[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan] Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; "50 million years of genomic stasis in endosymbiotic bacteria."; Science 296:2376-2379(2002).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-158. DOI=10.1007/s002849900392; PubMed=9767718 [NCBI, ExPASy, EBI, Israel, Japan] Clark M.A., Baumann L., Baumann P.; "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes of histidine biosynthesis."; Curr. Microbiol. 37:356-358(1998).

Comments

CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
SIMILARITY: Belongs to the ahpC/TSA 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

AE013218; AAM67659.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067228; AAC97351.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660448.1; -.

3D structure databases

HSSP

P32119; 1QMV. [HSSP ENTRY / PDB]

ModBase

Q9ZHF0.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG089-MON; -.

Ontologies

GO:0051920;	Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.

PROSITE

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

ProtoNet

Q9ZHF0.

Genome annotation databases

GeneID

1005906; -.

GenomeReviews

AE013218_GR; BUsg_089.

KEGG

bas:BUsg089; -.

Phylogenomic databases

HOGENOM

Q9ZHF0; -.

Genome annotation databases

CMR

Q9ZHF0; BUsg_089.

Other

UniRef

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

Keywords

Complete proteome; Oxidoreductase; Peroxidase; Redox-active center.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 158`	`158`	`Putative peroxiredoxin bcp.`	`PRO_0000135133`
`DOMAIN`	`4 157`	`154`	`Thioredoxin.`
`ACT_SITE`	`46 46`		`By similarity.`

Sequence information

Length: 158 AA [This is the length of the unprocessed precursor]

Molecular weight: 18138 Da [This is the MW of the unprocessed precursor]

CRC64: 7D06D4025FF297B5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTLKPGDIA PKFILPNCID KSIKLSDFLG KKVLVYFYPK AMTPGCTVQA CNIRDNLELF 

        70         80         90        100        110        120 
KSKKVEVLGI SPDNTNKLLT FVEKKMLNFT LLSDKQNIVS KKFGVWGEKI FMGKKYFGIY 

       130        140        150 
RTSFLINSSG FIDKIFFKFK CKDHHKIILT YLNSKKSD

Q9ZHF0 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