B2V726 (PYRDA_SULSY) 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:	SYO3AOP1_0163

Organism

Sulfurihydrogenibium sp. (strain YO3AOP1) [Complete proteome] [HAMAP]

Taxonomic identifier

436114 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Hydrogenothermaceae › Sulfurihydrogenibium

Protein attributes

Sequence length	311 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 – 311	311	Putative dihydroorotate dehydrogenase A (fumarate) HAMAP MF_00224		PRO_1000100234
Regions
	Nucleotide binding	45 – 46	2	FMN By similarity
	Nucleotide binding	245 – 246	2	FMN By similarity
	Nucleotide binding	267 – 268	2	FMN By similarity
	Region	69 – 73	5	Substrate binding By similarity
	Region	192 – 193	2	Substrate binding By similarity
Sites
	Active site	130	1	Nucleophile
	Binding site	21	1	FMN By similarity
	Binding site	45	1	Substrate By similarity
	Binding site	99	1	FMN By similarity
	Binding site	127	1	FMN By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	165	1	FMN By similarity
	Binding site	191	1	FMN; via carbonyl oxygen By similarity
	Binding site	217	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2V726 [UniParc]. Last modified July 1, 2008. Version 1. Checksum: 6DD26C66ED4D0C3F	FASTA	311	33,880
	10 20 30 40 50 60 MDKLKHTLFG LEFKNPVWTA SGTFSYGLEV AKIYDLSLLG AIVVKGLSLK PRKGNMPERI 70 80 90 100 110 120 VETPAGMLNS IGLQNPGVDY FINETLPKLK KYDTKIFANV FGEDEDEYLA VAERLDKADG 130 140 150 160 170 180 VHGLELNVSC PNVKKGGIAF GTDPEVLYNL VYKMKKITKK PLLVKLSPNV SNILDTADAC 190 200 210 220 230 240 VSAGADGLVL INTLLGVAID VEREKPILST ITGGLSGPAM LPIAVRMIWQ VYQKYGSRIP 250 260 270 280 290 300 IIGVGGISNY KDALQHILAG ASAIQVGTAN FYDPLSPLKI IEDLKNHLDK KGYVHYSQLI 310 GKAHQMIIKE V

References

[1]

"Complete and draft genome sequences of six members of the Aquificales." Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A. J. Bacteriol. 191:1992-1993(2009) [PubMed: 19136599] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: YO3AOP1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001080 Genomic DNA. Translation: ACD65808.1.
RefSeq	YP_001930362.1. NC_010730.1.
3D structure databases
ProteinModelPortal	B2V726.
ModBase	Search...
Protein-protein interaction databases
STRING	B2V726.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6331361.
GenomeReviews	Gene locus SYO3AOP1_0163 in contig CP001080_GR.
KEGG	sul:SYO3AOP1_0163.
PATRIC	23765015. VBISulSp94719_0174.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG472415.
OMA	VALRMVW.
ProtClustDB	PRK07259.
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_SULSY

Accession

Primary (citable) accession number: B2V726

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	July 1, 2008
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program