Thioredoxin reductase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P0A9P4 (TRXB_ECOLI)

Last modified June 16, 2009. Version 45. History...

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

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

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

Hide | Top

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

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.

Hide | Top

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.

Hide | Top

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
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW removal of superoxide radicals Inferred from electronic annotation. Source: InterPro
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 binding Inferred from physical interaction. Source: IntAct thioredoxin-disulfide reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Binary interactions

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

Hide | Top

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.9

Secondary structure

321

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9P4-1 [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

Hide | Top

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: 3288628] [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: 8905232] [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: 9278503] [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: 16738553] [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: 8380150] [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: 7934832] [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: 1575737] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.
[8]	"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: 2067578] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[9]	"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: 8114095] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BOND.
[10]	"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: 10595539] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[11]	"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: 10947986] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXA.

Hide | Top

Cross-references

Sequence databases

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

AP_001518.1.
NP_415408.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A9P4. 5 interactions.

2-D gel databases

SWISS-2DPAGE

P0A9P4.

ECO2DBASE

D031.5. 6TH EDITION.

Genome annotation databases

GeneID

949054.

GenomeReviews

Gene locus JW0871 in contig AP009048_GR.
Gene locus b0888 in contig U00096_GR.

KEGG

ecj:JW0871.
eco:b0888.

Organism-specific databases

EchoBASE

EB1025.

EcoGene

EG11032. trxB.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9P4.

OMA

P0A9P4. PSCGPCH.

Enzyme and pathway databases

BioCyc

EcoCyc:THIOREDOXIN-REDUCT-NADPH-MON.
MetaCyc:THIOREDOXIN-REDUCT-NADPH-MON.

Family and domain databases

InterPro

IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
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.

ProDom

PD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01292. TRX_reduct. 1 hit.

PROSITE

PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Hide | Top

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:	June 16, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

Hide | Top

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 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

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents