(data stored in SCRATCH zone)

HOGENOM: ALCBS_1_PE1003

ID   ALCBS_1_PE1003                       STANDARD;      PRT;   368 AA.
AC   ALCBS_1_PE1003; Q0VQU7;
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 (ALCBS_1.PE1003) (quinone);
DE   EC=1.3.5 2;AltName: Full=DHOdehase;AltName: Full=Dihydroorotate oxidase; .
GN   Name=pyrD; OrderedLocusNames=ABO_1003;
OS   ALCANIVORAX BORKUMENSIS SK2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ALCBS_1.PE1003.
CC       Alcanivorax borkumensis SK2, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:Q0VQU7_ALCBS
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC       with quinone as electron acceptor (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a
CC       quinol.
CC   -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; orotate from (S)-dihydroorotate (quinone route): step
CC       1/1.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 2 subfamily.
CC   -!- GENE_FAMILY: HOG000225103 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q0VQU7; -.
DR   EMBL; AM286690; CAL16451.1; -; Genomic_DNA.
DR   RefSeq; YP_692723.1; NC_008260.1.
DR   ProteinModelPortal; Q0VQU7; -.
DR   SMR; Q0VQU7; 33-363.
DR   STRING; Q0VQU7; -.
DR   GeneID; 4211158; -.
DR   GenomeReviews; AM286690_GR; ABO_1003.
DR   KEGG; abo:ABO_1003; -.
DR   NMPDR; fig|393595.12.peg.1010; -.
DR   eggNOG; COG0167; -.
DR   OMA; SYVTVNI; -.
DR   PhylomeDB; Q0VQU7; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
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_00225; DHO_dh_type2; 1; -.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005719; Dihydroorotate_DH_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; TIGR01036; PyrD_sub2; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
DR   HOGENOMDNA; ALCBS_1.PE1003; -.
KW   Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Pyrimidine biosynthesis.
SQ   SEQUENCE   368 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVHCSSYCST QNIEVPDALG YNAGDYYRSG SFMLYSLARP LLFSLSEEHS HELTLALLRK
     RAGKLWPGTV PAVPKTVMGI EFPNPVGLAA GLDKNGDCID GLADLGFGFI EVGTVTPRPQ
     SGNPQPRLFR LPEAQALINR MGFNNLGVDY LVAAVKRSRY KGVLGINIGK NKDTPVEDAV
     QDYLICQQKV HAYASYLVVN VSSPNTPGLR TLQHGAALDE LLDTLREAQT RLDQEQRRRV
     PLVIKIAPDN SEEELQSMAE AFLQHGIDGV CVGNTTLSRD GVQNLKNGGE QGGLSGTPLT
     PIANRALAVM RNTLNGRIPI IGVGGINSAG DALEKQRQGA DLVQIYSGLI YQGPGLIGDI
     ARAWPKSI
//

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