Q6AE78 (PYRD_LEIXX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotate dehydrogenase (quinone)
EC=1.3.5.2

Alternative name(s):
DHOdehase
Short name=DHOD
Short name=DHODase
Dihydroorotate oxidase

Gene names

Name:	pyrD
Ordered Locus Names:	Lxx15100

Organism

Leifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP]

Taxonomic identifier

281090 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Leifsonia

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP MF_00225
Catalytic activity	(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP MF_00225
Cofactor	Binds 1 FMN per subunit By similarity. HAMAP MF_00225
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP MF_00225
Subunit structure	Monomer By similarity. HAMAP MF_00225
Subcellular location	Cell membrane; Peripheral membrane protein By similarity HAMAP MF_00225.
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cell membrane Membrane
Ligand	FMN Flavoprotein
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	plasma membrane 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 – 343	343	Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225		PRO_0000148451
Regions
	Nucleotide binding	65 – 69	5	FMN By similarity
	Nucleotide binding	319 – 320	2	FMN By similarity
	Region	114 – 118	5	Substrate binding By similarity
	Region	244 – 245	2	Substrate binding By similarity
Sites
	Active site	181	1	Nucleophile By similarity
	Binding site	69	1	Substrate By similarity
	Binding site	89	1	FMN; via amide nitrogen By similarity
	Binding site	145	1	FMN By similarity
	Binding site	178	1	FMN By similarity
	Binding site	178	1	Substrate By similarity
	Binding site	183	1	Substrate By similarity
	Binding site	215	1	FMN By similarity
	Binding site	243	1	FMN; via carbonyl oxygen By similarity
	Binding site	269	1	FMN; via amide nitrogen By similarity
	Binding site	298	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6AE78 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: ADACC7DBCB1D1840	FASTA	343	36,075
	10 20 30 40 50 60 MYRTLFSLVL SRFDPERAHR LAFAAIRALP VIGLGSLLRR FTAPDPSLAV EALGLRFDSP 70 80 90 100 110 120 FGIAAGFDKD GEGVIGLGAL GFGHVEVGTI TARPQPGNDK PRLFRLLPDR AVINRMGFNN 130 140 150 160 170 180 HGAGAAANRL LRVRRARRRP VLGVNISKSR AVAVEDATAD YLISARALAP VADYLVVNVS 190 200 210 220 230 240 SPNTPGLRGL QEREALAPLL SAVKAASGKK PLLVKIAPDL TDEQIVAVAR LAVELGLAGI 250 260 270 280 290 300 IATNTTIARD GLSSDPAVVE AAGAGGLSGA PLAARSLEVL TLIRANVPPS LCVISVGGVE 310 320 330 340 TAQDVQRRLD AGATLVQGYT AFLYRGPLWA RQITRGLSAL RSR

References

[1]

"The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli subsp. xyli." Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P., Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D., de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R., Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H. , Coutinho L.L., El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S., Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F., Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A., Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C. Mol. Plant Microbe Interact. 17:827-836(2004) [PubMed: 15305603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CTCB07.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016822 Genomic DNA. Translation: AAT89318.1.
RefSeq	YP_062423.1. NC_006087.1.
3D structure databases
ProteinModelPortal	Q6AE78.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2940206.
GenomeReviews	Gene locus Lxx15100 in contig AE016822_GR.
KEGG	lxx:Lxx15100.
NMPDR	fig|281090.3.peg.415.
PATRIC	22336662. VBILeiXyl11655_1573.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG351027.
OMA	SYVTVNI.
ProtClustDB	PRK05286.
Enzyme and pathway databases
BioCyc	LXYL281090:LXX15100-MONOMER.
Family and domain databases
HAMAP	MF_00225. DHO_dh_type2. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005719. Dihydroorotate_DH_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	TIGR01036. PyrD_sub2. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRD_LEIXX

Accession

Primary (citable) accession number: Q6AE78

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2005
Last sequence update:	September 13, 2004
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program