ID E4Q1J1_CALOW Unreviewed; 255 AA.
AC E4Q1J1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=Calow_1167 {ECO:0000313|EMBL:ADQ04725.1};
OS Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632518 {ECO:0000313|EMBL:ADQ04725.1, ECO:0000313|Proteomes:UP000006889};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OL;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor owensensis OL.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ04725.1, ECO:0000313|Proteomes:UP000006889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700167 / DSM 13100 / OL
RC {ECO:0000313|Proteomes:UP000006889};
RX PubMed=21216991; DOI=10.1128/JB.01515-10;
RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL J. Bacteriol. 193:1483-1484(2011).
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}.
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DR EMBL; CP002216; ADQ04725.1; -; Genomic_DNA.
DR RefSeq; WP_013412101.1; NC_014657.1.
DR AlphaFoldDB; E4Q1J1; -.
DR STRING; 632518.Calow_1167; -.
DR KEGG; cow:Calow_1167; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_2_9; -.
DR OrthoDB; 9789468at2; -.
DR UniPathway; UPA00070; UER00945.
DR Proteomes; UP000006889; 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: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 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:UP000006889};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01211}.
FT DOMAIN 1..100
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 75..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 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 225
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 228
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 255 AA; 28235 MW; 1965AF4D41BEB641 CRC64;
MKLLEVEIEE NVKIANEIFL LSFESEYLAE NFKPGNFVNI LIDKDSIYPL LRRPFSISFV
EGKRVYIGYK VVGKGTNLLS QKSKGEAIDV LGPLGNSFLT DIFDGKVAVI GGGVGIFPLV
GLCKELKNRG NKVDVFLGFR DLDSMFLVER FKDICDNTLI ATDDGSSGYK GNVVELFKAN
FSKAEYKVVF CCGPKPMLKA IKNLNLPVKC YASLEEKMAC GIGACLCCSI RGKDEKMYHI
CSDGPVFDIM EVEIE
//
