ID A0A0B4RD43_9BACL Unreviewed; 255 AA.
AC A0A0B4RD43;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 44.
DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit {ECO:0000256|ARBA:ARBA00069792, ECO:0000256|HAMAP-Rule:MF_01211};
DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit {ECO:0000256|ARBA:ARBA00082223, ECO:0000256|HAMAP-Rule:MF_01211};
GN Name=pyrK {ECO:0000256|HAMAP-Rule:MF_01211};
GN ORFNames=Plano_1951 {ECO:0000313|EMBL:AIY05916.1};
OS Planococcus sp. PAMC 21323.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Caryophanaceae;
OC Planococcus.
OX NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY05916.1, ECO:0000313|Proteomes:UP000031496};
RN [1] {ECO:0000313|EMBL:AIY05916.1, ECO:0000313|Proteomes:UP000031496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY05916.1,
RC ECO:0000313|Proteomes:UP000031496};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT Antarctica.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for channeling the electrons from the oxidation
CC of dihydroorotate from the FMN redox center in the PyrD type B subunit
CC to the ultimate electron acceptor NAD(+). {ECO:0000256|HAMAP-
CC Rule:MF_01211}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01211,
CC ECO:0000256|PIRSR:PIRSR006816-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01211,
CC ECO:0000256|PIRSR:PIRSR006816-1};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01211};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01211};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000256|PIRSR:PIRSR006816-2};
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, ECO:0000256|HAMAP-Rule:MF_01211}.
CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
CC {ECO:0000256|ARBA:ARBA00011669, ECO:0000256|HAMAP-Rule:MF_01211}.
CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000256|ARBA:ARBA00006422,
CC ECO:0000256|HAMAP-Rule:MF_01211}.
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DR EMBL; CP009129; AIY05916.1; -; Genomic_DNA.
DR RefSeq; WP_038704304.1; NZ_CP009129.1.
DR AlphaFoldDB; A0A0B4RD43; -.
DR STRING; 1526927.Plano_1951; -.
DR KEGG; pln:Plano_1951; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_2_9; -.
DR OrthoDB; 9778346at2; -.
DR UniPathway; UPA00070; UER00945.
DR Proteomes; UP000031496; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06218; DHOD_e_trans; 1.
DR FunFam; 2.10.240.10:FF:000001; Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit; 1.
DR FunFam; 3.40.50.80:FF:000017; Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit; 1.
DR Gene3D; 2.10.240.10; Dihydroorotate dehydrogenase, electron transfer subunit; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_01211; DHODB_Fe_S_bind; 1.
DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR037117; Dihydroorotate_DH_ele_sf.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR023455; Dihydroorotate_DHASE_ETsu.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR050353; PyrK_electron_transfer.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; NF000797; PRK00054.1-2; 1.
DR NCBIfam; NF000799; PRK00054.1-4; 1.
DR PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR PANTHER; PTHR43513:SF3; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT-RELATED; 1.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_01211};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_01211};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01211};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01211};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01211};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01211};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01211,
KW ECO:0000256|PIRSR:PIRSR006816-2};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01211}; Reference proteome {ECO:0000313|Proteomes:UP000031496};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01211}.
FT DOMAIN 2..102
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 53..56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT ECO:0000256|PIRSR:PIRSR006816-1"
FT BINDING 70..72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT ECO:0000256|PIRSR:PIRSR006816-1"
FT BINDING 77..78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT ECO:0000256|PIRSR:PIRSR006816-1"
FT BINDING 219
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 224
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 227
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 242
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 255 AA; 28018 MW; 76550883793ED44D CRC64;
MIKQERMQII NQQEIAHRIF ELTVQGALAN EMAEPGQFVH IRVADSFEPL LRRPISVASI
DLEASQFTMI YRAEGRGTGL LAEKKPGDTL DVLGPLGHGF PVEEAEKKAY LIGGGIGVPP
LYELAKQLNA RGIETVHILG FESKQAVFYE DKFRELGDTH IATVDGSHGT QGFVTHILNE
LAIDFDTYYS CGPTPMLEAV QWAYPQKKGF LSYEQRMGCG IGACFACVCR TTKSETDYIK
VCSDGPVFPA GVVIS
//
