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P46539 (PYRDB_BACCL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit
Short name=DHOD B
Short name=DHODase B
Short name=DHOdehase B
EC=1.3.1.14
Alternative name(s):
Dihydrdoorotate oxidase B
Orotate reductase (NADH)
Gene names
Name:pyrD
OrganismBacillus caldolyticus
Taxonomic identifier1394 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with NAD+ as electron acceptor By similarity. HAMAP MF_00224

Catalytic activity

(S)-dihydroorotate + NAD+ = orotate + NADH. 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 (NAD(+) route): step 1/1. HAMAP MF_00224

Subunit structure

Heterotetramer of 2 PyrK and 2 PyrD type B subunits By similarity.

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
NAD
   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

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

orotate reductase (NADH) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP MF_00224
PRO_0000148387

Regions

Nucleotide binding45 – 462FMN By similarity
Nucleotide binding243 – 2442FMN By similarity
Nucleotide binding265 – 2662FMN By similarity
Region69 – 735Substrate binding By similarity
Region192 – 1932Substrate binding By similarity

Sites

Active site1301Nucleophile
Binding site211FMN By similarity
Binding site451Substrate By similarity
Binding site991FMN By similarity
Binding site1271FMN By similarity
Binding site1271Substrate By similarity
Binding site1911FMN; via carbonyl oxygen By similarity
Binding site2171FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P46539 [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 / NBRC 15313 / YP-T.
+Additional computationally mapped references.

Cross-references

Sequence databases

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

3D structure databases

ProteinModelPortalP46539.
SMRP46539. Positions 2-298.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00224. DHO_dh_type1.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR024920. Dihydroorotate_DH_1.
IPR012135. Dihydroorotate_DH_1_2.
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 namePYRDB_BACCL
AccessionPrimary (citable) accession number: P46539
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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