A8MIU4 (PYRDB_ALKOO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit
Short name=DHOD B
Short name=DHODase B
Short name=DHOdehase B
EC=1.3.1.14

Alternative name(s):
Dihydrdoorotate oxidase B
Orotate reductase (NADH)

Gene names

Name:	pyrD
Ordered Locus Names:	Clos_2191

Organism

Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]

Taxonomic identifier

350688 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Alkaliphilus

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of dihydroorotate to orotate with NAD+ as electron acceptor By similarity. HAMAP MF_00224
Catalytic activity	(S)-dihydroorotate + NAD+ = orotate + NADH. HAMAP MF_00224
Cofactor	Binds 1 FMN per subunit By similarity. HAMAP MF_00224
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. HAMAP MF_00224
Subunit structure	Heterotetramer of 2 PyrK and 2 PyrD type B subunits By similarity.
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 NAD
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 orotate reductase (NADH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP MF_00224		PRO_0000336442
Regions
	Nucleotide binding	47 – 48	2	FMN By similarity
	Nucleotide binding	244 – 245	2	FMN By similarity
	Nucleotide binding	266 – 267	2	FMN By similarity
	Region	71 – 75	5	Substrate binding By similarity
	Region	193 – 194	2	Substrate binding By similarity
Sites
	Active site	131	1	Nucleophile
	Binding site	23	1	FMN By similarity
	Binding site	47	1	Substrate By similarity
	Binding site	101	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)
	A8MIU4 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 4C3477FFBDCDD4F2	FASTA	302	31,887
	10 20 30 40 50 60 MTRRNMGVHI AGIQLKNPVM TASGTFGSGR EYSEFVDLNQ LGAVVVKGVA NEPWSGNPTP 70 80 90 100 110 120 RIAETYGGML NSVGLQNPGV EAFIKDDIQF LRQYDTKIIV NIAGRTVADY CKVTEKLGDA 130 140 150 160 170 180 DIDLIELNIS CPNVKAGGVN FGTNPAMVEE VTKAVKKVAR QPLIVKLTPN VTDIVEIAKA 190 200 210 220 230 240 AVAGGADAIS LINTLLGMAI DIHGRKPILA NVVGGLSGPA IKPVALRMVY QVANAVQVPI 250 260 270 280 290 300 IGMGGIATGE DAIAFMLAGA TGVAVGTANF MNPRATMEVL EGIEDYMDQY NIEDIHEIIG KL

References

[1]

"Complete genome of Alkaliphilus oremlandii OhILAs." 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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OhILAs.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000853 Genomic DNA. Translation: ABW19726.1.
RefSeq	YP_001513722.1. NC_009922.1.
3D structure databases
ProteinModelPortal	A8MIU4.
ModBase	Search...
Protein-protein interaction databases
STRING	A8MIU4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5675974.
GenomeReviews	Gene locus Clos_2191 in contig CP000853_GR.
KEGG	aoe:Clos_2191.
PATRIC	20869744. VBIAlkOre124042_2298.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG472415.
OMA	VALRMVW.
ProtClustDB	PRK07259.
Enzyme and pathway databases
BioCyc	AORE350688:CLOS_2191-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. False negative. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRDB_ALKOO

Accession

Primary (citable) accession number: A8MIU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	December 4, 2007
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program