Q81WF0 (PYRC_BACAN) 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:	BA_4027, GBAA_4027, BAS3739

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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	3D-structure Complete proteome Reference 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 – 428

428

Dihydroorotase HAMAP MF_00220_B

PRO_0000325582

Sites

Metal binding

59

1

Zinc 1 By similarity

Metal binding

61

1

Zinc 1 By similarity

Metal binding

141

1

Zinc 1; via carbamate group By similarity

Metal binding

141

1

Zinc 2; via carbamate group By similarity

Metal binding

178

1

Zinc 2 By similarity

Metal binding

231

1

Zinc 2 By similarity

Metal binding

304

1

Zinc 1 By similarity

Amino acid modifications

Modified residue

141

1

N6-carboxylysine By similarity

Secondary structure

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428

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Beta strand

22 – 25

4

Beta strand

29 – 31

3

Beta strand

41 – 45

5

Beta strand

50 – 52

3

Beta strand

56 – 60

5

Helix

78 – 81

4

Beta strand

87 – 90

4

Beta strand

94 – 96

3

Helix

101 – 114

14

Beta strand

116 – 121

6

Helix

127 – 129

3

Helix

137 – 142

6

Helix

158 – 170

13

Beta strand

175 – 177

3

Helix

182 – 184

3

Helix

195 – 198

4

Helix

207 – 223

17

Beta strand

227 – 229

3

Helix

238 – 246

9

Beta strand

251 – 253

3

Helix

257 – 261

5

Helix

264 – 266

3

Helix

272 – 274

3

Helix

284 – 290

7

Helix

312 – 314

3

Helix

330 – 337

8

Helix

346 – 351

6

Turn

352 – 354

3

Helix

355 – 360

6

Beta strand

376 – 379

4

Helix

389 – 391

3

Beta strand

410 – 414

5

Beta strand

419 – 422

4

Sequences

	Sequence		Length	Mass (Da)
	Q81WF0 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 6AA9493906CCA956	FASTA	428	46,656
	10 20 30 40 50 60 MNYLFKNGRY MNEEGKIVAT DLLVQDGKIA KVAENITADN AEVIDVNGKL IAPGLVDVHV 70 80 90 100 110 120 HLREPGGEHK ETIETGTLAA AKGGFTTICA MPNTRPVPDC REHMEDLQNR IKEKAHVNVL 130 140 150 160 170 180 PYGAITVRQA GSEMTDFETL KELGAFAFTD DGVGVQDASM MLAAMKRAAK LNMAVVAHCE 190 200 210 220 230 240 ENTLINKGCV HEGKFSEKHG LNGIPSVCES VHIARDILLA EAADCHYHVC HVSTKGSVRV 250 260 270 280 290 300 IRDAKRAGIK VTAEVTPHHL VLCEDDIPSA DPNFKMNPPL RGKEDHEALI EGLLDGTIDM 310 320 330 340 350 360 IATDHAPHTA EEKAQGIERA PFGITGFETA FPLLYTNLVK KGIITLEQLI QFLTEKPADT 370 380 390 400 410 420 FGLEAGRLKE GRTADITIID LEQEEEIDPT TFLSKGKNTP FAGWKCQGWP VMTIVGGKIA WQKESALV

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.
[3]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE016879 Genomic DNA. Translation: AAP27754.1.
AE017334 Genomic DNA. Translation: AAT33144.1.
AE017225 Genomic DNA. Translation: AAT56041.1.

RefSeq

NP_846268.1. NC_003997.3.
YP_020669.1. NC_007530.2.
YP_029990.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MPG	X-ray	2.60	A/B	1-428	[»]

ProteinModelPortal

Q81WF0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q81WF0. 2 interactions.

Protein family/group databases

MEROPS

M38.972.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000008470; EBBACP00000008226; EBBACG00000008462.
EBBACT00000016728; EBBACP00000016349; EBBACG00000016719.
EBBACT00000019675; EBBACP00000019160; EBBACG00000019666.

GeneID

1086660.
2819582.
2852141.

GenomeReviews

Gene locus BA_4027 in contig AE016879_GR.
Gene locus BAS3739 in contig AE017225_GR.
Gene locus GBAA_4027 in contig AE017334_GR.

KEGG

ban:BA_4027.
bar:GBAA_4027.
bat:BAS3739.

TIGR

BA_4027.
GBAA_4027.

Phylogenomic databases

GeneTree

EBGT00050000001626.

HOGENOM

HBG724623.

OMA

CDVHPVG.

ProtClustDB

PRK09357.

Enzyme and pathway databases

BioCyc

BANT260799:BAS3739-MONOMER.
BANT261594:GBAA4027-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_BACAN

Accession

Primary (citable) accession number: Q81WF0
Secondary accession number(s): Q6HUJ8, Q6KNT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	June 1, 2003
Last modified:	November 16, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program