ID   H2CBA4_9LEPT            Unreviewed;       446 AA.
AC   H2CBA4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EHQ05244.1};
GN   ORFNames=Lepil_0540 {ECO:0000313|EMBL:EHQ05244.1};
OS   Leptonema illini DSM 21528.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptonema.
OX   NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ05244.1, ECO:0000313|Proteomes:UP000005737};
RN   [1] {ECO:0000313|EMBL:EHQ05244.1, ECO:0000313|Proteomes:UP000005737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ05244.1,
RC   ECO:0000313|Proteomes:UP000005737};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; JH597773; EHQ05244.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2CBA4; -.
DR   STRING; 183.GCA_002009735_00230; -.
DR   HOGENOM; CLU_031864_5_3_12; -.
DR   Proteomes; UP000005737; Unassembled WGS sequence.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProt.
DR   CDD; cd02947; TRX_family; 1.
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; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
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.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005737}.
FT   DOMAIN          1..198
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   446 AA;  48954 MW;  97E3CA2650BB4970 CRC64;
     MAEHRFIQEI QASQYEALVV GAKGPVILDF YSEDCVPCEA LASKFESLAD LFGEEIRFYK
     IFRQQNRELA TELGVRSSPT LIFYRDGQEV GRRLTGAIRK KDIVEQIGQL IPADAFNRLY
     AKRSSSTREV DVAILGGGPA GLTAALYAAQ ARLNVLVIDQ DLTGGQVKTT HMISNYPGTG
     GPVSGWELSE KMLRQVQEAG ADVIAAVDVT MAKLKSGESV IRIDDEIEVH ARSVILATGA
     EPRSLGVPGE KEFRGRGISY CATCDGKYYD GKEVIVIGGG NSAVEESIFL TKFATRVTIV
     HQFDHLQANK QAQEEAFAND RIRFVWNSEP RRFEQLADGR MKLSVENVKT GETDEMITDG
     VFVFVGMVPN LTGIESDVPI EKNQWGYVIT DEDMETNVPG IFAIGDVRAK KYRQAAIAVG
     EGCIAAIACE KRLEAMKHSE KELASV
//