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Database: UniProt
Entry: Q8DQG9
LinkDB: Q8DQG9
Original site: Q8DQG9 
ID   PYRDA_STRR6             Reviewed;         311 AA.
AC   Q8DQG9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   19-FEB-2014, entry version 79.
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=spr0672;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E.,
RA   LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P.,
RA   McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I.,
RA   Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P.,
RA   Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G.,
RA   Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L.,
RA   Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(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; AE007317; AAK99476.1; -; Genomic_DNA.
DR   PIR; H97955; H97955.
DR   RefSeq; NP_358266.1; NC_003098.1.
DR   ProteinModelPortal; Q8DQG9; -.
DR   SMR; Q8DQG9; 6-308.
DR   STRING; 171101.spr0672; -.
DR   EnsemblBacteria; AAK99476; AAK99476; spr0672.
DR   GeneID; 934210; -.
DR   KEGG; spr:spr0672; -.
DR   PATRIC; 19701243; VBIStrPne107296_0744.
DR   eggNOG; COG0167; -.
DR   HOGENOM; HOG000225104; -.
DR   KO; K00226; -.
DR   OMA; DFDNCLM; -.
DR   OrthoDB; EOG6NPM9S; -.
DR   ProtClustDB; PRK02506; -.
DR   BioCyc; SPNE171101:GJC8-679-MONOMER; -.
DR   UniPathway; UPA00070; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052888; F:dihydroorotate oxidase (fumarate) activity; IEA:UniProtKB-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       Probable dihydroorotate dehydrogenase A
FT                                (fumarate).
FT                                /FTId=PRO_0000148403.
FT   NP_BIND      45     46       FMN (By similarity).
FT   NP_BIND     248    249       FMN (By similarity).
FT   NP_BIND     270    271       FMN (By similarity).
FT   REGION       69     73       Substrate binding (By similarity).
FT   REGION      194    195       Substrate binding (By similarity).
FT   ACT_SITE    131    131       Nucleophile.
FT   BINDING      45     45       Substrate (By similarity).
FT   BINDING     128    128       FMN (By similarity).
FT   BINDING     128    128       Substrate (By similarity).
FT   BINDING     165    165       FMN (By similarity).
FT   BINDING     193    193       FMN; via carbonyl oxygen (By similarity).
FT   BINDING     220    220       FMN; via amide nitrogen (By similarity).
SQ   SEQUENCE   311 AA;  34501 MW;  E00F94D5FCFEC3F4 CRC64;
     MVSTKTQIAG FEFDNCLMNA AGVACMTIEE LEEVKNSAAG TFVTKTATLD FRQGNPEPRY
     QDVPLGSINS MGLPNNGLDY YLDYLLDLQE KESNRTFFLS LVGMSPEETH TILKKVQESD
     FRGLTELNLS CPNVPGKPQI AYDFETTDRI LAEVFAYFTK PLGIKLPPYF DIVHFDQAAA
     IFNKYPLKFV NCVNSSGNGL YIEDESVVIR PKNGFGGIGG EYIKPTALAN VHAFYQRLNP
     QIQIIGTGGV LTGRDAFEHI LCGASMVQVG TTLHKEGVSA FDRITNELKA IMVEKGYESL
     EDFRGKLRYI D
//
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