ID F0RSR5_SPHGB Unreviewed; 282 AA.
AC F0RSR5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:ADY13965.1};
GN OrderedLocusNames=SpiBuddy_2146 {ECO:0000313|EMBL:ADY13965.1};
OS Sphaerochaeta globosa (strain ATCC BAA-1886 / DSM 22777 / Buddy)
OS (Spirochaeta sp. (strain Buddy)).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC Sphaerochaeta.
OX NCBI_TaxID=158189 {ECO:0000313|EMBL:ADY13965.1, ECO:0000313|Proteomes:UP000008466};
RN [1] {ECO:0000313|Proteomes:UP000008466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1886 / DSM 22777 / Buddy
RC {ECO:0000313|Proteomes:UP000008466};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Mikhailova N., Pagani I., Ritalahti K.M., Loeffler F.E.,
RA Woyke T.;
RT "Complete sequence of Spirochaeta sp. Buddy.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002541; ADY13965.1; -; Genomic_DNA.
DR RefSeq; WP_013607814.1; NC_015152.1.
DR AlphaFoldDB; F0RSR5; -.
DR STRING; 158189.SpiBuddy_2146; -.
DR KEGG; sbu:SpiBuddy_2146; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_0_12; -.
DR OrthoDB; 9778346at2; -.
DR Proteomes; UP000008466; 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008466}.
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 222
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 225
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 237
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 282 AA; 30643 MW; A79A5FDAF1990170 CRC64;
MNTILSKQRL SAEVFRMEIE AKEIAEARKP GQFIILQMGG DFGERIPLTI ADADPAKGSI
TLIFQAVGET THRLALLEKG DFIENLLGPL GRPTDIKKYG KVVCVGGGIG VAPLFPIVQG
MKMAGNEVKV IMGARNKDLL IMEDDMKATA DEVIVVTDDG SYGRKALVTE PLKELCETYK
PDCVVIIGPP IMMKFAALTT KPYGIHTIVS LNTIMIDGTG MCGGCRVTIG GKTKFVCVDG
PEFDGHLVDW DNMLLRLGTY KSKEQEAHHR CHVGLHITEG EA
//
