ID A1TB57_MYCVP Unreviewed; 304 AA.
AC A1TB57;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ABM14407.1};
GN OrderedLocusNames=Mvan_3616 {ECO:0000313|EMBL:ABM14407.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM14407.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM14407.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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; CP000511; ABM14407.1; -; Genomic_DNA.
DR RefSeq; WP_011780808.1; NZ_JACKSD010000298.1.
DR AlphaFoldDB; A1TB57; -.
DR STRING; 350058.Mvan_3616; -.
DR KEGG; mva:Mvan_3616; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_0_11; -.
DR Proteomes; UP000009159; 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:UP000009159}.
FT DOMAIN 6..289
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 304 AA; 30998 MW; BB2433C21EBFFBB6 CRC64;
MDKLWDCVII GGGAAGLSAA LVLGRARRRT LVVDAGAQSN LAATGIGGLL GFDGVPPGQL
YAQGRSQLAA YPSVEVRDGE VVTGAASDGG FTLELADGGV VQARRVLLAM GMRYEAPSLP
GLAELWGRSV FHCPFCHGWE VRDRPLAVLA NGERATHMAT LLRGWSDDVV LLTGGPAELT
DTDRSRLADA GAAVDERAVS HLVSAGGELA AVVFADGTSL GRRGLLVAVT LHQRSALAAK
LGVSFAAPGP VSVEAIEIDA THRTSVPGVF AAGDACVQMP QVAAAIAAGS AAAASIVASF
QEER
//
