ID F7YY76_9THEM Unreviewed; 279 AA.
AC F7YY76;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Sulfide dehydrogenase (Flavoprotein) subunit SudB {ECO:0000313|EMBL:AEH50897.1};
DE EC=1.8.1.- {ECO:0000313|EMBL:AEH50897.1};
GN ORFNames=Theth_0813 {ECO:0000313|EMBL:AEH50897.1};
OS Pseudothermotoga thermarum DSM 5069.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH50897.1, ECO:0000313|Proteomes:UP000006804};
RN [1] {ECO:0000313|EMBL:AEH50897.1, ECO:0000313|Proteomes:UP000006804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH50897.1,
RC ECO:0000313|Proteomes:UP000006804};
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., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermotoga thermarum DSM 5069.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002351; AEH50897.1; -; Genomic_DNA.
DR RefSeq; WP_013932119.1; NC_015707.1.
DR AlphaFoldDB; F7YY76; -.
DR STRING; 688269.Theth_0813; -.
DR KEGG; tta:Theth_0813; -.
DR PATRIC; fig|688269.3.peg.837; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_0_0; -.
DR OrthoDB; 9778346at2; -.
DR Proteomes; UP000006804; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UniProtKB-KW.
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 Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2};
KW Oxidoreductase {ECO:0000313|EMBL:AEH50897.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006804};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..94
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 220
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 223
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 235
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 279 AA; 30441 MW; 368FEAE3E9285DD3 CRC64;
MLNQIVKKSK LAPGVYEFYV ENPIIAAKAQ PGQFVVVIPS EKGERVPLTI ADAFDGNIRM
VVKVVGKSTA DLALKREGET LYGVVGPLGK PSEIKYYGNV LLVGGGVGIA AILPIAKALK
ALGNKVYAVL GGRSKDQVIL KDELEQYVDE ILVTTDDGSF GIKGVVTDGM DLILRKQRID
IAWAIGPTIM MKFCSLKARE YGLKIVVSLN PIMVDGTGMC GACRVTINGQ IKFACVDGPE
FDGTQVDWDE LLKRLQQYQE QEKLAFEKFK QKVGDLSWL
//
