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Reviewed, UniProtKB/Swiss-Prot P46539 (PYRD_BACCL)

Last modified February 9, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydroorotate dehydrogenase, catalytic subunit
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase
    DHOdehase
      Short name=DHODase
      Short name=DHOD
Gene names
Name: pyrD
OrganismBacillus caldolyticus
Taxonomic identifier1394 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + O2 = orotate + H2O2. HAMAP MF_00224

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00224

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (O2 route): step 1/1. HAMAP MF_00224

Subunit structure

Heterotetramer of 2 pyrK and 2 pyrD subunits By similarity. HAMAP MF_00224

Subcellular location

Cytoplasm By similarity HAMAP MF_00224.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological process'de novo' pyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

UMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Dihydroorotate dehydrogenase, catalytic subunit HAMAP MF_00224
PRO_0000148387

Sites

Active site1301Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P46539-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 8EB76F840A49798E

FASTA31332,857
        10         20         30         40         50         60 
MNRLAVELPG LSLKNPIMPA SGCFGFGREY ARFYDLSVLG AIMIKATTKE PRFGNPTPRV 

        70         80         90        100        110        120 
AETPGGMLNA IGLQNPGLDK VLEEELPWLE QFDVPIIANI AGSTVEEYVE VAEAISKAPN 

       130        140        150        160        170        180 
VHALELNISC PNVKKGGIAF GTVPDVAAEL TRLVKEVAAV PVYVNVSPNV TDIVAMAKAI 

       190        200        210        220        230        240 
EQAGADGLTM INTLVGMRID VKTGRPILAN GTGGLSGPAV KPIAIRMIYE VSQAVSIPII 

       250        260        270        280        290        300 
GMGGIQTAED VLEFFYAGAS AVAVGTANFV DPFVCPTIIA DLPALLDDLG IGHISECIGR 

       310 
SWKTGAHAVH CRA 

« Hide

References

[1]"Molecular characterization of pyrimidine biosynthesis genes from the thermophile Bacillus caldolyticus."
Ghim S.Y., Nielsen P., Neuhard J.
Microbiology 140:479-491(1994) [PubMed: 7516791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 405 / IFO 15313 / YP-T.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73308 Genomic DNA. Translation: CAA51741.1.
PIRI40171.

3D structure databases

SMRP46539. Positions 2-298.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.3.3.1. 1670.

Family and domain databases

HAMAPMF_00224_B. DHO_dh_type1_B.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005720. Dihydroorotate_DH_1_core.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_BACCL
AccessionPrimary (citable) accession number: P46539
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 9, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents