ID A0A395LMJ6_9SPHN Unreviewed; 327 AA.
AC A0A395LMJ6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|ARBA:ARBA00018719, ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN Name=trxB {ECO:0000313|EMBL:RDS78263.1};
GN ORFNames=DL238_12035 {ECO:0000313|EMBL:RDS78263.1};
OS Alteriqipengyuania lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Alteriqipengyuania.
OX NCBI_TaxID=1538146 {ECO:0000313|EMBL:RDS78263.1, ECO:0000313|Proteomes:UP000254101};
RN [1] {ECO:0000313|EMBL:RDS78263.1, ECO:0000313|Proteomes:UP000254101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-5 {ECO:0000313|EMBL:RDS78263.1,
RC ECO:0000313|Proteomes:UP000254101};
RA Chen X., Liu J.;
RT "Erythrobacter nanhaiensis sp. nov., a novel member of the genus
RT Erythrobacter isolated from the South China Sea.";
RL Submitted (JUL-2018) 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|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}.
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:RDS78263.1}.
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DR EMBL; QRBB01000001; RDS78263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395LMJ6; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000254101; Unassembled WGS sequence.
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..298
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 327 AA; 34985 MW; 8E8DD1D34782D4EE CRC64;
MATHRTKMLI IGSGPAGYSA AIYGARAMLE PVMVQGLQPG GQLTITTDVE NYPGFADVIQ
GPWLMEQMRA QAEHVGTKMH WDTIVEIDLK NGSPFRAVGD SGDEYIGDTV VIATGASAKW
LGVPGEQELG GKGVSACATC DGFFYRGKKV AVIGGGNTAV EEALYLTNHS DDVTLIHRRD
ELRSEKILQD RLFKSDKITP MWNKTVERFE AGDNGALHHL VLKDTVTGEE STMEVDGAFV
AIGHAPATEL FTGQLPTDDG GYLIVEPGTP RTEIPGVFAC GDVMDHTYRQ AVTAAGTGCM
AALDAERFLS GLEIELDGHV EEAEAAE
//
