ID A0A1T5L2M1_9CLOT Unreviewed; 363 AA.
AC A0A1T5L2M1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit {ECO:0000256|ARBA:ARBA00018101};
DE EC=1.3.1.14 {ECO:0000256|ARBA:ARBA00012061};
DE AltName: Full=Dihydroorotate oxidase B {ECO:0000256|ARBA:ARBA00029718};
DE AltName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
DE AltName: Full=Orotate reductase (NADH) {ECO:0000256|ARBA:ARBA00032046};
GN ORFNames=SAMN02194393_02318 {ECO:0000313|EMBL:SKC69859.1};
OS Maledivibacter halophilus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Maledivibacter.
OX NCBI_TaxID=36842 {ECO:0000313|EMBL:SKC69859.1, ECO:0000313|Proteomes:UP000190285};
RN [1] {ECO:0000313|EMBL:SKC69859.1, ECO:0000313|Proteomes:UP000190285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:SKC69859.1,
RC ECO:0000313|Proteomes:UP000190285};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC NAD(+) as electron acceptor. {ECO:0000256|ARBA:ARBA00003616}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate;
CC Xref=Rhea:RHEA:13513, ChEBI:CHEBI:15378, ChEBI:CHEBI:30839,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001903};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004715}.
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; FUZT01000005; SKC69859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5L2M1; -.
DR STRING; 36842.SAMN02194393_02318; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000190285; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004589; F:dihydroorotate dehydrogenase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.30.26.10; Dihydroorotate Dehydrogenase A, chain A, domain 2; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR023359; Dihydro_DH_chainA_dom2.
DR InterPro; IPR005720; Dihydroorotate_DH_cat.
DR PANTHER; PTHR48109:SF1; DIHYDROOROTATE DEHYDROGENASE (FUMARATE); 1.
DR PANTHER; PTHR48109; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF01180; DHO_dh; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000190285}.
FT DOMAIN 298..325
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 326..355
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 363 AA; 39977 MW; BB5D4771F8280A0D CRC64;
MYNLLGIELK SPIIIGSGPL SYNAQAIKKL FDAGAGAVVT KTIRREKAIN PAPHMALTTN
NSLINNEKWT DVNPETWINR EIPKLKDMGV VTIVSIGHTL EESSELVEKI EKAGANIIEL
VSYDYKDLIP MVKDTKKRVD IPVIVKLPPR IDDIGNFSRK LEKAGADAIT ACDSVGPAFR
INIETGKPLL GGNGFGWLSG EVIKPIILHK IYEIKKKVNI PIIGLGGCMT GADAVEMIMA
GANFIGICTA PILKGENIIN KIYRDCLAHL ERLGYESIDE ALGIVQKNLG KSNERTKFQF
VYHEDKCTGC KLCEKVCGYG ARKLKDTMEF DEDECRYCGL CISICPTKAL KAIELENSYE
ETL
//
