ID R6FUC3_9CLOT Unreviewed; 245 AA.
AC R6FUC3;
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=BN542_01996 {ECO:0000313|EMBL:CDB16818.1};
OS Clostridium sp. CAG:221.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB16818.1, ECO:0000313|Proteomes:UP000018176};
RN [1] {ECO:0000313|EMBL:CDB16818.1, ECO:0000313|Proteomes:UP000018176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:221 {ECO:0000313|Proteomes:UP000018176};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:CDB16818.1}.
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DR EMBL; CBDC010000117; CDB16818.1; -; Genomic_DNA.
DR AlphaFoldDB; R6FUC3; -.
DR UniPathway; UPA00070; UER00945.
DR Proteomes; UP000018176; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 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}; Membrane {ECO:0000256|SAM:Phobius};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01211}.
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..94
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 47..50
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 69..70
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 212
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 217
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 220
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 232
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 245 AA; 27183 MW; 930058EF14904C71 CRC64;
MKYTRAKILS NKKIVDGIYE MVVAEDSKVK PGQFYMLKHQ GGTLLPRPIS ISESKDGKVT
FVYATVGKGT KEFANLKEND YIELTGPLGN GFDVDKKYGN VALVSGGIGI APMVMLAREL
RKRNKGMKLD LYAGFRDEIY LTNEMCEYIN EGYVSTNTGK YGHHGFITDI LKVDEYDTVL
CCGPEVMMKK VAEMCKMHGV QVFVSMEKHM ACGVGACLVC TCKTKDGNKR TCKDGPVFDG
NYVEL
//
