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
//