ID R6LSC0_9CLOT Unreviewed; 261 AA.
AC R6LSC0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit {ECO:0000256|HAMAP-Rule:MF_01211};
DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit {ECO:0000256|HAMAP-Rule:MF_01211};
GN Name=pyrK {ECO:0000256|HAMAP-Rule:MF_01211};
GN ORFNames=BN565_01041 {ECO:0000313|EMBL:CDB88840.1};
OS Clostridium sp. CAG:253.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262785 {ECO:0000313|EMBL:CDB88840.1, ECO:0000313|Proteomes:UP000018071};
RN [1] {ECO:0000313|EMBL:CDB88840.1, ECO:0000313|Proteomes:UP000018071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:253 {ECO:0000313|Proteomes:UP000018071};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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|HAMAP-Rule:MF_01211}.
CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
CC {ECO:0000256|HAMAP-Rule:MF_01211}.
CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000256|ARBA:ARBA00006422,
CC ECO:0000256|HAMAP-Rule:MF_01211}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDB88840.1}.
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DR EMBL; CBEI010000017; CDB88840.1; -; Genomic_DNA.
DR AlphaFoldDB; R6LSC0; -.
DR STRING; 1262785.BN565_01041; -.
DR UniPathway; UPA00070; UER00945.
DR Proteomes; UP000018071; Unassembled WGS sequence.
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:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06218; DHOD_e_trans; 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; IPR008333; Cbr1-like_FAD-bd_dom.
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; IPR017938; Riboflavin_synthase-like_b-brl.
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; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
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|HAMAP-Rule:MF_01211, ECO:0000256|PIRSR:PIRSR006816-2};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_01211};
KW FAD {ECO:0000256|HAMAP-Rule:MF_01211, ECO:0000256|PIRSR:PIRSR006816-1};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01211,
KW ECO:0000256|PIRSR:PIRSR006816-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01211};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01211,
KW ECO:0000256|PIRSR:PIRSR006816-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01211};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01211};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01211}.
FT DOMAIN 4..106
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 57..60
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 74..76
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 81..82
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 221
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 226
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 229
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 248
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 261 AA; 28463 MW; A6818AEF1446ADB4 CRC64;
MADKKKTMAV IKSQENITKD IFSMWLEFEK ESNVVENAIP GQFISMYSSD GSRLLPRPIS
ICEIDKDSGS LRVVYRVVGK GTDEFSKMKK GEKIPVVGPL GNGFSLKGGK AVLIGGGIGI
PPMLELAKTL NSKENVSVVL GYRDNDLFLK NEFEPYANVY VSTEDGSVGT KGNVIDAIKE
NVLEADVIYS CGPIPMLRGV KAYAQEKNIE AQISMEEKMA CGIGACLGCV CKSKEIDDHS
KVHNKRICKD GPVFNAEDIE I
//
