ID TRXB_CHLTR Reviewed; 312 AA.
AC O84101;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9;
GN Name=trxB; OrderedLocusNames=CT_099;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P0A9P4};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67690.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE001273; AAC67690.1; ALT_INIT; Genomic_DNA.
DR PIR; B71556; B71556.
DR RefSeq; NP_219602.1; NC_000117.1.
DR RefSeq; WP_009871447.1; NC_000117.1.
DR AlphaFoldDB; O84101; -.
DR SMR; O84101; -.
DR STRING; 272561.CT_099; -.
DR EnsemblBacteria; AAC67690; AAC67690; CT_099.
DR GeneID; 884181; -.
DR KEGG; ctr:CT_099; -.
DR PATRIC; fig|272561.5.peg.109; -.
DR HOGENOM; CLU_031864_5_1_0; -.
DR InParanoid; O84101; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
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 Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..312
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166726"
FT BINDING 33..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT BINDING 283..292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT DISULFID 138..141
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ SEQUENCE 312 AA; 33508 MW; 729D0D22F8FA0A39 CRC64;
MTHAKLVIIG SGPAGYTAAI YASRALLTPV LFEGFFSGIA GGQLMTTTEV ENFPGFPEGV
LGHQLMDLMK TQAQRFGTQV LSKDITAVDF SVRPFVLKSG KETFTCDACI IATGASAKRL
SIPGAGDNEF WQKGVTACAV CDGASPIFRD KDLFVVGGGD SALEEAMFLT RYGKRVFVVH
RRDTLRASKV MVNKAQANEK IFFLWNSEIV KISGDTLVRS IDIYNNVDET TTTMEAAGVF
FAIGHQPNTA FLGGQVALDE NGYIITEKGS SRTSVPGVFA AGDVQDKYYR QAITSAGSGC
MAALDAERFL EN
//
