ID D5UB81_BRAM5 Unreviewed; 275 AA.
AC D5UB81;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:ADG71954.1};
GN OrderedLocusNames=Bmur_1872 {ECO:0000313|EMBL:ADG71954.1};
OS Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS murdochii).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG71954.1, ECO:0000313|Proteomes:UP000001915};
RN [1] {ECO:0000313|EMBL:ADG71954.1, ECO:0000313|Proteomes:UP000001915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC {ECO:0000313|Proteomes:UP000001915};
RX PubMed=21304710; DOI=10.4056/sigs.831993;
RA Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL Stand. Genomic Sci. 2:260-269(2010).
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|PIRSR:PIRSR006816-2};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000256|PIRSR:PIRSR006816-2};
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DR EMBL; CP001959; ADG71954.1; -; Genomic_DNA.
DR RefSeq; WP_013114329.1; NC_014150.1.
DR AlphaFoldDB; D5UB81; -.
DR STRING; 526224.Bmur_1872; -.
DR KEGG; brm:Bmur_1872; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_0_12; -.
DR OrthoDB; 9778346at2; -.
DR Proteomes; UP000001915; 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; cd06219; DHOD_e_trans_like1; 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; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-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 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 4: Predicted;
KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
KW FAD {ECO:0000256|PIRSR:PIRSR006816-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR006816-1};
KW Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2}.
FT DOMAIN 1..96
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 63..65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
FT BINDING 224
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 227
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"
SQ SEQUENCE 275 AA; 30234 MW; 7AB676AB6C1EA692 CRC64;
MGYKIVAREQ WSEKVFMMKV VAPDIAKHRK AGNFIIFRLD EKGERIPLTI ADADAEAGTI
TIVTQSIGYS TAKLMELQVG DEILDVIGPL GQPTHIEKKD GIVLGVGGGV GIAPLHPIME
AHHKAGNKVI SILGARDKSL IIMEDMMRKI SDEVLICTDN GSYGEKGVVT NMIERIYDRG
DKISEVIAIG PAIMMKFVTI LTKKYNLPTV VSLNPIMIDG TGMCGCCRVK VGDETKFACV
EGPEFDGHLI DFDLLMKRQA MYKKEEHECN LKLAN
//
