(data stored in ACNUC7421 zone)

HOGENOM: ECO5T_1_PE1008

ID   ECO5T_1_PE1008                       STANDARD;      PRT;   336 AA.
AC   ECO5T_1_PE1008; C6UNL1;
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 (ECO5T_1.PE1008) (quinone);
DE   EC=1.3.5 2;AltName: Full=DHOdehase;AltName: Full=Dihydroorotate oxidase; .
GN   Name=pyrD; OrderedLocusNames=ECSP_1051;
OS   ESCHERICHIA COLI O157:H7 STR. TW14359.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=544404;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECO5T_1.PE1008.
CC       Escherichia coli O157:H7 str. TW14359, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6UNL1_ECO5T
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; C6UNL1; -.
DR   EMBL; CP001368; ACT70906.1; -; Genomic_DNA.
DR   RefSeq; YP_003076982.1; NC_013008.1.
DR   ProteinModelPortal; C6UNL1; -.
DR   SMR; C6UNL1; 1-336.
DR   STRING; C6UNL1; -.
DR   PRIDE; C6UNL1; -.
DR   EnsemblBacteria; EBESCT00000169885; EBESCP00000154387; EBESCG00000166462.
DR   GeneID; 8215617; -.
DR   GenomeReviews; CP001368_GR; ECSP_1051.
DR   KEGG; etw:ECSP_1051; -.
DR   GeneTree; EBGT00050000011106; -.
DR   OMA; SYVTVNI; -.
DR   ProtClustDB; PRK05286; -.
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; ECO5T_1.PE1008; -.
KW   dihydroorotate dehydrogenase 2;
KW   Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Pyrimidine biosynthesis.
SQ   SEQUENCE   336 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MYYPFVRKAL FQLDPERAHE FTFQQLRRIT GTPFEALVRQ KVPAKPVNCM GLTFKNPLGL
     AAGLDKDGEC IDALGAMGFG SIEIGTVTPR PQPGNDKPRL FRLVDAEGLI NRMGFNNLGV
     DNLVENVKKA HYDGVLGINI GKNKDTPVEQ GKDDYLICME KIYAYAGYIA INISSPNTPG
     LRTLQYGEAL DDLLTAIKNK QNDLQAMHHK YVPIAVKIAP DLSEEELIQV ADSLVRHNID
     GVIATNTTLD RSLVQGMKNC DQTGGLSGRP LQLKSTEIIR RLSLELNGRL PIIGVGGIDS
     VIAAREKIAA GASLVQIYSG FIFKGPPLIK EIVTHI
//

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