(data stored in ACNUC7421 zone)

HOGENOM: ESCF3_1_PE1013

ID   ESCF3_1_PE1013                       STANDARD;      PRT;   336 AA.
AC   ESCF3_1_PE1013; B7LNV5;
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 (ESCF3_1.PE1013) (quinone);
DE   EC=1.3.5 2;AltName: Full=DHOdehase; Short=DHOD; Short=DHODase;AltName:
DE   Full=Dihydroorotate oxidase; .
GN   Name=pyrD; OrderedLocusNames=EFER_1082;
OS   ESCHERICHIA FERGUSONII ATCC 35469.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ESCF3_1.PE1013.
CC       Escherichia fergusonii ATCC 35469, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:PYRD_ESCF3
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; B7LNV5; -.
DR   EMBL; CU928158; CAQ88611.1; -; Genomic_DNA.
DR   RefSeq; YP_002382245.1; NC_011740.1.
DR   STRING; B7LNV5; -.
DR   EnsemblBacteria; EBESCT00000123667; EBESCP00000117446; EBESCG00000122627.
DR   GeneID; 7121950; -.
DR   GenomeReviews; CU928158_GR; EFER_1082.
DR   KEGG; efe:EFER_1082; -.
DR   GeneTree; EBGT00050000011106; -.
DR   ProtClustDB; PRK05286; -.
DR   BioCyc; EFER585054:EFER_1082-MON; -.
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; ESCF3_1.PE1013; -.
KW   Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Pyrimidine biosynthesis.
SQ   SEQUENCE   336 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MYYPFVRKAL FQLDPERAHE FTFQQLRRIT GTPFEALVRQ KVPVKPVSCM GLTFKNPLGL
     AAGLDKDGEC IDALGAMGFG SIEIGTVTPR PQPGNDKPRL FRLVDAEGLI NRMGFNNLGV
     DNLIENVKKA HYDGVLGINI GKNKDTPVEQ GKDDYLICMD KIYPYAGYIA INISSPNTPG
     LRTLQYGEAL DDLLIAIKNK QNDLQKIHQK YVPIAVKIAP DLSEEELIQV ADSLVRHNID
     GVIATNTTLD RSLVQGMKNC DQTGGLSGRP LQLKSTEIIR RLSQELNGRL PIIGVGGIDS
     VIAAREKIAA GATLVQIYSG FIFKGPPLIK EIVSNI
//

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