Bifunctional thioredoxin reductase/thioredoxin

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Reviewed, UniProtKB/Swiss-Prot P46843 (TRXB_MYCLE)

Last modified November 3, 2009. Version 83. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Bifunctional thioredoxin reductase/thioredoxin
Including the following 2 domains:
    1- Recommended name:
            Thioredoxin reductase
                Short name=TRXR
              EC=1.8.1.9
    2- Recommended name:
            Thioredoxin

Gene names

Name:	trxB/A
Synonyms:	trx
Ordered Locus Names:	ML2703

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

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Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

Catalytic activity	Thioredoxin + NADP⁺ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	In the N-terminal section; belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. Contains 1 thioredoxin domain.

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Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro removal of superoxide radicals Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 458

458

Bifunctional thioredoxin reductase/thioredoxin

PRO_0000166758

Regions

Domain

341 – 455

115

Thioredoxin

Nucleotide binding

41 – 48

FAD By similarity

Nucleotide binding

285 – 294

FAD By similarity

Region

1 – 321

321

Thioredoxin reductase

Region

322 – 347

Linker

Amino acid modifications

Disulfide bond

142 ↔ 145

Redox-active By similarity

Disulfide bond

379 ↔ 382

Redox-active By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P46843-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 84D367AB31899987
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FASTA

458

49,046

        10         20         30         40         50         60 
MNTTPSAHET IHEVIVIGSG PAGYTAALYA ARAQLTPLVF EGTSFGGALM TTTEVENYPG 

        70         80         90        100        110        120 
FRNGITGPEL MDDMREQALR FGAELRTEDV ESVSLRGPIK SVVTAEGQTY QARAVILAMG 

       130        140        150        160        170        180 
TSVRYLQIPG EQELLGRGVS ACATCDGSFF RGQDIAVIGG GDSAMEEALF LTRFARSVTL 

       190        200        210        220        230        240 
VHRRDEFRAS KIMLGRARNN DKIKFITNHT VVAVNGYTTV TGLRLRNTTT GEETTLVVTG 

       250        260        270        280        290        300 
VFVAIGHEPR SSLVSDVVDI DPDGYVLVKG RTTSTSMDGV FAAGDLVDRT YRQAITAAGS 

       310        320        330        340        350        360 
GCAAAIDAER WLAEHAGSKA NETTEETGDV DSTDTTDWST AMTDAKNAGV TIEVTDASFF 

       370        380        390        400        410        420 
ADVLSSNKPV LVDFWATWCG PCKMVAPVLE EIASEQRNQL TVAKLDVDTN PEMAREFQVV 

       430        440        450 
SIPTMILFQG GQPVKRIVGA KGKAALLRDL SDVVPNLN

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene arrangement and organization in an approximately 76 kb fragment encompassing the oriC region of the chromosome of Mycobacterium leprae." Fsihi H., de Rossi E., Salazar L., Cantoni R., Labo M., Riccardi G., Takiff H.E., Eiglmeier K., Bergh S., Cole S.T. Microbiology 142:3147-3161(1996) [PubMed: 8969512] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Unique gene organization of thioredoxin and thioredoxin reductase in Mycobacterium leprae." Wieles B., van Soolingen D., Holmgren A., Offringa R., Ottenhoff T., Thole J. Mol. Microbiol. 16:921-929(1995) [PubMed: 7476189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

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Cross-references

Sequence databases
	L39923 Genomic DNA. Translation: AAB53131.1. X87899 Genomic DNA. Translation: CAA61150.1. AL583926 Genomic DNA. Translation: CAC32235.1.
PIR	S77662.
RefSeq	NP_302724.1.
3D structure databases
HSSP	HSSP built from PDB template 1QUW based on UniProtKB P80579.
SMR	P46843. Positions 7-318, 351-456.
ModBase	Search...
Genome annotation databases
GeneID	910819.
GenomeReviews	Gene locus ML2703 in contig AL450380_GR.
KEGG	mle:ML2703.
NMPDR	fig\|272631.1.peg.1596.
Organism-specific databases
Leproma	ML2703.
CMR	Search...
Phylogenomic databases
HOGENOM	P46843.
OMA	HYIANSI.
Enzyme and pathway databases
BioCyc	MLEP272631:ML2703-MON.
BRENDA	1.8.1.9. 808.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR016040. NAD(P)-bd_dom. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR000103. Pyridine_nuc-diS_OxRdtase_2. IPR005982. Thioredox_Rdtase. IPR005746. Thioredoxin. IPR017936. Thioredoxin-like. IPR015467. Thioredoxin_core. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR10438. Trx. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00469. PNDRDTASEII.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01068. thioredoxin. 1 hit. TIGR01292. TRX_reduct. 1 hit.
PROSITE	PS00573. PYRIDINE_REDOX_2. 1 hit. PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

TRXB_MYCLE

Accession

Primary (citable) accession number: P46843

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents