PYRD_DICDI
ID PYRD_DICDI Reviewed; 370 AA.
AC P07670; Q551R6; Q86AD1;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Dihydroorotate dehydrogenase;
DE Short=DHOD;
DE Short=DHODase;
DE Short=DHOdehase;
DE EC=1.3.-.- {ECO:0000269|PubMed:2996629};
DE AltName: Full=Dihydroorotate oxidase;
GN Name=pyr4; ORFNames=DDB_G0276331;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=2996629; DOI=10.1016/s0300-9084(85)80197-8;
RA Jacquet M., Kalekine M., Boy-Marcotte E.;
RT "Sequence analysis of a Dictyostelium discoideum gene coding for an active
RT dihydroorotate dehydrogenase in yeast.";
RL Biochimie 67:583-588(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC (PubMed:2996629). Participates in the pyrimidine biosynthetic pathway
CC (PubMed:2996629). {ECO:0000269|PubMed:2996629,
CC ECO:0000303|PubMed:2996629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + A = AH2 + orotate; Xref=Rhea:RHEA:18073,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:30839,
CC ChEBI:CHEBI:30864; Evidence={ECO:0000269|PubMed:2996629};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18074;
CC Evidence={ECO:0000305|PubMed:2996629};
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 {ECO:0000305|PubMed:2996629}.
CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26674.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X02917; CAA26674.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AAFI02000014; EAL69246.1; -; Genomic_DNA.
DR PIR; A23559; A23559.
DR RefSeq; XP_643195.1; XM_638103.1.
DR AlphaFoldDB; P07670; -.
DR SMR; P07670; -.
DR STRING; 44689.DDB0185217; -.
DR PaxDb; P07670; -.
DR EnsemblProtists; EAL69246; EAL69246; DDB_G0276331.
DR GeneID; 8620469; -.
DR KEGG; ddi:DDB_G0276331; -.
DR dictyBase; DDB_G0276331; pyr4.
DR eggNOG; ENOG502S3NB; Eukaryota.
DR HOGENOM; CLU_785030_0_0_1; -.
DR InParanoid; P07670; -.
DR OMA; CPNEGHN; -.
DR PhylomeDB; P07670; -.
DR UniPathway; UPA00070; -.
DR PRO; PR:P07670; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IGI:dictyBase.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; ISS:dictyBase.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005720; Dihydroorotate_DH.
DR Pfam; PF01180; DHO_dh; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..370
FT /note="Dihydroorotate dehydrogenase"
FT /id="PRO_0000148498"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 82..83
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135..139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 270..271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 328..329
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 350..351
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT CONFLICT 60
FT /note="G -> E (in Ref. 1; CAA26674)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="E -> V (in Ref. 1; CAA26674)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="M -> I (in Ref. 1; CAA26674)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..152
FT /note="DIA -> GIT (in Ref. 1; CAA26674)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..255
FT /note="RLF -> GLL (in Ref. 1; CAA26674)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> P (in Ref. 1; CAA26674)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="V -> D (in Ref. 1; CAA26674)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="T -> I (in Ref. 1; CAA26674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 40520 MW; B0E6BCE179A7D544 CRC64;
MEWPINKPIY DINKSWEDNL ENGPFIEGYK KVDRNDNKDP SKYIDFLGQK LASPIGVPAG
PLLNSQWVKF ALEAGFDLPT YKTIRSHEHF GHPVPNVMYL DLESEDKQFT KSDSGSTLHA
TQTIPTTMDQ LAITNSFGMP SMGKEYLYKD IALAHSYLGS GQSMIVSITG TASSAHDFLQ
DFVDTVRIAC DAGAKMVEVN YSCPNVVTGE GQIYHNPDAV YEISSTLVKE LSSKNIPLII
KVGVMDDLEK MERLFQQAER AGVAAIAGIN TLSMKVTDKI TGEPSLGASR LTSGVCGAPI
RSAALDWVST ASSIIKKQNS KLKLLGCGGI VKPEHFDDFL NSGADIAMSA TGLMWDPYIA
MKWHNNNKNN
