Q0A8M5 (PYRD_ALHEH) 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:	Mlg_1463

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

Protein attributes

Sequence length	340 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 – 340	340	Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225		PRO_0000336452
Regions
	Nucleotide binding	62 – 66	5	FMN By similarity
	Nucleotide binding	318 – 319	2	FMN By similarity
	Region	111 – 115	5	Substrate binding By similarity
	Region	246 – 247	2	Substrate binding By similarity
Sites
	Active site	175	1	Nucleophile By similarity
	Binding site	66	1	Substrate By similarity
	Binding site	86	1	FMN; via amide nitrogen By similarity
	Binding site	139	1	FMN By similarity
	Binding site	172	1	FMN By similarity
	Binding site	172	1	Substrate By similarity
	Binding site	177	1	Substrate By similarity
	Binding site	217	1	FMN By similarity
	Binding site	245	1	FMN; via carbonyl oxygen By similarity
	Binding site	268	1	FMN; via amide nitrogen By similarity
	Binding site	297	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0A8M5 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: BA1ED21D9836E4D7	FASTA	340	37,191
	10 20 30 40 50 60 MYSLIRPLLM RMDAERSHEF SLAWMDRLAR LGLGRLLCGH RLPDMPRRVM GLTFANPVGL 70 80 90 100 110 120 AAGLDKNGEH LEALGHVGFG FIEVGTVTPR PQPGNPEPRL FRLPAHEAII NRMGFNNQGV 130 140 150 160 170 180 DALVQRLRVT RYQGVLGVNI GKNKDTPTER ATDDYLSCLQ KVYPYADYVA VNVSSPNTPG 190 200 210 220 230 240 LRDLQGGELL EALLGRLTHL RGVLAREYGR YVPLVVKIAP DMDEAQRAHF CQQVLRYGID 250 260 270 280 290 300 GVAATNTTLS RDGVEDDPLA REQGGLSGAP LRPRAQAVLE ELGQRLGHRV PLIGVGGIMS 310 320 330 340 GADAQARMAA GADLLQIYSG FIYRGPLLLE ELLKAVAPEH

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MLHE-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000453 Genomic DNA. Translation: ABI56812.1.
RefSeq	YP_742302.1. NC_008340.1.
3D structure databases
ProteinModelPortal	Q0A8M5.
SMR	Q0A8M5. Positions 2-335.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0A8M5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4270244.
GenomeReviews	Gene locus Mlg_1463 in contig CP000453_GR.
KEGG	aeh:Mlg_1463.
NMPDR	fig|187272.6.peg.1403.
PATRIC	20862175. VBIAlkEhr114327_1463.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0167.
HOGENOM	HBG351027.
OMA	SYVTVNI.
PhylomeDB	Q0A8M5.
Enzyme and pathway databases
BioCyc	AEHR187272:MLG_1463-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_ALHEH

Accession

Primary (citable) accession number: Q0A8M5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program