ID E1RBA1_SEDSS Unreviewed; 412 AA.
AC E1RBA1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADK79631.1};
GN OrderedLocusNames=Spirs_0484 {ECO:0000313|EMBL:ADK79631.1};
OS Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
OS (Spirochaeta smaragdinae).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Sediminispirochaeta.
OX NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK79631.1, ECO:0000313|Proteomes:UP000002318};
RN [1] {ECO:0000313|EMBL:ADK79631.1, ECO:0000313|Proteomes:UP000002318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228
RC {ECO:0000313|Proteomes:UP000002318};
RX PubMed=21304743; DOI=10.4056/sigs.1143106;
RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M.,
RA Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M.,
RA Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT 4228).";
RL Stand. Genomic Sci. 3:136-144(2010).
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DR EMBL; CP002116; ADK79631.1; -; Genomic_DNA.
DR RefSeq; WP_013253095.1; NC_014364.1.
DR AlphaFoldDB; E1RBA1; -.
DR STRING; 573413.Spirs_0484; -.
DR KEGG; ssm:Spirs_0484; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_3_12; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000002318; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002318}.
FT DOMAIN 9..299
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 312..397
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF00085"
SQ SEQUENCE 412 AA; 45186 MW; 404F446E49321EED CRC64;
MREKKREQYD VVIIGGGAAG LTAGIYCGRA RLKTLIIEKA LVGGLATYTN EIANFPGFPE
PLPGLDLMNL FKKQAEGFGV KFKGTDVKSV NFEGDVKIVE TFRNIFEAKA VIVAAGGRPR
VTTAKNEEKY LFDKGISFCA TCDAAANTDK TVMVIGSGDA AIEEGMFLTK FAKKVIVSVI
HDEGKMDCNE IAREQALSNP KMEFKWNTLA DSFEGEEQLE RVVLKNLKTG ELDPVAVDTC
FEFIGYLPNT EIFENILKLS KQKYVITNER METGIPGVFA AGDVREKELK QVSTAVGDGA
IAGVGSEKYI AETEMFEKQI MQKEKVGLIY VYSAINAPSR ELLPVLQETA ESYDGKIKMN
VIDLYKGKTL CDRLSCDIEP MTIFYTKNGE VSAVSTDCST PAVKKQLDAL LA
//