Reviewed, UniProtKB/Swiss-Prot O66990 (PYRC_AQUAE)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	aq_806

Organism

Aquifex aeolicus [Complete proteome] [HAMAP]

Taxonomic identifier

63363 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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	3D-structure 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 – 422

422

Dihydroorotase

PRO_0000147226

Sites

Metal binding

61

1

Zinc 1 By similarity

Metal binding

63

1

Zinc 1 By similarity

Metal binding

143

1

Zinc 1; via carbamate group By similarity

Metal binding

143

1

Zinc 2; via carbamate group By similarity

Metal binding

180

1

Zinc 2 By similarity

Metal binding

232

1

Zinc 2 By similarity

Metal binding

305

1

Zinc 1 By similarity

Amino acid modifications

Modified residue

143

1

N6-carboxylysine

Secondary structure

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422

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Beta strand

10 – 13

4

Helix

14 – 16

3

Beta strand

18 – 21

4

Beta strand

23 – 27

5

Beta strand

30 – 37

8

Beta strand

41 – 47

7

Beta strand

52 – 55

4

Beta strand

57 – 62

6

Turn

66 – 68

3

Turn

70 – 72

3

Helix

75 – 84

10

Beta strand

87 – 92

6

Beta strand

96 – 98

3

Helix

103 – 116

14

Beta strand

118 – 123

6

Helix

129 – 131

3

Beta strand

133 – 136

4

Helix

139 – 145

7

Helix

160 – 173

14

Beta strand

177 – 179

3

Helix

210 – 224

15

Beta strand

228 – 230

3

Helix

236 – 247

12

Beta strand

252 – 256

5

Helix

258 – 261

4

Helix

287 – 295

9

Helix

327 – 329

3

Helix

330 – 339

10

Helix

345 – 352

8

Helix

354 – 359

6

Beta strand

375 – 385

11

Turn

388 – 390

3

Turn

399 – 402

4

Beta strand

404 – 414

11

Beta strand

417 – 421

5

Sequences

	Sequence		Length	Mass (Da)
	O66990-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 7004E6A48B0165EB	FASTA	422	46,380
	10 20 30 40 50 60 MLKLIVKNGY VIDPSQNLEG EFDILVENGK IKKIDKNILV PEAEIIDAKG LIVCPGFIDI 70 80 90 100 110 120 HVHLRDPGQT YKEDIESGSR CAVAGGFTTI VCMPNTNPPI DNTTVVNYIL QKSKSVGLCR 130 140 150 160 170 180 VLPTGTITKG RKGKEIADFY SLKEAGCVAF TDDGSPVMDS SVMRKALELA SQLGVPIMDH 190 200 210 220 230 240 CEDDKLAYGV INEGEVSALL GLSSRAPEAE EIQIARDGIL AQRTGGHVHI QHVSTKLSLE 250 260 270 280 290 300 IIEFFKEKGV KITCEVNPNH LLFTEREVLN SGANARVNPP LRKKEDRLAL IEGVKRGIID 310 320 330 340 350 360 CFATDHAPHQ TFEKELVEFA MPGIIGLQTA LPSALELYRK GIISLKKLIE MFTINPARII 370 380 390 400 410 420 GVDLGTLKLG SPADITIFDP NKEWILNEET NLSKSRNTPL WGKVLKGKVI YTIKDGKMVY KD

References

[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000657 Genomic DNA. Translation: AAC06948.1.

PIR

C70370.

RefSeq

NP_213551.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XRF	X-ray	1.65	A	1-422	[»]
1XRT	X-ray	1.61	A/B	1-422	[»]

ModBase

Search...

Genome annotation databases

GeneID

1193440.

GenomeReviews

Gene locus aq_806 in contig AE000657_GR.

KEGG

aae:aq_806.

NMPDR

fig|224324.1.peg.566.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

O66990.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_806-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]

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_AQUAE

Accession

Primary (citable) accession number: O66990

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	September 2, 2008
This is version 68 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)