Reviewed, UniProtKB/Swiss-Prot P46539 (PYRD_BACCL)

Names and origin

Protein names

Recommended 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

Organism

Bacillus caldolyticus

Taxonomic identifier

1394 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + O(2) = orotate + H(2)O(2).
Cofactor	Binds 1 FMN per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6.
Subunit structure	Heterotetramer of 2 pyrK and 2 pyrD subunits By similarity.
Subcellular location	CytoplasmBy similarity.
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
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 component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	dihydroorotate oxidase activity 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 – 313	313	Dihydroorotate dehydrogenase, catalytic subunit		PRO_0000148387
Sites
	Active site	130	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P46539-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 8EB76F840A49798E	FASTA	313	32,857
	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

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
EMBLGenBankDDBJ	X73308 Genomic DNA. Translation: CAA51741.1.
PIR	I40171.
3D structure databases
HSSP	HSSP built from PDB template 1EP2 based on UniProtKB P54322.
ModBase	Search...
Family and domain databases
HAMAP	MF_00224. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR012135. DHO_DHase_1_2. IPR005720. DHO_DHase_1_core. IPR001295. Dihydroorotate_DHase_core. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01180. DHO_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMs	TIGR01037. pyrD_sub1_fam. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRD_BACCL

Accession

Primary (citable) accession number: P46539

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 25, 2008
This is version 60 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)