Reviewed, UniProtKB/Swiss-Prot P19480 (AHPF_SALTY)

Names and origin

Protein names

Recommended name:
    Alkyl hydroperoxide reductase subunit F
    EC=1.6.4.-
Alternative name(s):
    Alkyl hydroperoxide reductase F52A protein

Gene names

Name:	ahpF
Ordered Locus Names:	STM0609

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Contains 1 glutaredoxin domain.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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_0000166777

Regions

Domain

109 – 208

100

Glutaredoxin

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

Disulfide bond

345 ↔ 348

Redox-active By similarity

Experimental info

Sequence conflict

9

1

Q → N AA sequence Ref.3

Sequence conflict

15

1

E → DR AA sequence Ref.3

Secondary structure

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521

Helix Strand Turn

Details...

Helix

4 – 14

11

Beta strand

21 – 26

6

Helix

31 – 44

14

Beta strand

50 – 54

5

Beta strand

58 – 60

3

Beta strand

62 – 68

7

Beta strand

77 – 80

4

Helix

84 – 86

3

Helix

87 – 97

11

Helix

106 – 114

9

Beta strand

119 – 125

7

Helix

132 – 145

14

Beta strand

149 – 155

7

Turn

156 – 158

3

Helix

160 – 165

6

Beta strand

170 – 176

7

Beta strand

179 – 184

6

Helix

188 – 195

8

Helix

202 – 208

7

Beta strand

213 – 218

6

Helix

222 – 233

12

Beta strand

238 – 241

4

Helix

247 – 249

3

Beta strand

261 – 264

4

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 – 341

10

Helix

350 – 353

4

Beta strand

356 – 361

6

Helix

365 – 377

13

Beta strand

378 – 384

7

Beta strand

386 – 389

4

Helix

394 – 400

7

Beta strand

406 – 409

4

Beta strand

411 – 419

9

Beta strand

421 – 431

11

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 – 518

22

Sequences

	Sequence		Length	Mass (Da)
	P19480-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 813DEA1398DAE26F	FASTA	521	55,950
	10 20 30 40 50 60 MLDTNMKTQL RAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV TFKEDNTLPV 70 80 90 100 110 120 RKPSFLITNP GSQQGPRFAG SPLGHEFTSL VLALLWTGGH PSKEAQSLLE QIRDIDGDFE 130 140 150 160 170 180 FETYYSLSCH NCPDVVQALN LMAVLNPRIK HTAIDGGTFQ NEITERNVMG VPAVFVNGKE 190 200 210 220 230 240 FGQGRMTLTE IVAKVDTGAE KRAAEALNKR DAYDVLIVGS GPAGAAAAVY SARKGIRTGL 250 260 270 280 290 300 MGERFGGQVL DTVDIENYIS VPKTEGQKLA GALKAHVSDY DVDVIDSQSA SKLVPAATEG 310 320 330 340 350 360 GLHQIETASG AVLKARSIII ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG PLFKGKRVAV 370 380 390 400 410 420 IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKV RSLKNVDIIL NAQTTEVKGD 430 440 450 460 470 480 GSKVVGLEYR DRVSGDIHSV ALAGIFVQIG LLPNTHWLEG ALERNRMGEI IIDAKCETSV 490 500 510 520 KGVFAAGDCT TVPYKQIIIA TGEGAKASLS AFDYLIRTKI A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases." Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N. J. Biol. Chem. 265:10535-10540(1990) [PubMed: 2191951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties." Jacobson F.S., Morgan R.W., Christman M.F., Ames B.N. J. Biol. Chem. 264:1488-1496(1989) [PubMed: 2643600] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-25. Strain: oxyR1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J05478 Unassigned DNA. Translation: AAA16432.1.
AE008724 Genomic DNA. Translation: AAL19560.1.

PIR

B35441.

RefSeq

NP_459601.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HYU	X-ray	2.00	A	1-521	[»]
1ZYN	X-ray	2.30	A/B	1-202	[»]
1ZYP	X-ray	2.40	A/B	1-202	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2906N.

Genome annotation databases

GeneID

1252129.

GenomeReviews

Gene locus STM0609 in contig AE006468_GR.

KEGG

stm:STM0609.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P19480.

OMA

P19480. ELEGVFV.

Enzyme and pathway databases

BioCyc

STYP99287:STM0609-MON.

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.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.

Pfam

PF00462. Glutaredoxin. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]

PIRSF

PIRSF000238. AhpF. 1 hit.

PRINTS

PR00368. FADPNR.
PR00469. PNDRDTASEII.

ProDom

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

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_SALTY

Accession

Primary (citable) accession number: P19480

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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