(data stored in ACNUC7421 zone)

SWISSPROT: PYRD_SINFN

ID   PYRD_SINFN              Reviewed;         362 AA.
AC   C3MFT0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=Dihydroorotate dehydrogenase (quinone) {ECO:0000255|HAMAP-Rule:MF_00225};
DE            EC=1.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00225};
DE   AltName: Full=DHOdehase {ECO:0000255|HAMAP-Rule:MF_00225};
DE            Short=DHOD {ECO:0000255|HAMAP-Rule:MF_00225};
DE            Short=DHODase {ECO:0000255|HAMAP-Rule:MF_00225};
DE   AltName: Full=Dihydroorotate oxidase {ECO:0000255|HAMAP-Rule:MF_00225};
GN   Name=pyrD {ECO:0000255|HAMAP-Rule:MF_00225};
GN   OrderedLocusNames=NGR_c01810;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC       with quinone as electron acceptor. {ECO:0000255|HAMAP-
CC       Rule:MF_00225}.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a
CC       quinol. {ECO:0000255|HAMAP-Rule:MF_00225}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00225};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_00225};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; orotate from (S)-dihydroorotate (quinone route): step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_00225}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00225}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00225}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00225}.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00225}.
DR   EMBL; CP001389; ACP23981.1; -; Genomic_DNA.
DR   RefSeq; WP_012706766.1; NC_012587.1.
DR   RefSeq; YP_002824734.1; NC_012587.1.
DR   SMR; C3MFT0; -.
DR   STRING; 394.NGR_c01810; -.
DR   EnsemblBacteria; ACP23981; ACP23981; NGR_c01810.
DR   GeneID; 7790759; -.
DR   KEGG; rhi:NGR_c01810; -.
DR   PATRIC; fig|394.7.peg.2976; -.
DR   eggNOG; ENOG4107QYT; Bacteria.
DR   eggNOG; COG0167; LUCA.
DR   HOGENOM; HOG000225103; -.
DR   KO; K00254; -.
DR   OMA; LQNAMGF; -.
DR   OrthoDB; POG091H018H; -.
DR   UniPathway; UPA00070; UER00946.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004152; F:dihydroorotate dehydrogenase 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; cd04738; DHOD_2_like; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00225; DHO_dh_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005720; Dihydroorotate_DH.
DR   InterPro; IPR005719; Dihydroorotate_DH_2.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Pfam; PF01180; DHO_dh; 1.
DR   TIGRFAMs; TIGR01036; pyrD_sub2; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MFT0.
DR   SWISS-2DPAGE; C3MFT0.
KW   Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN         1    362       Dihydroorotate dehydrogenase (quinone).
FT                                /FTId=PRO_1000195086.
FT   NP_BIND      62     66       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   NP_BIND     316    317       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   REGION      111    115       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   REGION      244    245       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   ACT_SITE    173    173       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   BINDING      66     66       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   BINDING      86     86       FMN; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     139    139       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     170    170       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     170    170       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   BINDING     175    175       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00225}.
FT   BINDING     215    215       FMN. {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     243    243       FMN; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     266    266       FMN; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00225}.
FT   BINDING     295    295       FMN; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00225}.
SQ   SEQUENCE   362 AA;  38704 MW;  A49956E26107015A CRC64;
     MTGPLERLAR RGLFLLDPET AHGVSIKALK SGVVPSCAAP ADTRLEQVIA GLNFPNPLGM
     AAGYDKNAEV PEALLRLGFG FTEIGTVTPR PQAGNDKPRI FRLVEDEAVI NRLGFNNDGH
     GAALARLQAC SRQALIGVNI GANKDSADRI ADYVAGIRTF YAVARYFTAN ISSPNTPGLR
     DLQARESLAA LLSAVLAARD EEAAKTGRRV PVFLKIAPDL TEEGMDDIAA EVLAHNLDGL
     IVSNTTLARD GLRDQRQAKE AGGLSGRPLF EKSTAVLARM RKRLGPDVPI IGVGGVSSAE
     TAAEKIRAGA DLVQLYSCMV YEGPGLPGRI VRGLSQLCDR DKLASIREIR DSRLDYWAGR
     NV
//

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