Thioredoxin reductase - Escherichia coli (strain K12)

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P0A9P4 (TRXB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Thioredoxin reductase
Short name=TRXR
EC=1.8.1.9

Gene names

Name:	trxB
Ordered Locus Names:	b0888, JW0871

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP⁺ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	removal of superoxide radicals Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	flavin adenine dinucleotide binding Inferred from direct assay PubMed 2644268. Source: EcoCyc thioredoxin-disulfide reductase activity Inferred from direct assay PubMed 2644268. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-1029826,EBI-548960

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.7

Chain

2 – 321

320

Thioredoxin reductase

PRO_0000166729

Regions

Nucleotide binding

36 – 43

FAD

Nucleotide binding

287 – 296

FAD

Amino acid modifications

Disulfide bond

136 ↔ 139

Redox-active Ref.10

Secondary structure

321

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9P4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8E5AF86FB195CC82
Show »

FASTA

321

34,623

        10         20         30         40         50         60 
MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL 

        70         80         90        100        110        120 
TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL 

       130        140        150        160        170        180 
GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG 

       190        200        210        220        230        240 
FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL 

       250        260        270        280        290        300 
FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA 

       310        320 
GTGCMAALDA ERYLDGLADA K

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases." Russel M., Model P. J. Biol. Chem. 263:9015-9019(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Molecular characterization of the Escherichia coli htrD gene: cloning, sequence, regulation, and involvement with cytochrome d oxidase." Delaney J.M., Wall D., Georgopoulos C. J. Bacteriol. 175:166-175(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-321. Strain: K12.
[6]	"Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter." Poole R.K., Hatch L., Cleeter M.W.J., Gibson F., Cox G.B., Wu G. Mol. Microbiol. 10:421-430(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-321.
[7]	"Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit." Ueshima R., Fujita N., Ishihama A. Biochem. Biophys. Res. Commun. 184:634-639(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.
[8]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[9]	"Convergent evolution of similar function in two structurally divergent enzymes." Kuriyan J., Krishna T.S.R., Wong L., Guenther B., Pahler A., Williams C.H. Jr., Model P. Nature 352:172-174(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[10]	"Crystal structure of Escherichia coli thioredoxin reductase refined at 2-A resolution. Implications for a large conformational change during catalysis." Waksman G., Krishna T.S.R., Williams C.H. Jr., Kuriyan J. J. Mol. Biol. 236:800-816(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BOND.
[11]	"Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor." Lennon B.W., Williams C.H. Jr., Ludwig M.L. Protein Sci. 8:2366-2379(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[12]	"Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase." Lennon B.W., Williams C.H. Jr., Ludwig M.L. Science 289:1190-1194(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03762 Genomic DNA. Translation: AAA24697.1.
U00096 Genomic DNA. Translation: AAC73974.1.
AP009048 Genomic DNA. Translation: BAA35613.1.
L21749 Genomic DNA. Translation: AAA66170.1.
M95935 Genomic DNA. No translation available.

PIR

RDECT. A28074.

RefSeq

NP_415408.1. NC_000913.2.
YP_489160.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CL0	X-ray	2.50	A	2-321	[»]
1F6M	X-ray	2.95	A/B/E/F	2-321	[»]
1TDE	X-ray	2.10	A	2-317	[»]
1TDF	X-ray	2.30	A	2-317	[»]
1TRB	X-ray	2.00	A	2-321	[»]

ProteinModelPortal

P0A9P4.

SMR

P0A9P4. Positions 2-316.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A9P4. 5 interactions.

STRING

511145.b0888.

2D gel databases

SWISS-2DPAGE

P0A9P4.

Proteomic databases

PaxDb

P0A9P4.

PRIDE

P0A9P4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73974; AAC73974; b0888.
BAA35613; BAA35613; BAA35613.

GeneID

12932721.
949054.

KEGG

ecj:Y75_p0860.
eco:b0888.

PATRIC

32116985. VBIEscCol129921_0917.

Organism-specific databases

EchoBASE

EB1025.

EcoGene

EG11032. trxB.

Phylogenomic databases

eggNOG

COG0492.

HOGENOM

HOG000072912.

K00384.

OMA

VMGAFIA.

ProtClustDB

PRK10262.

Enzyme and pathway databases

BioCyc

EcoCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.
ECOL316407:JW0871-MONOMER.
MetaCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.

SABIO-RK

P0A9P4.

Gene expression databases

Genevestigator

P0A9P4.

Family and domain databases

InterPro

IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.
PR00469. PNDRDTASEII.

TIGRFAMs

TIGR01292. TRX_reduct. 1 hit.

PROSITE

PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A9P4.

Entry information

Entry name

TRXB_ECOLI

Accession

Primary (citable) accession number: P0A9P4
Secondary accession number(s): P09625

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents