Q01YA2 (PYRDA_SOLUE) 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:	Acid_4402

Organism

Solibacter usitatus (strain Ellin6076) [Complete proteome] [HAMAP]

Taxonomic identifier

234267 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Solibacteres › Solibacterales › Solibacteraceae › Candidatus Solibacter

Protein attributes

Sequence length	304 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
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 – 304	304	Putative dihydroorotate dehydrogenase A (fumarate) HAMAP MF_00224		PRO_1000100226
Regions
	Nucleotide binding	46 – 47	2	FMN By similarity
	Nucleotide binding	244 – 245	2	FMN By similarity
	Nucleotide binding	266 – 267	2	FMN By similarity
	Region	70 – 74	5	Substrate binding By similarity
	Region	193 – 194	2	Substrate binding By similarity
Sites
	Active site	131	1	Nucleophile
	Binding site	22	1	FMN By similarity
	Binding site	46	1	Substrate By similarity
	Binding site	100	1	FMN By similarity
	Binding site	128	1	FMN By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	166	1	FMN By similarity
	Binding site	192	1	FMN; via carbonyl oxygen By similarity
	Binding site	218	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01YA2 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: CD53DDD8F92B8C1B	FASTA	304	31,894
	10 20 30 40 50 60 MTPQLATTIC GIALKNPVLA ASGTFAYGVE FEKLVDLNAL GGFVVKGLSR EPIEGNPPPR 70 80 90 100 110 120 VFESEAGMIN SVGLQNIGVR AFVAEKLPAL AGLRTAVFAN VFGYCTEDYV EVVRVLNDHA 130 140 150 160 170 180 GLAGYELNVS CPNTAHGGIY FSNDPVLLAE VVTAAKRVAT RPLIVKLSPN VSAIEPLARV 190 200 210 220 230 240 AEESGADALS LVNTVISLAI DARTRRPRIG AGFGGLSGPA IKPIALRFVY QAARAVRIPV 250 260 270 280 290 300 IGLGGIATGE DAAEFLIAGA SAVEVGTATF WDPRAPLRIA EELGKFLERE GIRKATDLVG TLKF

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ellin6076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000473 Genomic DNA. Translation: ABJ85363.1.
RefSeq	YP_825648.1. NC_008536.1.
3D structure databases
ProteinModelPortal	Q01YA2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q01YA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4427326.
GenomeReviews	Gene locus Acid_4402 in contig CP000473_GR.
KEGG	sus:Acid_4402.
NMPDR	fig|234267.9.peg.4188.
PATRIC	32011298. VBICanSol30224_4614.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0167.
HOGENOM	HBG472415.
OMA	VALRMVW.
PhylomeDB	Q01YA2.
ProtClustDB	CLSK774280.
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. False negative. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRDA_SOLUE

Accession

Primary (citable) accession number: Q01YA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program