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Database: UniProt
Entry: R6ASL9_9CLOT
LinkDB: R6ASL9_9CLOT
Original site: R6ASL9_9CLOT 
ID   R6ASL9_9CLOT            Unreviewed;       254 AA.
AC   R6ASL9;
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=BN491_00917 {ECO:0000313|EMBL:CDA51764.1};
OS   Clostridium sp. CAG:138.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262775 {ECO:0000313|EMBL:CDA51764.1, ECO:0000313|Proteomes:UP000017905};
RN   [1] {ECO:0000313|EMBL:CDA51764.1, ECO:0000313|Proteomes:UP000017905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:138 {ECO:0000313|Proteomes:UP000017905};
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:CDA51764.1}.
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DR   EMBL; CBBZ010000072; CDA51764.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6ASL9; -.
DR   STRING; 1262775.BN491_00917; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000017905; 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; 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; PR00410; PHEHYDRXLASE.
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}; Reference proteome {ECO:0000313|Proteomes:UP000017905};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01211}.
FT   DOMAIN          1..97
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         48..51
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         72..73
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         241
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   254 AA;  27563 MW;  D96E5B21839DD7CC CRC64;
     MIQSLFQIVS NECIARNTYK MVLSGDVSSI NRPGQFVNIK LKGFFLRRPI SVCDIDRNEN
     TLTIVYKVVG KGTEFMSRLP MNEQLDVLAG LGNGYDTSLC GEHPLLIGGG AGVPPMFLLA
     KQLISEGKIP MVIAGFNTVD ECFFEDEFKK IGARIIVATA DGSCGVKGFV TDAMRCFNAE
     SNDGITAYTD YCACGPEPML KAVFDIAETS GQLSFEERMG CGFGACMGCS CKTKYGSKRI
     CKDGPVLVSE EVIW
//
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