(data stored in ACNUC7421 zone)

HOGENOM: ACHXA_1_PE1008

ID   ACHXA_1_PE1008                       STANDARD;      PRT;   346 AA.
AC   ACHXA_1_PE1008; E3HJP5;
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 (ACHXA_1.PE1008) (quinone);
DE   EC=1.3.5 2;AltName: Full=DHOdehase;AltName: Full=Dihydroorotate oxidase; .
GN   Name=pyrD; OrderedLocusNames=AXYL_01022;
OS   ACHROMOBACTER XYLOSOXIDANS A8.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACHXA_1.PE1008.
CC       Achromobacter xylosoxidans A8 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E3HJP5_ACHXA
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; E3HJP5; -.
DR   EMBL; CP002287; ADP14370.1; -; Genomic_DNA.
DR   RefSeq; YP_003977085.1; NC_014640.1.
DR   GeneID; 9895354; -.
DR   GenomeReviews; CP002287_GR; AXYL_01022.
DR   KEGG; axy:AXYL_01022; -.
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; ACHXA_1.PE1008; -.
KW   dihydroorotate oxidase;
KW   Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Pyrimidine biosynthesis.
SQ   SEQUENCE   346 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSILFHAYPL ARPALFAMDA ETAHEVTLSG LQRAYECGAT RKLMHAQPKA PSTLMGLQLA
     NPIGLAAGLD KNGAYIDALG NLGFGFIEVG TVTPRAQPGN PKPRMFRLPR ANALINRLGF
     NNQGLDAFLA NVQRSAWRKQ GGILGLNIGK NADTPIERAA DDYLIGLEGV YPHADYVTVN
     ISSPNTKNLR ALQGGDELSA LLAQLADKRR ALEDKHQRRV PMAVKIAPDL THEQIDSIAE
     TLPRHGIDGV IATNTTLSRD AVTGQPHAEE AGGLSGAPVH ELSLAVIRRL KERLGGSLAI
     IGVGGVMSGR QAREKMDAGA DAVQLYTGLI YRGPALVGEC VRAVAR
//

If you have problems or comments...

PBIL Back to PBIL home page