O66461 (PYRDA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative dihydroorotate dehydrogenase A (fumarate)
Short name=DHOD A
Short name=DHODase A
Short name=DHOdehase A
EC=1.3.98.1

Gene names

Name:	pyrD
Ordered Locus Names:	aq_046

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor By similarity. HAMAP MF_00224
Catalytic activity	(S)-dihydroorotate + fumarate = orotate + succinate. HAMAP MF_00224
Cofactor	Binds 1 FMN per subunit By similarity. HAMAP MF_00224
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway. HAMAP MF_00224
Subunit structure	Homodimer By similarity. HAMAP MF_00224
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
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 306	306	Putative dihydroorotate dehydrogenase A (fumarate) HAMAP MF_00224		PRO_0000148386
Regions
	Nucleotide binding	44 – 45	2	FMN By similarity
	Nucleotide binding	244 – 245	2	FMN By similarity
	Nucleotide binding	266 – 267	2	FMN By similarity
	Region	68 – 72	5	Substrate binding By similarity
	Region	191 – 192	2	Substrate binding By similarity
Sites
	Active site	129	1	Nucleophile
	Binding site	20	1	FMN By similarity
	Binding site	44	1	Substrate By similarity
	Binding site	98	1	FMN By similarity
	Binding site	126	1	FMN By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	164	1	FMN By similarity
	Binding site	190	1	FMN; via carbonyl oxygen By similarity
	Binding site	216	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	O66461 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 3E1E04D8DE1FCD53	FASTA	306	33,523
	10 20 30 40 50 60 MDLSVELFGI RFKNPVWVAS GTFGYGVEAA EIYDISKLGA VVTKGLSLKE RLGNETPRIV 70 80 90 100 110 120 ETPCGMLNSI GLQNPGVEKF LKEIYPKIKD VDTHFIANVF GETEEEYVEV CMALEDADKI 130 140 150 160 170 180 VAYELNVSCP NVKKGGILFG HDPVILGNLV DRIKAKIKKP LLVKLSPNVT DVTEFAKVCI 190 200 210 220 230 240 ENGADGLVLI NTLMGMKINI WKRKPDLATK TGGLSGPAIL PIAVRMIYQV YEKFGDRIPI 250 260 270 280 290 300 IGVGGITTWE DAMEHVMAGA SAVQVGTANF YEPLAPLKVI EGIENFMKSQ NIKDFKELIG IAHRVE

References

[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC06426.1.
PIR	B70304.
RefSeq	NP_213021.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O66461.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1192658.
GenomeReviews	Gene locus aq_046 in contig AE000657_GR.
KEGG	aae:aq_046.
NMPDR	fig|224324.1.peg.36.
PATRIC	20957793. VBIAquAeo85532_0037.
Phylogenomic databases
HOGENOM	HBG472415.
OMA	VALRMVW.
PhylomeDB	O66461.
ProtClustDB	PRK07259.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_046-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

PYRDA_AQUAE

Accession

Primary (citable) accession number: O66461

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program