ID D8JES3_ACISD Unreviewed; 315 AA.
AC D8JES3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN OrderedLocusNames=AOLE_15340 {ECO:0000313|EMBL:ADI91955.1};
OS Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=436717 {ECO:0000313|EMBL:ADI91955.1, ECO:0000313|Proteomes:UP000000392};
RN [1] {ECO:0000313|EMBL:ADI91955.1, ECO:0000313|Proteomes:UP000000392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16667 / KCTC 23045 / DR1
RC {ECO:0000313|Proteomes:UP000000392};
RX PubMed=20639327; DOI=10.1128/JB.00722-10;
RA Jung J., Baek J.H., Park W.;
RT "Complete genome sequence of the diesel-degrading Acinetobacter sp. strain
RT DR1.";
RL J. Bacteriol. 192:4794-4795(2010).
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|RuleBase:RU003880};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003881};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003880}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333,
CC ECO:0000256|RuleBase:RU003880}.
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DR EMBL; CP002080; ADI91955.1; -; Genomic_DNA.
DR RefSeq; WP_013198771.1; NC_014259.1.
DR AlphaFoldDB; D8JES3; -.
DR GeneID; 9383493; -.
DR KEGG; acd:AOLE_15340; -.
DR PATRIC; fig|436717.3.peg.3040; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_1_6; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000000392; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:UniProtKB-UniRule.
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 InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR NCBIfam; TIGR01292; TRX_reduct; 1.
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.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|RuleBase:RU003880};
KW Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW NADP {ECO:0000256|RuleBase:RU003881};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003880};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003880}.
FT DOMAIN 7..300
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 315 AA; 33747 MW; A237F7C29228291B CRC64;
MSARHSRLII LGSGPAGYSA AVYAARANLK PTLIAGLQLG GQLTTTTEVD NWPGDPEGLT
GPALMDRMQA HAERFGTELV YDHINEVDLN VRPFVLKGDM EEYTCDALII ATGATAQYLG
LESEQNFMGQ GVSACATCDG FFYKNQKVMV VGGGNTAVEE ALYLSNIASH VTLVHRRDSL
RSEKILQDHL FAKEKEGKIS IIWNHEVEEV LGDNTGVTSV RLKSTQDESK QDVEVHGLFV
AIGHKPNTGM FDGQLNLRDG YIQVQSGTSG NATATSVAGV FAAGDVADSI YRQAITSAGS
GCMAALDAEK YLDNL
//
