Q9WYG8 (PYRDB_THEMA) 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:	TM_0333

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	270 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 – 270	270	Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP MF_00224		PRO_0000148404
Regions
	Nucleotide binding	35 – 36	2	FMN By similarity
	Nucleotide binding	226 – 227	2	FMN By similarity
	Nucleotide binding	248 – 249	2	FMN By similarity
	Region	59 – 63	5	Substrate binding By similarity
	Region	180 – 181	2	Substrate binding By similarity
Sites
	Active site	117	1	Nucleophile
	Binding site	12	1	FMN By similarity
	Binding site	35	1	Substrate By similarity
	Binding site	114	1	FMN By similarity
	Binding site	114	1	Substrate By similarity
	Binding site	153	1	FMN By similarity
	Binding site	179	1	FMN; via carbonyl oxygen By similarity
	Binding site	199	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9WYG8 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: E773E89BDB473C20	FASTA	270	29,742
	10 20 30 40 50 60 MLELKPPLVL LSGPAGFGEY LKLMDHRYVG GVLLKTVTLH PKEGNPTPRM ADSDFYVINR 70 80 90 100 110 120 IGLENPGIHA FVENIPELPV PMIASLGGDS FEEYLEVARV FKKVADRFYA VEFNFSCPNV 130 140 150 160 170 180 KEGGLSIVKN AEEWKKLLNT LRKELPDSFL IAKVGVEGIF VEDAAEFVMK TGWDGITLVN 190 200 210 220 230 240 TVRGLHFEKD TMILGGLSGP VLKPIALRAV YEVKKRFPEL FVIASGGVYS VKDAEEFLKV 250 260 270 GADVIGVGSA LFKDPGVVEE IGKYLLEVKR

References

[1]

"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000512 Genomic DNA. Translation: AAD35420.1.
PIR	G72390.
RefSeq	NP_228144.1. NC_000853.1.
3D structure databases
ProteinModelPortal	Q9WYG8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	897288.
GenomeReviews	Gene locus TM_0333 in contig AE000512_GR.
KEGG	tma:TM0333.
NMPDR	fig|243274.1.peg.328.
PATRIC	23935547. VBITheMar51294_0338.
TIGR	TM_0333.
Phylogenomic databases
HOGENOM	HBG472415.
OMA	VALRMVW.
PhylomeDB	Q9WYG8.
ProtClustDB	CLSK875095.
Enzyme and pathway databases
BioCyc	TMAR243274:TM_0333-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_THEMA

Accession

Primary (citable) accession number: Q9WYG8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program