ID A0A1H3B3G2_9ACTN Unreviewed; 552 AA.
AC A0A1H3B3G2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Thioredoxin reductase (NADPH) {ECO:0000313|EMBL:SDX36463.1};
GN ORFNames=SAMN05660209_00289 {ECO:0000313|EMBL:SDX36463.1};
OS Geodermatophilus africanus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137993 {ECO:0000313|EMBL:SDX36463.1, ECO:0000313|Proteomes:UP000198921};
RN [1] {ECO:0000313|EMBL:SDX36463.1, ECO:0000313|Proteomes:UP000198921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45422 {ECO:0000313|EMBL:SDX36463.1,
RC ECO:0000313|Proteomes:UP000198921};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNOT01000001; SDX36463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3B3G2; -.
DR STRING; 1137993.SAMN05660209_00289; -.
DR OrthoDB; 109585at2; -.
DR Proteomes; UP000198921; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 5..128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 552 AA; 59123 MW; 0FBA16E9A8F4899B CRC64;
MARPVLLTVD DDPAVSRAVA RDLRRRYGEG HRVLRAGSGA EALEALRELK LRGDPVAVLL
ADHRMPEMNG VEFLERAMDL VPRARRALLT AYADTDAAIA AINVVDVDSY LLKPWDPPEE
KLYPVVDAML EAWRDTPDPE VRGVKLVGHR WSAPSFRARD LLARNAVPYR WFNVDEPDGR
RILAAAGAGP DDVPVIVTAD ARVLRRPTEA ELAAVAGLAV EAREEFYDLV VVGGGPAGLG
AAVYGASEGL RTVLVEREAT GGQAGQSSRI ENYLGFPDGV SGGQLADRAR RQAVKFGAEL
LLARDVVALE AHGPKRVLHL DDGRRIAAHA VVLATGVSYR SLGVDGVDDL TGRGVYYGSA
MTEAAECADS DVYIVGGANS AGQAAVFFSR YASSVSLLVR GSSLEASMSA YLIEQIAGIE
AIRVRTCTIV AQAQGDGHLE ALTVEDTRTG ERETLPASHL FVFIGGAPRT GWLDGAVVRD
ERGFIPTGPA LLREGRRPAG WDLDRDPYLL ETSLPGVFVA GDVRADSVKR VASAVGEGAM
AVTLVHRYLE ER
//
