(data stored in SCRATCH zone)

SWISSPROT: C6B0B4_RHILS

ID   C6B0B4_RHILS            Unreviewed;       362 AA.
AC   C6B0B4;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Dihydroorotate dehydrogenase (quinone) {ECO:0000256|HAMAP-Rule:MF_00225};
DE            EC=1.3.5.2 {ECO:0000256|HAMAP-Rule:MF_00225};
DE   AltName: Full=DHOdehase {ECO:0000256|HAMAP-Rule:MF_00225};
DE            Short=DHOD {ECO:0000256|HAMAP-Rule:MF_00225};
DE            Short=DHODase {ECO:0000256|HAMAP-Rule:MF_00225};
DE   AltName: Full=Dihydroorotate oxidase {ECO:0000256|HAMAP-Rule:MF_00225};
GN   Name=pyrD {ECO:0000256|HAMAP-Rule:MF_00225};
GN   OrderedLocusNames=Rleg_0222 {ECO:0000313|EMBL:ACS54533.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54533.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54533.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54533.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC       with quinone as electron acceptor. {ECO:0000256|HAMAP-
CC       Rule:MF_00225, ECO:0000256|SAAS:SAAS00767022}.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a
CC       quinol. {ECO:0000256|HAMAP-Rule:MF_00225,
CC       ECO:0000256|SAAS:SAAS00767028}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; orotate from (S)-dihydroorotate (quinone route): step
CC       1/1. {ECO:0000256|SAAS:SAAS00767035}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00225}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00225}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00225}.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 2 subfamily. {ECO:0000256|SAAS:SAAS00767034}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001622; ACS54533.1; -; Genomic_DNA.
DR   RefSeq; WP_012755949.1; NC_012850.1.
DR   ProteinModelPortal; C6B0B4; -.
DR   EnsemblBacteria; ACS54533; ACS54533; Rleg_0222.
DR   KEGG; rlg:Rleg_0222; -.
DR   HOGENOM; HOG000225103; -.
DR   KO; K00254; -.
DR   OMA; LQNAMGF; -.
DR   OrthoDB; POG091H018H; -.
DR   UniPathway; UPA00070; UER00946.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04738; DHOD_2_like; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00225; DHO_dh_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005720; Dihydroorotate_DH.
DR   InterPro; IPR005719; Dihydroorotate_DH_2.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Pfam; PF01180; DHO_dh; 1.
DR   TIGRFAMs; TIGR01036; pyrD_sub2; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B0B4.
DR   SWISS-2DPAGE; C6B0B4.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00225};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00225,
KW   ECO:0000256|SAAS:SAAS00459606};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_00225, ECO:0000256|SAAS:SAAS00243566};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00225,
KW   ECO:0000256|SAAS:SAAS00767044};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00225,
KW   ECO:0000256|SAAS:SAAS00459560, ECO:0000313|EMBL:ACS54533.1};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00225,
KW   ECO:0000256|SAAS:SAAS00767026}.
FT   DOMAIN       45    338       DHO_dh. {ECO:0000259|Pfam:PF01180}.
FT   NP_BIND      62     66       FMN. {ECO:0000256|HAMAP-Rule:MF_00225}.
FT   NP_BIND     316    317       FMN. {ECO:0000256|HAMAP-Rule:MF_00225}.
FT   REGION      111    115       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00225}.
FT   REGION      244    245       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00225}.
FT   ACT_SITE    173    173       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00225}.
FT   BINDING      66     66       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00225}.
FT   BINDING      86     86       FMN; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00225}.
FT   BINDING     139    139       FMN. {ECO:0000256|HAMAP-Rule:MF_00225}.
FT   BINDING     170    170       FMN. {ECO:0000256|HAMAP-Rule:MF_00225}.
FT   BINDING     170    170       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00225}.
FT   BINDING     175    175       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00225}.
FT   BINDING     215    215       FMN. {ECO:0000256|HAMAP-Rule:MF_00225}.
FT   BINDING     243    243       FMN; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00225}.
FT   BINDING     266    266       FMN; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00225}.
FT   BINDING     295    295       FMN; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00225}.
SQ   SEQUENCE   362 AA;  38722 MW;  13F90CED094E4FF5 CRC64;
     MIDPFKRLAR KGLFLFDPET AHGMSIAALK SGLVPACQIT PDPRLRQTVA GLTFENPLGM
     AAGYDKNAEV PEALLKLGFG FTEIGTVTPK PQSGNPRPRI FRLVEDEAVI NRLGFNNEGH
     DAAFGHLAAL RGGGMIGVNI GANKDSEDRI ADYVAGIRRF YSVARYFTAN ISSPNTPGLR
     DLQGRESLAV LLSAVLAARD EMAAASGRTI PVFLKIAPDL TEEGMDDIAA EALSHGLDGL
     IVSNTTLSRD GLKDQRQAKE AGGLSGVPLF EKSTAVLARM RKRVGPDLPI IGVGGVSSAE
     TALEKIRAGA DLVQLYSCMV YEGPGLAGDI VRGLSKLLDR EKAASIRDLR DVRLDYWAAR
     KV
//

If you have problems or comments...

PBIL Back to PBIL home page