(data stored in SCRATCH zone)

HOGENOM: FUNUC1_1_PE1004

ID   FUNUC1_1_PE1004                      STANDARD;      PRT;   304 AA.
AC   FUNUC1_1_PE1004; Q8RG85;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Dihydroorotate dehydrogenase B (FUNUC1_1.PE1004) (NAD(+)),
DE   catalytic subunit; Short=DHOD B; Short=DHODase B; Short=DHOdehase B;
DE   EC=1.3.1 14;AltName: Full=Dihydrdoorotate oxidase B;AltName: Full=Orotate
DE   reductase (NADH); .
GN   Name=pyrD; OrderedLocusNames=FN0424;
OS   FUSOBACTERIUM NUCLEATUM SUBSP. NUCLEATUM ATCC 25586.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FUNUC1_1.PE1004.
CC       Fusobacterium nucleatum subsp. nucleatum ATCC 25586 chromosome, complet
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:PYRDB_FUSNN
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC       with NAD(+) as electron acceptor (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + NAD(+) = orotate + NADH.
CC   -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
CC   -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 1 subfamily.
CC   -!- GENE_FAMILY: HOG000225105 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8RG85; -.
DR   EMBL; AE009951; AAL94627.1; -; Genomic_DNA.
DR   RefSeq; NP_603328.1; NC_003454.1.
DR   ProteinModelPortal; Q8RG85; -.
DR   SMR; Q8RG85; 2-298.
DR   GeneID; 992857; -.
DR   GenomeReviews; AE009951_GR; FN0424.
DR   KEGG; fnu:FN0424; -.
DR   NMPDR; fig|190304.1.peg.1007; -.
DR   OMA; VALRMVW; -.
DR   ProtClustDB; PRK07259; -.
DR   BioCyc; FNUC190304:FN0424-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
DR   GO; GO:0004589; F:orotate reductase (NADH) activity; IEA:EC.
DR   GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0006222; P:UMP biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00224; DHO_dh_type1; 1; -.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005720; Dihydroorotate_DH_1.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
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.
DR   HOGENOMDNA; FUNUC1_1.PE1004; -.
KW   dihydroorotate dehydrogenase 1B;
KW   Complete proteome; Cytoplasm; Flavoprotein; FMN; NAD; Oxidoreductase;
KW   Pyrimidine biosynthesis; Reference proteome.
SQ   SEQUENCE   304 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSERLRVQIP GLDLKNPIMP ASGCFAFGIE YAELYDISKL GAIMIKAATK EARFGNPTPR
     VAETSSGMLN AIGLQNPGVD EIISNQLKKL EKYDVPIIAN VAGSDIEDYV YVANKISKSP
     NVKALELNIS CPNVKHGGIQ FGTDPNVARN LTEKVKAVSS VPVYVKLSPN VTDIVAMAKA
     VETGGADGLT MINTLVGIVL DRKTGKPIIA NTTGGLSGPA IRPVAIRMVY QVAQAVNIPI
     IGMGGVMDEW DVIDFISAGA SAVAVGTANF TDPFVCPKII DSLELALDKL GVNHILDLKG
     RAFR
//

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