ID D4S7U4_9FIRM Unreviewed; 541 AA.
AC D4S7U4;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Putative thioredoxin-disulfide reductase {ECO:0000313|EMBL:EFF65644.1};
DE EC=1.8.1.9 {ECO:0000313|EMBL:EFF65644.1};
GN Name=trxB2 {ECO:0000313|EMBL:EFF65644.1};
GN ORFNames=HMPREF7545_1609 {ECO:0000313|EMBL:EFF65644.1};
OS Selenomonas noxia ATCC 43541.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=585503 {ECO:0000313|EMBL:EFF65644.1, ECO:0000313|Proteomes:UP000003701};
RN [1] {ECO:0000313|EMBL:EFF65644.1, ECO:0000313|Proteomes:UP000003701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43541 {ECO:0000313|EMBL:EFF65644.1,
RC ECO:0000313|Proteomes:UP000003701};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFF65644.1}.
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DR EMBL; ACKT01000034; EFF65644.1; -; Genomic_DNA.
DR AlphaFoldDB; D4S7U4; -.
DR eggNOG; COG0492; Bacteria.
DR eggNOG; COG3634; Bacteria.
DR HOGENOM; CLU_031864_5_4_9; -.
DR InParanoid; D4S7U4; -.
DR Proteomes; UP000003701; Unassembled WGS sequence.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR CDD; cd02974; AhpF_NTD_N; 1.
DR Gene3D; 3.40.30.80; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR044142; AhpF_NTD_N.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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; PF13192; Thioredoxin_3; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EFF65644.1}.
FT DOMAIN 2..293
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 464..532
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
SQ SEQUENCE 541 AA; 58664 MW; 3B4B7ADF330AF0F8 CRC64;
MYDAVIVGGG PAGLSAAIYL ARAKCKVLVI EKEKIGGQIT ITADVVNYPG TGRVSGSELA
AQMEQQARGF GAEFVSAEVI GLKLDQDVKE LETTAGTVQA LSVILATGAN PRKVGFLGEK
KFQGRGVAYC ATCDAEFFSG MDIFVIGGGL SAVEESMFLS RYGRSVTILV RSDKFRAPQT
TVDALANYPN IKVRFNTVVE RVDGETMISR ADFRNSATGE VEHYTAKEGE TFGVFVFAGY
LPNTGLFRDQ VVLNEDGYVI TNEEKETSVK GVFAAGDVCI KTLRQVVTAV SDGAISAVAA
ERHAAALHDR LKLPAFVRAE VDTNRFEQRK SSIEKEAAEG NETNFISAEI REQLAVVFDK
FAAPVKVVGH YDDGDLSREL RGFMDEFAGL TDKVSYEERK DANGAPGLEL FYADGTPSGI
TFHAVPGGHE FNSFILALYN VAGPGQELRP ETRAKIEQIS APADVKVLMS LSCTMCPDVV
AAVQRIAAER KDIRADIYDI RYFPELKEKY SVMSVPCMVV GEELHFGKKN IDEVADILGN
R
//
