TRXB_MYCLE
ID TRXB_MYCLE Reviewed; 458 AA.
AC P46843;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Bifunctional thioredoxin reductase/thioredoxin;
DE Includes:
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9 {ECO:0000250|UniProtKB:P9WHH1};
DE Includes:
DE RecName: Full=Thioredoxin;
GN Name=trxB/A; Synonyms=trx; OrderedLocusNames=ML2703;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8969512; DOI=10.1099/13500872-142-11-3147;
RA Fsihi H., de Rossi E., Salazar L., Cantoni R., Labo M., Riccardi G.,
RA Takiff H.E., Eiglmeier K., Bergh S., Cole S.T.;
RT "Gene arrangement and organization in an approximately 76 kb fragment
RT encompassing the oriC region of the chromosome of Mycobacterium leprae.";
RL Microbiology 142:3147-3161(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7476189; DOI=10.1111/j.1365-2958.1995.tb02318.x;
RA Wieles B., van Soolingen D., Holmgren A., Offringa R., Ottenhoff T.,
RA Thole J.;
RT "Unique gene organization of thioredoxin and thioredoxin reductase in
RT Mycobacterium leprae.";
RL Mol. Microbiol. 16:921-929(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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:0000250|UniProtKB:P9WHH1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P9WHH1};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P9WHH1};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WHH1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: In the pathogen M.leprae, thioredoxin reductase (TR) and
CC thioredoxin (Trx) are encoded by a single gene. N-terminal part of the
CC protein corresponds to TR and the C-terminal part to Trx.
CC {ECO:0000305|PubMed:7476189}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250|UniProtKB:P9WHH1}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the class-II pyridine
CC nucleotide-disulfide oxidoreductase family. {ECO:0000305}.
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DR EMBL; L39923; AAB53131.1; -; Genomic_DNA.
DR EMBL; X87899; CAA61150.1; -; Genomic_DNA.
DR EMBL; AL583926; CAC32235.1; -; Genomic_DNA.
DR PIR; S77662; S77662.
DR RefSeq; NP_302724.1; NC_002677.1.
DR RefSeq; WP_010909042.1; NC_002677.1.
DR AlphaFoldDB; P46843; -.
DR SMR; P46843; -.
DR STRING; 272631.ML2703; -.
DR EnsemblBacteria; CAC32235; CAC32235; CAC32235.
DR KEGG; mle:ML2703; -.
DR PATRIC; fig|272631.5.peg.5206; -.
DR Leproma; ML2703; -.
DR eggNOG; COG0492; Bacteria.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_031864_5_1_11; -.
DR OMA; VDNFPGY; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 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 InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 1.
DR TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; Electron transport; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Redox-active center; Reference proteome; Transport.
FT CHAIN 1..458
FT /note="Bifunctional thioredoxin reductase/thioredoxin"
FT /id="PRO_0000166758"
FT DOMAIN 341..455
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 1..321
FT /note="Thioredoxin reductase"
FT REGION 322..347
FT /note="Linker"
FT BINDING 19..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 41..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 245
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 265
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 292..295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 292
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT DISULFID 142..145
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 379..382
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 458 AA; 49046 MW; 84D367AB31899987 CRC64;
MNTTPSAHET IHEVIVIGSG PAGYTAALYA ARAQLTPLVF EGTSFGGALM TTTEVENYPG
FRNGITGPEL MDDMREQALR FGAELRTEDV ESVSLRGPIK SVVTAEGQTY QARAVILAMG
TSVRYLQIPG EQELLGRGVS ACATCDGSFF RGQDIAVIGG GDSAMEEALF LTRFARSVTL
VHRRDEFRAS KIMLGRARNN DKIKFITNHT VVAVNGYTTV TGLRLRNTTT GEETTLVVTG
VFVAIGHEPR SSLVSDVVDI DPDGYVLVKG RTTSTSMDGV FAAGDLVDRT YRQAITAAGS
GCAAAIDAER WLAEHAGSKA NETTEETGDV DSTDTTDWST AMTDAKNAGV TIEVTDASFF
ADVLSSNKPV LVDFWATWCG PCKMVAPVLE EIASEQRNQL TVAKLDVDTN PEMAREFQVV
SIPTMILFQG GQPVKRIVGA KGKAALLRDL SDVVPNLN
