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Entry: A0A517Y1I0_9BACT
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ID   A0A517Y1I0_9BACT        Unreviewed;       269 AA.
AC   A0A517Y1I0;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   18-JUN-2025, entry version 19.
DE   SubName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit {ECO:0000313|EMBL:QDU23627.1};
GN   Name=pyrK {ECO:0000313|EMBL:QDU23627.1};
GN   ORFNames=ETAA1_56310 {ECO:0000313|EMBL:QDU23627.1};
OS   Urbifossiella limnaea.
OC   Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Gemmatales;
OC   Gemmataceae; Urbifossiella.
OX   NCBI_TaxID=2528023 {ECO:0000313|EMBL:QDU23627.1, ECO:0000313|Proteomes:UP000319576};
RN   [1] {ECO:0000313|EMBL:QDU23627.1, ECO:0000313|Proteomes:UP000319576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ETA_A1 {ECO:0000313|EMBL:QDU23627.1,
RC   ECO:0000313|Proteomes:UP000319576};
RA   Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA   Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA   Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA   Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA   Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R.,
RA   Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA   Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT   "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT   characterization uncovers novel biology.";
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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   -!- SIMILARITY: Belongs to the PyrK family.
CC       {ECO:0000256|ARBA:ARBA00006422}.
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DR   EMBL; CP036273; QDU23627.1; -; Genomic_DNA.
DR   RefSeq; WP_145243857.1; NZ_CP036273.1.
DR   AlphaFoldDB; A0A517Y1I0; -.
DR   KEGG; uli:ETAA1_56310; -.
DR   OrthoDB; 9789468at2; -.
DR   Proteomes; UP000319576; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
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   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; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR050353; PyrK_electron_transfer.
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   PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
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|PIRSR:PIRSR006816-2};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR006816-
KW   2}; Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000319576};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..101
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         231
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         236
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         239
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         255
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   269 AA;  28444 MW;  46689699D0B550CE CRC64;
     MFQRTARVLE HVRLAERTYR VRLHCPDVAA AVRPGQFVML RLPGTSDPLL GRPFALYDLS
     PDSAALDVVY LVVGKMTGRL VDVQAGEALE VWGPLGKPFP EVGSVDEVRL VAGGIGQTPF
     LAYARELLGA RGYSGDAPRR RARRVTLYYG VRTAALAAGV DDFRAAGVTV KLASDDGSLG
     TKGFVTQLLA AEGPGGPVVG CGPEPMLHAL AKLTAGWGVS CHVSLETPMA CGVGACFSCV
     TKVKTADGWD YKRVCVDGPV FDAAALAWE
//
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