[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan] 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., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.; "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."; DNA Res. 3:137-155(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[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]. 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 1-162. STRAIN=K12; PubMed=1592833 [NCBI, ExPASy, EBI, Israel, Japan] Smillie D.A., Hayward R.S., Suzuki T., Fujita N., Ishihama A.; "Locations of genes encoding alkyl hydroperoxide reductase on the physical map of the Escherichia coli K-12 genome."; J. Bacteriol. 174:3826-3827(1992).
[6]	ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-354, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan] Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.; "Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli."; Mol. Cell. Proteomics 0:0-0(2008).

Comments

FUNCTION: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the ahpC protein.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer.
INTERACTION:
P32719:alsE; NbExp=1; IntAct=EBI-907438, EBI-1128770;
P07604:tyrR; NbExp=1; IntAct=EBI-907438, EBI-559274;
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

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

U82598; AAB40807.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73707.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35236.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D13187; BAA02486.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

AP_001254.1; -.
NP_415139.2; -.

3D structure databases

PDB

1FL2; X-ray; 1.90 A; A=212-521.

[ExPASy / RCSB / EBI]

1FL2; -.

P35340; 1-521.

Protein-protein interaction databases

IntAct

P35340; -.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11385-MON; -.
MetaCyc:EG11385-MON; -.

2D gel databases

SWISS-2DPAGE

P35340; -.

Organism-specific databases

EchoBASE

EB1358; -.

EcoGene

EG11385; ahpF.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0016651;	Molecular function: oxidoreductase activity, acting on NADH or NADPH (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: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

IPR000759; Adrndx_reductase.
IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
IPR003042; Rng_hydrolase.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 2.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000238; AhpF; 1.

PRINTS

PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.
PR00420; RNGMNOXGNASE.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR03140; AhpF; 1.

PROSITE

PS51354; GLUTAREDOXIN_2; 1.
PS00573; PYRIDINE_REDOX_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P35340.

Genome annotation databases

GeneID

947540; -.

GenomeReviews

U00096_GR; b0606.
AP009048_GR; JW0599.

KEGG

ecj:JW0599; -.
eco:b0606; -.

Phylogenomic databases

HOGENOM

P35340; -.

Other

LinkHub

P35340; -.

Genome annotation databases

CMR

P35340; b0606.

Other

UniRef

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

Keywords

3D-structure; Acetylation; Complete proteome; FAD; Flavoprotein; NAD; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 521`	`521`	`Alkyl hydroperoxide reductase subunit F.`	`PRO_0000166774`
`NP_BIND`	`214 229`	`16`	`FAD (By similarity).`
`NP_BIND`	`357 371`	`15`	`NAD or NADP (By similarity).`
`NP_BIND`	`478 488`	`11`	`FAD (By similarity).`
`MOD_RES`	`53 53`		`N6-acetyllysine.`
`MOD_RES`	`354 354`		`N6-acetyllysine.`
`DISULFID`	`345 348`		`Redox-active (By similarity).`
`STRAND`	`213 218`	`6`
`HELIX`	`222 232`	`11`
`TURN`	`233 235`	`3`
`STRAND`	`238 241`	`4`
`HELIX`	`247 251`	`5`
`STRAND`	`261 265`	`5`
`HELIX`	`266 278`	`13`
`STRAND`	`282 285`	`4`
`STRAND`	`290 294`	`5`
`STRAND`	`303 307`	`5`
`STRAND`	`312 320`	`9`
`STRAND`	`324 326`	`3`
`TURN`	`332 337`	`6`
`TURN`	`339 341`	`3`
`STRAND`	`342 344`	`3`
`HELIX`	`346 349`	`4`
`HELIX`	`350 353`	`4`
`STRAND`	`357 361`	`5`
`HELIX`	`365 375`	`11`
`STRAND`	`378 384`	`7`
`STRAND`	`386 389`	`4`
`HELIX`	`394 401`	`8`
`STRAND`	`406 431`	`26`
`TURN`	`432 434`	`3`
`STRAND`	`437 441`	`5`
`STRAND`	`443 447`	`5`
`STRAND`	`451 454`	`4`
`HELIX`	`456 458`	`3`
`TURN`	`459 461`	`3`
`STRAND`	`483 485`	`3`
`HELIX`	`497 517`	`21`

Sequence information

Length: 521 AA [This is the length of the unprocessed precursor]

Molecular weight: 56177 Da [This is the MW of the unprocessed precursor]

CRC64: F39C50F922395B48 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLDTNMKTQL KAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV TFKEDNSLPV 

        70         80         90        100        110        120 
RKPSFLITNP GSNQGPRFAG SPLGHEFTSL VLALLWTGGH PSKEAQSLLE QIRHIDGDFE 

       130        140        150        160        170        180 
FETYYSLSCH NCPDVVQALN LMSVLNPRIK HTAIDGGTFQ NEITDRNVMG VPAVFVNGKE 

       190        200        210        220        230        240 
FGQGRMTLTE IVAKIDTGAE KRAAEELNKR DAYDVLIVGS GPAGAAAAIY SARKGIRTGL 

       250        260        270        280        290        300 
MGERFGGQIL DTVDIENYIS VPKTEGQKLA GALKVHVDEY DVDVIDSQSA SKLIPAAVEG 

       310        320        330        340        350        360 
GLHQIETASG AVLKARSIIV ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG PLFKGKRVAV 

       370        380        390        400        410        420 
IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKL RSLKNVDIIL NAQTTEVKGD 

       430        440        450        460        470        480 
GSKVVGLEYR DRVSGDIHNI ELAGIFVQIG LLPNTNWLEG AVERNRMGEI IIDAKCETNV 

       490        500        510        520 
KGVFAAGDCT TVPYKQIIIA TGEGAKASLS AFDYLIRTKT A

P35340 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