ID E8R0I8_ISOPI Unreviewed; 298 AA.
AC E8R0I8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Dihydroorotate dehydrogenase, electron transfer subunit, iron-sulfur cluster binding domain protein {ECO:0000313|EMBL:ADV63320.1};
GN OrderedLocusNames=Isop_2754 {ECO:0000313|EMBL:ADV63320.1};
OS Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Isosphaera.
OX NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV63320.1, ECO:0000313|Proteomes:UP000008631};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43644;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders E., Brettin T.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.;
RT "The complete sequence of chromosome of Isophaera pallida ATCC 43644.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADV63320.1, ECO:0000313|Proteomes:UP000008631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43644 / DSM 9630 / IS1B
RC {ECO:0000313|Proteomes:UP000008631};
RX PubMed=21475588; DOI=10.4056/sigs.1533840;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Isosphaera pallida type strain (IS1B).";
RL Stand. Genomic Sci. 4:63-71(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR006816-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR006816-1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002353; ADV63320.1; -; Genomic_DNA.
DR AlphaFoldDB; E8R0I8; -.
DR STRING; 575540.Isop_2754; -.
DR KEGG; ipa:Isop_2754; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_2_0; -.
DR InParanoid; E8R0I8; -.
DR Proteomes; UP000008631; 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; 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 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|PIRSR:PIRSR006816-2};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|PIRSR:PIRSR006816-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR006816-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR006816-2};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR006816-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008631};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 12..114
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 89..90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
FT BINDING 257
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 262
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 265
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 282
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 298 AA; 31896 MW; 709A0FC2822A0AC9 CRC64;
MNSSATVPTM QPVYRRVEVI ANHAMTPTRF RTRLAVPEIA SVIRPGQFVM VRATGEPVSD
PLLARALALY DVTEDLGAVD VVYDLHGKGT RTLARVRPGD SVTILGPLGR DFGLPPDDGR
VVWMVAGGIG QTPFLALAKW WMGRFAYAGI NPCYGNPAPR EVVLMHGGSN AQAVEGLEDF
LAVGVVGLVA TEDGSRGWRG RVTDLVEQRR READAGLCEP PGLIITCGPS AMMAAVARLA
QRMGVPCRAS LENPMACGFG ACFSCVAPIR QSDGTTDLKR VCLDGPVFDA ETVVWDEM
//
