ID F1T524_9ACTN Unreviewed; 334 AA.
AC F1T524;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative thioredoxin-disulfide reductase {ECO:0000313|EMBL:EGF23790.1};
GN ORFNames=HMPREF0091_10737 {ECO:0000313|EMBL:EGF23790.1};
OS Fannyhessea vaginae DSM 15829.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Fannyhessea.
OX NCBI_TaxID=525256 {ECO:0000313|EMBL:EGF23790.1, ECO:0000313|Proteomes:UP000005947};
RN [1] {ECO:0000313|EMBL:EGF23790.1, ECO:0000313|Proteomes:UP000005947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15829 {ECO:0000313|EMBL:EGF23790.1,
RC ECO:0000313|Proteomes:UP000005947};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000849};
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:EGF23790.1}.
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DR EMBL; ACGK02000001; EGF23790.1; -; Genomic_DNA.
DR RefSeq; WP_006302919.1; NZ_ADNA01000029.1.
DR AlphaFoldDB; F1T524; -.
DR GeneID; 78489542; -.
DR eggNOG; COG0492; Bacteria.
DR OrthoDB; 109585at2; -.
DR Proteomes; UP000005947; Unassembled WGS sequence.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
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 PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_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:UP000005947}.
FT DOMAIN 15..312
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 334 AA; 36745 MW; FF4F498ACB0E3458 CRC64;
MNTTTTEQTE QPTLKDLVII GGGPAGLSAA LYAQRALLDI VILEQEALGG QMIVTDKIDN
YLGVPHINGY ELSEIMHKQV KDMDVPLCME RVDSLKRFED EQGLSYFLVH TSRHSFKTKA
VLIACGATAK EAEFKGESRY TGHGVSYCAT CDAMFYRDKP VYVVGGGNAA CEEGLFLARF
AKKVTLLVRR DVLRAQDGVI RQVQENPKMV IVYNTRIKEL AGESDEGFTS ITLENTKTRS
TETITCEPHD IGVFVFAGRK PMNQLVGQFV DTDKNGFIKT DDHMQTRTEG LYAAGDVRDK
VLRQLITAAS DGAVAATSAA SYIRKLKRAA KTNS
//
