ID PYRDA_LACLA Reviewed; 311 AA.
AC Q9CFC9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 01-MAY-2013, entry version 94.
DE RecName: Full=Dihydroorotate dehydrogenase A (fumarate);
DE Short=DHOD A;
DE Short=DHODase A;
DE Short=DHOdehase A;
DE EC=1.3.98.1;
GN Name=pyrDA; Synonyms=pydA; OrderedLocusNames=LL1552; ORFNames=L192589;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus
OS lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA Weissenbach J., Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC with fumarate as the electron acceptor (By similarity).
CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + fumarate = orotate +
CC succinate.
CC -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC Type 1 subfamily.
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DR EMBL; AE005176; AAK05650.1; -; Genomic_DNA.
DR PIR; H86818; H86818.
DR RefSeq; NP_267708.1; NC_002662.1.
DR ProteinModelPortal; Q9CFC9; -.
DR SMR; Q9CFC9; 1-311.
DR STRING; 272623.L192589; -.
DR EnsemblBacteria; AAK05650; AAK05650; L192589.
DR GeneID; 1115211; -.
DR KEGG; lla:L192589; -.
DR PATRIC; 22295518; VBILacLac136773_1666.
DR eggNOG; COG0167; -.
DR HOGENOM; HOG000225104; -.
DR KO; K00226; -.
DR OMA; QAAAVFN; -.
DR ProtClustDB; PRK02506; -.
DR BioCyc; LLAC272623:GHSH-1691-MONOMER; -.
DR SABIO-RK; Q9CFC9; -.
DR UniPathway; UPA00070; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052888; F:dihydroorotate oxidase (fumarate) activity; IEA:EC.
DR GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00224; DHO_dh_type1; 1; -.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005720; Dihydroorotate_DH.
DR InterPro; IPR024920; Dihydroorotate_DH_1.
DR InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR InterPro; IPR001295; Dihydroorotate_DH_CS.
DR Pfam; PF01180; DHO_dh; 1.
DR PIRSF; PIRSF000164; DHO_oxidase; 1.
DR TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
DR PROSITE; PS00911; DHODEHASE_1; 1.
DR PROSITE; PS00912; DHODEHASE_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1 311 Dihydroorotate dehydrogenase A
FT (fumarate).
FT /FTId=PRO_0000148393.
FT NP_BIND 43 44 FMN (By similarity).
FT NP_BIND 249 250 FMN (By similarity).
FT NP_BIND 271 272 FMN (By similarity).
FT REGION 67 71 Substrate binding (By similarity).
FT REGION 193 194 Substrate binding (By similarity).
FT ACT_SITE 130 130 Nucleophile.
FT BINDING 19 19 FMN (By similarity).
FT BINDING 43 43 Substrate (By similarity).
FT BINDING 127 127 FMN (By similarity).
FT BINDING 127 127 Substrate (By similarity).
FT BINDING 164 164 FMN (By similarity).
FT BINDING 192 192 FMN; via carbonyl oxygen (By similarity).
FT BINDING 221 221 FMN; via amide nitrogen (By similarity).
SQ SEQUENCE 311 AA; 34231 MW; 80B3619EC408BBA8 CRC64;
MLKTTFANAE FANPFMNASG VHCMTTEDLE ELKASQAGAY ITKSSTLEKR EGNPLPRYVD
LELGSINSMG LPNLGFDYYL DYVLKNQKEK AQEAPIFFSI AGMSAAENIA MLKKIQESNF
SGITELNLSC PNVPGKPQLA YDFEATEKLL KEVFTFFTKP LGVKLPPYFD LVHFDIMAEI
LNQFPLTYVN SVNSIGNGLF IDSEAESVVI KPKDGFGGIG GAYIKPTALA NVRAFYTRLK
PEIKIIGTGG IETGQDAFEH LLCGATMLQI GTALHKEGPA IFDRIIKELE EIMDKKGYQS
IADFHGKLKS L
//
