A0AJT8 (PYRDB_LISW6) 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):
Dihydroorotate oxidase B
Orotate reductase (NADH)

Gene names

Name:	pyrD
Ordered Locus Names:	lwe1852

Organism

Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334) [Complete proteome] [HAMAP]

Taxonomic identifier

386043 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria welshimeri

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 NAD+ as electron acceptor By similarity. HAMAP-Rule MF_00224
Catalytic activity	(S)-dihydroorotate + NAD+ = orotate + NADH. HAMAP-Rule MF_00224
Cofactor	Binds 1 FMN per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. HAMAP-Rule MF_00224
Subunit structure	Heterotetramer of 2 PyrK and 2 PyrD type B subunits By similarity.
Subcellular location	Cytoplasm By similarity.
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' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' pyrimidine nucleobase 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 – 304	304	Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP-Rule MF_00224		PRO_1000024138
Regions
	Nucleotide binding	45 – 46	2	FMN By similarity
	Nucleotide binding	243 – 244	2	FMN By similarity
	Nucleotide binding	265 – 266	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)
	A0AJT8 [UniParc]. Last modified November 28, 2006. Version 1. Checksum: AA42E240D5407E0D	FASTA	304	32,227
	10 20 30 40 50 60 MNRLAVEIPG LSLKNPIMPA SGCFGFGQEY SKYYDLNKLG AIMAKAVTPE PRLGNPTPRV 70 80 90 100 110 120 AETASGMLNA IGLQNPGLEH VLAHELPFLE QFETPIIANV AGATEDDYVE VCSRIGESKA 130 140 150 160 170 180 VKAIELNISC PNVKHGGIAF GTDPEVAHRL TKAVKSVASV PVYVKLSPNV ADIVSIAQAI 190 200 210 220 230 240 EAAGADGLTM INTLLGMRID LKTRKPIIAN GTGGLSGPAI KPVAIRMIHQ VRSVSNIPII 250 260 270 280 290 300 GMGGVQTVDD VLEFLIAGAD AVAVGTMNFT DPFICPKLIT ELPIRMDELG ISSLQELKKE RANQ

References

[1]

"Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes." Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T. , Lampidis R., Kreft J., Goebel W., Chakraborty T. J. Bacteriol. 188:7405-7415(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35897 / DSM 20650 / SLCC5334.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM263198 Genomic DNA. Translation: CAK21270.1.
RefSeq	YP_850049.1. NC_008555.1.
3D structure databases
ProteinModelPortal	A0AJT8.
SMR	A0AJT8. Positions 2-300.
ModBase	Search...
Protein-protein interaction databases
STRING	386043.lwe1852.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAK21270; CAK21270; lwe1852.
GeneID	4465480.
KEGG	lwe:lwe1852.
PATRIC	20330909. VBILisWel39304_1861.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0167.
HOGENOM	HOG000225105.
KO	K00226.
OMA	RNPVMTA.
ProtClustDB	PRK07259.
Enzyme and pathway databases
BioCyc	LWEL386043:GI5X-1871-MONOMER.
UniPathway	UPA00070; UER00945.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00224. DHO_dh_type1.
InterPro	IPR013785. Aldolase_TIM. IPR005720. Dihydroorotate_DH. IPR024920. Dihydroorotate_DH_1. IPR012135. Dihydroorotate_DH_1_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view]
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. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRDB_LISW6

Accession

Primary (citable) accession number: A0AJT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 28, 2006
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program