ID N8REP3_9GAMM Unreviewed; 155 AA.
AC N8REP3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:ENU33893.1};
GN ORFNames=F989_00865 {ECO:0000313|EMBL:ENU33893.1};
OS Acinetobacter parvus NIPH 1103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217671 {ECO:0000313|EMBL:ENU33893.1, ECO:0000313|Proteomes:UP000018426};
RN [1] {ECO:0000313|EMBL:ENU33893.1, ECO:0000313|Proteomes:UP000018426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 1103 {ECO:0000313|EMBL:ENU33893.1,
RC ECO:0000313|Proteomes:UP000018426};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter parvus NIPH 1103.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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:ENU33893.1}.
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DR EMBL; APOL01000019; ENU33893.1; -; Genomic_DNA.
DR AlphaFoldDB; N8REP3; -.
DR PATRIC; fig|1217671.3.peg.848; -.
DR HOGENOM; CLU_031864_5_6_6; -.
DR Proteomes; UP000018426; Unassembled WGS sequence.
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:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 7..150
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 155 AA; 16611 MW; 68344C96AC8D4A83 CRC64;
MQNQHSRLII LGSGPAGYSA AVYAARANLK PTLIAGLQLG GQLTTTTEVD NWVGDAEGLT
GPILMERMQA HAECFGTEMV YDHINEVDLK TRPFVLKGDM GEYTCDALII ATGATAQYLG
LESEAAFIGQ GVSACATCDG FFYKNQGSRL TYLFC
//
