[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NCK436; Hall C.R., Dietrich F.S.; "Lactococcus lactis subsp. cremoris gene encoding the biosynthetic enzyme dihydroorotate dehydrogenase family 1a."; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[2]	MUTAGENESIS OF LYS-43; CYS-130; ASN-132 AND LYS-164. DOI=10.1021/bi971628y; PubMed=9405053 [NCBI, ExPASy, EBI, Israel, Japan] Bjoernberg O., Rowland P., Larsen S., Jensen K.F.; "Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis."; Biochemistry 36:16197-16205(1997).
[3]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1016/S0969-2126(97)00182-2; PubMed=9032071 [NCBI, ExPASy, EBI, Israel, Japan] Rowland P., Nielsen F.S., Jensen K.F., Larsen S.; "The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis."; Structure 5:239-252(1997).
[4]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). PubMed=9655329 [NCBI, ExPASy, EBI, Israel, Japan] Rowland P., Bjoernberg O., Nielsen F.S., Jensen K.F., Larsen S.; "The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function."; Protein Sci. 7:1269-1279(1998).

Comments

CATALYTIC ACTIVITY: (S)-dihydroorotate + O₂ = orotate + H₂O₂.
COFACTOR: Binds 1 FMN per subunit.
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
MISCELLANEOUS: Can use fumarate but not NAD as an electron acceptor.
SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY323899; AAQ01776.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1DOR; X-ray; 2.00 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1JQV; X-ray; 2.10 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1JQX; X-ray; 1.70 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1JRB; X-ray; 1.90 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1JRC; X-ray; 1.80 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1JUB; X-ray; 1.40 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1JUE; X-ray; 1.80 A; A/B=1-311.	[ExPASy / RCSB / EBI]
1NFC; Model; -; A=1-311.	[ExPASy / RCSB / EBI]
1OVD; X-ray; 2.25 A; A/B=1-311.	[ExPASy / RCSB / EBI]
2BSL; X-ray; 2.30 A; A/B=-.	[ExPASy / RCSB / EBI]
2BX7; X-ray; 2.04 A; A/B=1-311.	[ExPASy / RCSB / EBI]
2DOR; X-ray; 2.00 A; A/B=1-311.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DOR; -.
1JQV; -.
1JQX; -.
1JRB; -.
1JRC; -.
1JUB; -.
1JUE; -.
1NFC; -.
1OVD; -.
2BSL; -.
2BX7; -.
2DOR; -.

ModBase

Q53ZE5.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004158;	Molecular function: dihydroorotate oxidase activity (inferred from electronic annotation from HAMAP).
GO:0006207;	Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006222;	Biological process: UMP biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00224; -; 1.
PBIL [Tree]

InterPro

IPR013785; Aldolase_TIM.
IPR012135; DHO_DHase_1_2.
IPR005720; DHO_DHase_1_core.
IPR001295; Dihydroorotate_DHase_core.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF01180; DHO_dh; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000164; DHO_oxidase; 1.

TIGRFAMs

TIGR01037; pyrD_sub1_fam; 1.

PROSITE

PS00911; DHODEHASE_1; 1.
PS00912; DHODEHASE_2; 1.

Other

Q53ZE5; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 311`	`311`	`Dihydroorotate dehydrogenase A.`	`PRO_0000148394`
`ACT_SITE`	`130 130`		`Nucleophile.`
`MUTAGEN`	`43 43`		`K->A: More than 500-fold reduction of enzymatic activity with oxygen or DCIP as electron acceptor.`
`MUTAGEN`	`43 43`		`K->E: 40-fold reduction of enzymatic activity with oxygen as electron acceptor; more than 120-fold reduction with DCIP as electron acceptor.`
`MUTAGEN`	`130 130`		`C->A: Almost total loss of activity with oxygen or DCIP as electron acceptor.`
`MUTAGEN`	`130 130`		`C->S: Almost total loss of activity with oxygen or DCIP as electron acceptor.`
`MUTAGEN`	`132 132`		`N->A: 54-fold reduction of enzymatic activity with oxygen as electron acceptor; more than 250-fold reduction with DCIP as electron acceptor.`
`MUTAGEN`	`164 164`		`K->A: Almost total loss of activity with oxygen or DCIP as electron acceptor.`
`STRAND`	`4 6`	`3`
`STRAND`	`9 17`	`9`
`HELIX`	`26 34`	`9`
`STRAND`	`58 61`	`4`
`STRAND`	`64 67`	`4`
`HELIX`	`76 89`	`14`
`STRAND`	`92 94`	`3`
`STRAND`	`97 100`	`4`
`HELIX`	`105 117`	`13`
`STRAND`	`122 128`	`7`
`STRAND`	`133 135`	`3`
`HELIX`	`139 141`	`3`
`HELIX`	`143 153`	`11`
`TURN`	`154 156`	`3`
`STRAND`	`161 165`	`5`
`HELIX`	`171 181`	`11`
`STRAND`	`188 191`	`4`
`STRAND`	`195 199`	`5`
`TURN`	`203 206`	`4`
`STRAND`	`207 209`	`3`
`HELIX`	`212 215`	`4`
`STRAND`	`216 221`	`6`
`HELIX`	`222 224`	`3`
`HELIX`	`225 236`	`12`
`STRAND`	`243 250`	`8`
`HELIX`	`254 263`	`10`
`STRAND`	`266 270`	`5`
`HELIX`	`272 277`	`6`
`HELIX`	`281 296`	`16`
`HELIX`	`301 303`	`3`
`TURN`	`304 306`	`3`

Sequence information

Length: 311 AA [This is the length of the unprocessed precursor]

Molecular weight: 34210 Da [This is the MW of the unprocessed precursor]

CRC64: 30157E3C2791CDD7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLNTTFANAK FANPFMNASG VHCMTIEDLE ELKASQAGAY ITKSSTLEKR EGNPLPRYVD 

        70         80         90        100        110        120 
LELGSINSMG LPNLGFDYYL DYVLKNQKEN AQEGPIFFSI AGMSAAENIA MLKKIQESDF 

       130        140        150        160        170        180 
SGITELNLSC PNVPGKPQLA YDFEATEKLL KEVFTFFTKP LGVKLPPYFD LVHFDIMAEI 

       190        200        210        220        230        240 
LNQFPLTYVN SVNSIGNGLF IDPEAESVVI KPKDGFGGIG GAYIKPTALA NVRAFYTRLK 

       250        260        270        280        290        300 
PEIQIIGTGG IETGQDAFEH LLCGATMLQI GTALHKEGPA IFDRIIKELE EIMNQKGYQS 

       310 
IADFHGKLKS L

Q53ZE5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools