PYRDA_STRPN
ID PYRDA_STRPN Reviewed; 311 AA.
AC Q9X9S0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable 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; OrderedLocusNames=SP_0764;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1235/89;
RX PubMed=10432287; DOI=10.1084/jem.190.2.241;
RA Llull D., Munoz R., Lopez R., Garcia E.;
RT "A single gene (tts) located outside the cap locus directs the formation of
RT Streptococcus pneumoniae type 37 capsular polysaccharide. Type 37
RT pneumococci are natural, genetically binary strains.";
RL J. Exp. Med. 190:241-251(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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 -!- INTERACTION:
CC Q9X9S0; Q97SE7: gatB; NbExp=2; IntAct=EBI-2207999, EBI-2207023;
CC Q9X9S0; P65946: pyrR; NbExp=2; IntAct=EBI-2207999, EBI-2207248;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ131985; CAB51330.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74902.1; -; Genomic_DNA.
DR PIR; E95088; E95088.
DR RefSeq; WP_000255160.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q9X9S0; -.
DR SMR; Q9X9S0; -.
DR IntAct; Q9X9S0; 2.
DR STRING; 170187.SP_0764; -.
DR EnsemblBacteria; AAK74902; AAK74902; SP_0764.
DR GeneID; 66805909; -.
DR KEGG; spn:SP_0764; -.
DR eggNOG; COG0167; Bacteria.
DR OMA; CPISFIT; -.
DR PhylomeDB; Q9X9S0; -.
DR BioCyc; SPNE170187:G1FZB-780-MON; -.
DR UniPathway; UPA00070; -.
DR Proteomes; UP000000585; 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; PS00911; DHODEHASE_1; 1.
DR PROSITE; PS00912; DHODEHASE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.
FT CHAIN 1..311
FT /note="Probable dihydroorotate dehydrogenase A (fumarate)"
FT /id="PRO_0000148402"
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"
FT CONFLICT 174
FT /note="H -> Y (in Ref. 1; CAB51330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34527 MW; B01594DE3BF3752F CRC64;
MVSTKTQIAG FEFDNCLMNA AGVACMTIEE LEEVKNSAAG TFVTKTATLD FRQGNPEPRY
QDVPLGSINS MGLPNNGLDY YLDYLLDLQE KESNRTFFLS LVGMSPEETH TILKKVQESD
FRGLTELNLS CPNVPGKPQI AYDFETTDRI LAEVFAYFTK PLGIKLPPYF DIVHFDQAAA
IFNKYPLKFV NCVNSIGNGL YIEDESVVIR PKNGFGGIGG EYIKPTALAN VHAFYQRLNP
QIQIIGTGGV LTGRDAFEHI LCGASMVQVG TTLHKEGVSA FDRITNELKA IMVEKGYESL
EDFRGKLRYI D
