Q6A912 (PYRDB_PROAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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
Ordered Locus Names:	PPA1002

Organism

Propionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]

Taxonomic identifier

267747 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Pyrimidine biosynthesis
Cellular component	Cytoplasm
Ligand	FMN Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
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 component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydroorotate 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 307	307	Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP MF_00224		PRO_1000024141
Regions
	Nucleotide binding	45 – 46	2	FMN By similarity
	Nucleotide binding	245 – 246	2	FMN By similarity
	Nucleotide binding	267 – 268	2	FMN By similarity
	Region	69 – 73	5	Substrate binding By similarity
	Region	194 – 195	2	Substrate binding By similarity
Sites
	Active site	132	1	Nucleophile
	Binding site	21	1	FMN By similarity
	Binding site	45	1	Substrate By similarity
	Binding site	101	1	FMN By similarity
	Binding site	129	1	FMN By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	167	1	FMN By similarity
	Binding site	193	1	FMN; via carbonyl oxygen By similarity
	Binding site	219	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6A912 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 6B5E90B0EBC522B1	FASTA	307	31,976
	10 20 30 40 50 60 MTRLAVSLPG LNLKNPIMPA SGCFGFGAEY AEYYDLSVLG SIMVKATTLE PRRGNPVIRV 70 80 90 100 110 120 AETPGGMLNA IGLQNPGLDV VMAEKLPWLA EHFPDLPIIA NVAGYTTEDY VRVCEVISTA 130 140 150 160 170 180 PNVAAVEINI SCPNVKRGGI TFGTNVTAAH DLTQAVVAAA SVPVYVKLSP NVTDITEIAR 190 200 210 220 230 240 ATADAGADGL TLINTLTGMR INLARRTPVI ANATGGLSGP AVLPIAVRMI DAVTRVVDIP 250 260 270 280 290 300 VIGMGGVMTS ADALELMMAG ASAVGVGTAN FTDPLACPKI INGLEPLMDD LSIASLEDLR TQVRQSR

References

[1]

"The complete genome sequence of Propionibacterium acnes, a commensal of human skin." Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G. Science 305:671-673(2004) [PubMed: 15286373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017283 Genomic DNA. Translation: AAT82754.1.
RefSeq	YP_055712.1. NC_006085.1.
3D structure databases
HSSP	HSSP built from PDB template 1EP2 based on UniProtKB P54322.
ProteinModelPortal	Q6A912.
SMR	Q6A912. Positions 3-307.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2932792.
GenomeReviews	Gene locus PPA1002 in contig AE017283_GR.
KEGG	pac:PPA1002.
NMPDR	fig|267747.1.peg.989.
PATRIC	23036729. VBIProAcn64440_1037.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG472415.
OMA	VALRMVW.
PhylomeDB	Q6A912.
ProtClustDB	CLSK2763661.
Enzyme and pathway databases
BioCyc	PACN267747:PPA1002-MONOMER.
Family and domain databases
HAMAP	MF_00224. DHO_dh_type1. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR005720. Dihydroorotate_DH. IPR024920. Dihydroorotate_DH_1. IPR012135. Dihydroorotate_DH_1_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K00226.
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. False negative. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRDB_PROAC

Accession

Primary (citable) accession number: Q6A912

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 13, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program