Reviewed, UniProtKB/Swiss-Prot P35340 (AHPF_ECOLI)

Names and origin

Protein names

Recommended name:
    Alkyl hydroperoxide reductase subunit F
    EC=1.8.1.-
Alternative name(s):
    Alkyl hydroperoxide reductase F52A protein

Gene names

Name:	ahpF
Ordered Locus Names:	b0606, JW0599

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (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 structure	Homodimer.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on NADH or NADPH Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
alsE	P32719	1	EBI-907438,EBI-1128770
tyrR	P07604	1	EBI-907438,EBI-559274

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 521

521

Alkyl hydroperoxide reductase subunit F

PRO_0000166774

Regions

Nucleotide binding

214 – 229

16

FAD By similarity

Nucleotide binding

357 – 371

15

NAD or NADP By similarity

Nucleotide binding

478 – 488

11

FAD By similarity

Amino acid modifications

Modified residue

53

1

N6-acetyllysine Ref.6

Modified residue

354

1

N6-acetyllysine Ref.6

Disulfide bond

345 ↔ 348

Redox-active By similarity

Secondary structure

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521

Helix Strand Turn

Details...

Beta strand

213 – 218

6

Helix

222 – 232

11

Turn

233 – 235

3

Beta strand

238 – 241

4

Helix

247 – 251

5

Beta strand

261 – 265

5

Helix

266 – 278

13

Beta strand

282 – 285

4

Beta strand

290 – 294

5

Beta strand

303 – 307

5

Beta strand

312 – 320

9

Beta strand

324 – 326

3

Turn

332 – 337

6

Turn

339 – 341

3

Beta strand

342 – 344

3

Helix

346 – 349

4

Helix

350 – 353

4

Beta strand

357 – 361

5

Helix

365 – 375

11

Beta strand

378 – 384

7

Beta strand

386 – 389

4

Helix

394 – 401

8

Beta strand

406 – 431

26

Turn

432 – 434

3

Beta strand

437 – 441

5

Beta strand

443 – 447

5

Beta strand

451 – 454

4

Helix

456 – 458

3

Turn

459 – 461

3

Beta strand

483 – 485

3

Helix

497 – 517

21

Sequences

	Sequence		Length	Mass (Da)
	P35340-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: F39C50F922395B48	FASTA	521	56,177
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , 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. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Sequence of minutes 4-25 of Escherichia coli." 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. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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]	"Locations of genes encoding alkyl hydroperoxide reductase on the physical map of the Escherichia coli K-12 genome." Smillie D.A., Hayward R.S., Suzuki T., Fujita N., Ishihama A. J. Bacteriol. 174:3826-3827(1992) [PubMed: 1592833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-162. Strain: K12.
[6]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-354, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U82598 Genomic DNA. Translation: AAB40807.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73707.1. Different initiation.
AP009048 Genomic DNA. Translation: BAA35236.1.
D13187 Genomic DNA. Translation: BAA02486.1.

RefSeq

AP_001254.1.
NP_415139.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FL2	X-ray	1.90	A	212-521	[»]

SMR

P35340. Positions 1-521.

ModBase

Search...

Protein-protein interaction databases

IntAct

P35340. 21 interactions.

STRING

P35340.

2-D gel databases

SWISS-2DPAGE

P35340.

Genome annotation databases

GeneID

947540.

GenomeReviews

Gene locus JW0599 in contig AP009048_GR.
Gene locus b0606 in contig U00096_GR.

KEGG

ecj:JW0599.
eco:b0606.

Organism-specific databases

EchoBASE

EB1358.

EcoGene

EG11385. ahpF.

CMR

Search...

Phylogenomic databases

eggNOG

COG3634.

HOGENOM

HBG289531.

OMA

VPLGHEF.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11385-MONOMER.
ECOL168927:B0606-MONOMER.
MetaCyc:EG11385-MONOMER.

Gene expression databases

Genevestigator

P35340.

Family and domain databases

InterPro

IPR012081. Alkyl_hydroperoxide_Rdtase_suF.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR002109. Glutaredoxin.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR012336. Thioredoxin-like_fold.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.

Pfam

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

PIRSF

PIRSF000238. AhpF. 1 hit.

PRINTS

PR00368. FADPNR.
PR00469. PNDRDTASEII.

TIGRFAMs

TIGR03140. AhpF. 1 hit.

PROSITE

PS51354. GLUTAREDOXIN_2. 1 hit.
PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AHPF_ECOLI

Accession

Primary (citable) accession number: P35340
Secondary accession number(s): P77251, P77462

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 94 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)