[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. STRAIN=K12 / TG1; DOI=10.1074/jbc.272.49.30841; PubMed=9388228 [NCBI, ExPASy, EBI, Israel, Japan] Miranda-Vizuete A., Damdimopoulos A.E., Gustafsson J.-A., Spyrou G.; "Cloning, expression, and characterization of a novel Escherichia coli thioredoxin."; J. Biol. Chem. 272:30841-30847(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/4.2.91; PubMed=9205837 [NCBI, ExPASy, EBI, Israel, Japan] Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.; "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."; DNA Res. 4:91-113(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-104. STRAIN=K12; Nashimoto H.; "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia coli."; (In) Nierhaus K.H. (eds.); The translational apparatus, pp.185-195, Plenum Press, New York (1993).
[6]	IDENTIFICATION. Rudd K.E.; Unpublished observations (NOV-1993).

Comments

FUNCTION: Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin.
CATALYTIC ACTIVITY: Protein dithiol + NAD(P)⁺ = protein disulfide + NAD(P)H.
INTERACTION:
P14900:murD; NbExp=1; IntAct=EBI-549392, EBI-554780;
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the thioredoxin family.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U85942; AAB88587.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75635.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16469.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D13169; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

E65036; E65036.

RefSeq

AP_003168.1; -.
NP_417077.1; -.

3D structure databases

HSSP

P23400; 1DBY. [HSSP ENTRY / PDB]

ModBase

P0AGG4.

Protein-protein interaction databases

IntAct

P0AGG4; 23.

Enzyme and pathway databases

BioCyc

EcoCyc:RED-THIOREDOXIN2-MON; -.

Organism-specific databases

EchoBASE

EB1833; -.

EcoGene

EG11887; trxC.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0015035;	Molecular function: protein disulfide oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0047134;	Molecular function: protein-disulfide reductase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006662;	Biological process: glycerol ether metabolic process (inferred from electronic annotation from InterPro).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005746; Thioredoxin.
IPR006662; Thioredoxin-like.
IPR013766; Thioredoxin_dom.
IPR012335; Thioredoxin_fold.
IPR015467; Trx.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

PANTHER

PTHR10438; Trx; 1.

Pfam

PF00085; Thioredoxin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00421; THIOREDOXIN.

TIGRFAMs

TIGR01068; thioredoxin; 1.

PROSITE

PS00194; THIOREDOXIN_1; 1.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

947062; -.

GenomeReviews

AP009048_GR; JW2566.
U00096_GR; b2582.

KEGG

ecj:JW2566; -.
eco:b2582; -.

Phylogenomic databases

HOGENOM

P0AGG4; -.

Genome annotation databases

CMR

P0AGG4; b2582.

Other

ProtoNet

P0AGG4.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Electron transport; Metal-binding; NAD; Oxidoreductase; Redox-active center; Transport; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 139`	`139`	`Thioredoxin-2.`	`PRO_0000120102`
`DOMAIN`	`26 139`	`114`	`Thioredoxin.`
`ZN_FING`	`5 18`	`14`	`Potential.`
`DISULFID`	`64 67`		`Redox-active (By similarity).`

Sequence information

Length: 139 AA [This is the length of the unprocessed precursor]

Molecular weight: 15555 Da [This is the MW of the unprocessed precursor]

CRC64: 4C973F6FE55C8856 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNTVCTHCQA INRIPDDRIE DAAKCGRCGH DLFDGEVINA TGETLDKLLK DDLPVVIDFW 

        70         80         90        100        110        120 
APWCGPCRNF APIFEDVAQE RSGKVRFVKV NTEAERELSS RFGIRSIPTI MIFKNGQVVD 

       130 
MLNGAVPKAP FDSWLNESL

P0AGG4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools