ID   PYRDA_STRP3             Reviewed;         311 AA.
AC   P0DD66; Q79XJ9; Q8K6X4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Putative dihydroorotate dehydrogenase A (fumarate);
DE            Short=DHOD A;
DE            Short=DHODase A;
DE            Short=DHOdehase A;
DE            EC=1.3.98.1;
GN   Name=pyrD; OrderedLocusNames=SpyM3_1091;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC       fumarate as the electron acceptor. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + fumarate = orotate + succinate;
CC         Xref=Rhea:RHEA:30059, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:30839, ChEBI:CHEBI:30864; EC=1.3.98.1;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE014074; AAM79698.1; -; Genomic_DNA.
DR   RefSeq; WP_011054669.1; NC_004070.1.
DR   AlphaFoldDB; P0DD66; -.
DR   SMR; P0DD66; -.
DR   EnsemblBacteria; AAM79698; AAM79698; SpyM3_1091.
DR   KEGG; spg:SpyM3_1091; -.
DR   HOGENOM; CLU_042042_3_0_9; -.
DR   OMA; CPISFIT; -.
DR   UniPathway; UPA00070; -.
DR   Proteomes; UP000000564; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1990663; F:dihydroorotate dehydrogenase (fumarate) activity; IEA:UniProtKB-EC.
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   CDD; cd04741; DHOD_1A_like; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00224; DHO_dh_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR033886; DHOD_1A.
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; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.
FT   CHAIN           1..311
FT                   /note="Putative dihydroorotate dehydrogenase A (fumarate)"
FT                   /id="PRO_1000100231"
FT   ACT_SITE        131
FT                   /note="Nucleophile"
FT   BINDING         45..46
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         248..249
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         270..271
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  34365 MW;  B5A5CC14DB1FA841 CRC64;
     MVSTATQIGH FSFDNCLMNA AGVYCMTKEE LMEVEKSQAA SFVTKTGTLE VRPGNPEPRY
     ADTRLGSINS MGLPNNGFRY YLDFVSDLAK TGQHKPHFLS VVGLSPTETE TILKVIMASD
     YEGLVELNLS CPNVPGKPQI AYDFETTDQL LENIFTYYTK PLGIKLPPYF DIVHFDQAAA
     IFNKYPLSFV NCVNSIGNGL VIEDEQVLIK PKNGFGGIGG DYIKPTALAN VHAFYKRLKP
     SIHIIGTGGI KTGRDAFEHI LCGASMVQIG TALHQEGPAI FERVTKELKT IMVEKGYQSL
     DDFRGNLRYK D