
Phylogenomic databases
HOGENOM	Q2GL89.
Enzyme and pathway databases
BioCyc	APHA212042:APH_0245-MON.
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_ANAPZ

Accession

Primary (citable) accession number: Q2GL89

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 21, 2006
Last modified:	September 2, 2008
This is version 22 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)