PYRD_HELPG
ID PYRD_HELPG Reviewed; 351 AA.
AC B5Z6I2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Dihydroorotate dehydrogenase (quinone) {ECO:0000255|HAMAP-Rule:MF_00225};
DE EC=1.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00225};
DE AltName: Full=DHOdehase {ECO:0000255|HAMAP-Rule:MF_00225};
DE Short=DHOD {ECO:0000255|HAMAP-Rule:MF_00225};
DE Short=DHODase {ECO:0000255|HAMAP-Rule:MF_00225};
DE AltName: Full=Dihydroorotate oxidase {ECO:0000255|HAMAP-Rule:MF_00225};
GN Name=pyrD {ECO:0000255|HAMAP-Rule:MF_00225}; OrderedLocusNames=HPG27_417;
OS Helicobacter pylori (strain G27).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27;
RX PubMed=18952803; DOI=10.1128/jb.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC quinone as electron acceptor. {ECO:0000255|HAMAP-Rule:MF_00225}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate;
CC Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00225};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00225};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_00225};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC orotate from (S)-dihydroorotate (quinone route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00225}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00225}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00225};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00225}.
CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00225}.
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DR EMBL; CP001173; ACI27181.1; -; Genomic_DNA.
DR RefSeq; WP_000966728.1; NC_011333.1.
DR PDB; 6B8S; X-ray; 2.25 A; A/B=1-351.
DR PDBsum; 6B8S; -.
DR AlphaFoldDB; B5Z6I2; -.
DR SMR; B5Z6I2; -.
DR EnsemblBacteria; ACI27181; ACI27181; HPG27_417.
DR KEGG; hpg:HPG27_417; -.
DR HOGENOM; CLU_013640_2_0_7; -.
DR OMA; ERIKMGA; -.
DR OrthoDB; 1109542at2; -.
DR UniPathway; UPA00070; UER00946.
DR Proteomes; UP000001735; 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-UniRule.
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; IPR012135; Dihydroorotate_DH_1_2.
DR InterPro; IPR005719; Dihydroorotate_DH_2.
DR InterPro; IPR001295; Dihydroorotate_DH_CS.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Flavoprotein; FMN; Membrane; Oxidoreductase;
KW Pyrimidine biosynthesis.
FT CHAIN 1..351
FT /note="Dihydroorotate dehydrogenase (quinone)"
FT /id="PRO_1000100267"
FT ACT_SITE 181
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 67..71
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 91
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 116..120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 145
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 178
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 214
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 242
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 243..244
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 262
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 291
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT BINDING 312..313
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00225"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:6B8S"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:6B8S"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 266..280
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:6B8S"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:6B8S"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:6B8S"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:6B8S"
SQ SEQUENCE 351 AA; 38985 MW; D9323D5317035868 CRC64;
MLYPLVKKYL FSLDAEDAHE KVCKILRTLS KSSFLCSLIH SQWGYKNPKL ENEILGLNFP
NPLGLAAGFD KNASMLRALI AFGFGYLEAG TLTNEAQVGN ERPRLFRHIE EESLQNAMGF
NNYGAVLGAR SFNRFAPYKT PIGINLGKNK HIEQAHALED YKAVLNQCLN IGDYYTFNLS
SPNTPNLRDL QNKAFVNELF CMAKEMTHKP LFLKIAPDLE IDDMLEIVNS AIEAGAHGII
ATNTTIDKSL VFAPKEMGGL SGKCLTKKSR EVFKELAKAF FNKSVLVSVG GISDAKEAYE
RIKMGASLLQ IYSAFIYNGP NLCQNILKDL VKLLQKDGFL SVKEAIGADL R
