ID A0A109QWJ5_9MICO Unreviewed; 305 AA.
AC A0A109QWJ5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AMB58142.1};
GN ORFNames=AWU67_03895 {ECO:0000313|EMBL:AMB58142.1};
OS Microterricola viridarii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microterricola.
OX NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB58142.1, ECO:0000313|Proteomes:UP000058305};
RN [1] {ECO:0000313|EMBL:AMB58142.1, ECO:0000313|Proteomes:UP000058305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB58142.1,
RC ECO:0000313|Proteomes:UP000058305};
RX PubMed=26854947; DOI=10.1016/j.jbiotec.2016.02.011;
RA Himanshu, Swarnkar M.K., Singh D., Kumar R.;
RT "First complete genome sequence of a species in the genus Microterricola,
RT an extremophilic cold active enzyme producing bacterial strain ERGS5:02
RT isolated from Sikkim Himalaya.";
RL J. Biotechnol. 222:17-18(2016).
RN [2] {ECO:0000313|Proteomes:UP000058305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS5:02 {ECO:0000313|Proteomes:UP000058305};
RA Kumar R., Singh D., Swarnkar M.K.;
RT "First complete genome sequence of a species in the genus Microterricola,
RT an extremophilic cold active enzyme producing strain ERGS5:02 isolated from
RT Sikkim Himalaya.";
RL Submitted (JAN-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};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP014145; AMB58142.1; -; Genomic_DNA.
DR RefSeq; WP_067226837.1; NZ_CP014145.1.
DR AlphaFoldDB; A0A109QWJ5; -.
DR KEGG; mvd:AWU67_03895; -.
DR OrthoDB; 9786503at2; -.
DR Proteomes; UP000058305; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR PANTHER; PTHR48105:SF28; THIOREDOXIN REDUCTASE GLIT (AFU_ORTHOLOGUE AFUA_6G09740); 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000058305}.
FT DOMAIN 4..289
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 305 AA; 32015 MW; 46024C21A3EED53E CRC64;
MSDFDVAVIG AGPAGLSAAL GLVRSRRTVL LIDSNRPRNA ATLRSHGFLT RDGVPPLELR
KLGREEFEGY PGATFHAGLV QGVQATPDGF RLSARGIRGA SDLEATVGNI VVATGLIEKL
PSVPSLRAWY GTDLHSCVEC DGYEKRDAAL ALIGESDDLA ERALLISQWS SDLIVFTNGV
PAVTEAEQSA LARRGVRIER RPIADVVGER GRMTGVLLAD GETIPREAGF VRPEWTPAIA
YLDGLGVRLD DSGLIAVDAL GRTSVPGIYA AGDSTAPGPE QLIIAAGHGA QVAAALNRDL
LGPLL
//
