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PYRDA_LACLC
ID   PYRDA_LACLC             Reviewed;         311 AA.
AC   Q53ZE5; P54321;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Dihydroorotate dehydrogenase A (fumarate);
DE            Short=DHOD A;
DE            Short=DHODase A;
DE            Short=DHOdehase A;
DE            EC=1.3.98.1;
GN   Name=pyrDA;
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCK436;
RA   Hall C.R., Dietrich F.S.;
RT   "Lactococcus lactis subsp. cremoris gene encoding the biosynthetic enzyme
RT   dihydroorotate dehydrogenase family 1a.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC       fumarate as the electron acceptor. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + fumarate = orotate + succinate;
CC         Xref=Rhea:RHEA:30059, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:30839, ChEBI:CHEBI:30864; EC=1.3.98.1;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY323899; AAQ01776.1; -; Genomic_DNA.
DR   RefSeq; WP_011834894.1; NZ_VERW01000005.1.
DR   AlphaFoldDB; Q53ZE5; -.
DR   SMR; Q53ZE5; -.
DR   DrugBank; DB03247; Flavin mononucleotide.
DR   DrugBank; DB02262; Orotic acid.
DR   PATRIC; fig|1359.23.peg.1510; -.
DR   OMA; CPISFIT; -.
DR   UniPathway; UPA00070; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1990663; F:dihydroorotate dehydrogenase (fumarate) activity; IEA:UniProtKB-EC.
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; cd04741; DHOD_1A_like; 1.
DR   Gene3D; 2.30.26.10; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00224; DHO_dh_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR033886; DHOD_1A.
DR   InterPro; IPR023359; Dihydro_DH_chainA_dom2.
DR   InterPro; IPR005720; Dihydroorotate_DH.
DR   InterPro; IPR024920; Dihydroorotate_DH_1.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Pfam; PF01180; DHO_dh; 1.
DR   PIRSF; PIRSF000164; DHO_oxidase; 1.
DR   TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.
FT   CHAIN           1..311
FT                   /note="Dihydroorotate dehydrogenase A (fumarate)"
FT                   /id="PRO_0000148394"
FT   ACT_SITE        130
FT                   /note="Nucleophile"
FT   BINDING         19
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         43..44
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         193..194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         249..250
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..272
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  34210 MW;  30157E3C2791CDD7 CRC64;
     MLNTTFANAK FANPFMNASG VHCMTIEDLE ELKASQAGAY ITKSSTLEKR EGNPLPRYVD
     LELGSINSMG LPNLGFDYYL DYVLKNQKEN AQEGPIFFSI AGMSAAENIA MLKKIQESDF
     SGITELNLSC PNVPGKPQLA YDFEATEKLL KEVFTFFTKP LGVKLPPYFD LVHFDIMAEI
     LNQFPLTYVN SVNSIGNGLF IDPEAESVVI KPKDGFGGIG GAYIKPTALA NVRAFYTRLK
     PEIQIIGTGG IETGQDAFEH LLCGATMLQI GTALHKEGPA IFDRIIKELE EIMNQKGYQS
     IADFHGKLKS L
 
 
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