Q8A9C3 (PYRDB_BACTN) 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:	BT_0892

Organism

Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)

Taxonomic identifier

226186 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	303 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 Reference 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 – 303	303	Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP MF_00224		PRO_1000024131
Regions
	Nucleotide binding	45 – 46	2	FMN By similarity
	Nucleotide binding	243 – 244	2	FMN By similarity
	Nucleotide binding	265 – 266	2	FMN By similarity
	Region	69 – 73	5	Substrate binding By similarity
	Region	192 – 193	2	Substrate binding By similarity
Sites
	Active site	130	1	Nucleophile
	Binding site	21	1	FMN By similarity
	Binding site	45	1	Substrate By similarity
	Binding site	99	1	FMN By similarity
	Binding site	127	1	FMN By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	165	1	FMN By similarity
	Binding site	191	1	FMN; via carbonyl oxygen By similarity
	Binding site	217	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8A9C3 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: B51FAAF443050485	FASTA	303	32,296
	10 20 30 40 50 60 MADLSVNIGE LQMKNPVMTA SGTFGYGEEF SDFIDIARIG GIIVKGTTLH KREGNPYPRM 70 80 90 100 110 120 AETPSGMLNA VGLQNKGVDY FVEQIYPRIK DIQTNMIVNV SGSAIEDYVK TAEIINELDK 130 140 150 160 170 180 IPAIELNISC PNVKQGGMAF GVSAKGASEV VKAVRAAYKK TLIVKLSPNV TDITEIARAA 190 200 210 220 230 240 EESGADSVSL INTLLGMAID AERKRPILST VTGGMSGAAV KPIALRMVWQ VAKAVNIPVI 250 260 270 280 290 300 GLGGIMNWKD AVEFMLAGAS AIQIGTANFI DPAVTIKVED GINNYLERHG CKSVKEIIGA LEV

References

[1]

"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis." Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I. Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015928 Genomic DNA. Translation: AAO75999.1.
RefSeq	NP_809805.1. NC_004663.1.
3D structure databases
HSSP	HSSP built from PDB template 1EP2 based on UniProtKB P54322.
ProteinModelPortal	Q8A9C3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1074664.
GenomeReviews	Gene locus BT_0892 in contig AE015928_GR.
KEGG	bth:BT_0892.
NMPDR	fig|226186.1.peg.892.
PATRIC	21056577. VBIBacThe70966_0904.
Phylogenomic databases
HOGENOM	HBG472415.
OMA	VALRMVW.
PhylomeDB	Q8A9C3.
ProtClustDB	PRK07259.
Enzyme and pathway databases
BioCyc	BTHE226186:BT_0892-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. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRDB_BACTN

Accession

Primary (citable) accession number: Q8A9C3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program