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Database: UniProt
Entry: A0A0M2HHA5_9MICO
LinkDB: A0A0M2HHA5_9MICO
Original site: A0A0M2HHA5_9MICO 
ID   A0A0M2HHA5_9MICO        Unreviewed;       550 AA.
AC   A0A0M2HHA5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:KJL43685.1};
DE            EC=1.8.1.9 {ECO:0000313|EMBL:KJL43685.1};
GN   Name=trxB_2 {ECO:0000313|EMBL:KJL43685.1};
GN   ORFNames=RS82_01381 {ECO:0000313|EMBL:KJL43685.1};
OS   Microbacterium trichothecenolyticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL43685.1, ECO:0000313|Proteomes:UP000034098};
RN   [1] {ECO:0000313|EMBL:KJL43685.1, ECO:0000313|Proteomes:UP000034098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL43685.1,
RC   ECO:0000313|Proteomes:UP000034098};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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:KJL43685.1}.
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DR   EMBL; JYJA01000030; KJL43685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2HHA5; -.
DR   PATRIC; fig|69370.6.peg.1419; -.
DR   Proteomes; UP000034098; Unassembled WGS sequence.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KJL43685.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034098}.
FT   DOMAIN          15..119
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
SQ   SEQUENCE   550 AA;  58651 MW;  C590D927F9639F45 CRC64;
     MGNAKMTQRE FERMMKPALT DAQWERLLSF GEPHDVEAGE YLFEAGDLDY DLILVDTGEL
     EIVRVAFGWV GETHVGTMGP RSFVGELGLL NGQGAFLSAR ATKTGRMLRV SRERLRVLMA
     EDDELCDIIL HALWARREIL RTGPAALTLK LVGPRSSRDF LALRRFAERV DLVHTAIELA
     PGDLWTLGEH GIGLDDLPVA FIQGEAMKNA TPGMVAERLG LSYQGRADEV VDLVVVGGGP
     AGLAAAIYGA SEGLSTVLLD AVAPGGQAAA TSRIENFLGF PFGVSGGDLI GQASLQALKF
     GVRVYAPCEA ADLRPAGRDL DVTLTDGRVI RARTAIVTSG AAYRTLDLER WNEFEGAGIY
     YAATPLELRQ VFESPVVVVG GANSAGQASL YLAANGCPVH LVVRGSDLGS RMSSYLVDRL
     LEDPRIDVHT GSRVTALGGG SALESVSIDS IGDVAARGLF CFIGAEPATS WLAELDRDAD
     GFLRTGTDVS VQSLERWQGM GREPLPFETS VPRIFAAGDV RRGSMKRVAA AVGEGSSAVA
     SVHRALADIR
//
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