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Protein

Alkyl hydroperoxide reductase subunit F

Gene

ahpF

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 229FADBy similarityAdd BLAST16
Nucleotide bindingi357 – 371NAD or NADPBy similarityAdd BLAST15
Nucleotide bindingi478 – 488FADBy similarityAdd BLAST11

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyl hydroperoxide reductase subunit F (EC:1.8.1.-)
Alternative name(s):
Alkyl hydroperoxide reductase F52A protein
Gene namesi
Name:ahpF
Ordered Locus Names:STM0609
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001667771 – 521Alkyl hydroperoxide reductase subunit FAdd BLAST521

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi345 ↔ 348Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP19480.
PRIDEiP19480.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-2906N.
STRINGi99287.STM0609.

Structurei

Secondary structure

1521
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Beta strandi21 – 26Combined sources6
Helixi31 – 44Combined sources14
Beta strandi50 – 54Combined sources5
Beta strandi58 – 60Combined sources3
Beta strandi62 – 68Combined sources7
Beta strandi77 – 80Combined sources4
Helixi84 – 86Combined sources3
Helixi87 – 97Combined sources11
Helixi106 – 114Combined sources9
Beta strandi119 – 125Combined sources7
Helixi132 – 145Combined sources14
Beta strandi149 – 155Combined sources7
Turni156 – 158Combined sources3
Helixi160 – 165Combined sources6
Beta strandi170 – 176Combined sources7
Beta strandi179 – 184Combined sources6
Helixi188 – 195Combined sources8
Helixi202 – 208Combined sources7
Beta strandi213 – 218Combined sources6
Helixi222 – 233Combined sources12
Beta strandi238 – 241Combined sources4
Helixi247 – 249Combined sources3
Beta strandi261 – 264Combined sources4
Helixi266 – 278Combined sources13
Beta strandi282 – 285Combined sources4
Beta strandi290 – 294Combined sources5
Beta strandi303 – 307Combined sources5
Beta strandi312 – 320Combined sources9
Beta strandi324 – 326Combined sources3
Turni332 – 341Combined sources10
Helixi350 – 353Combined sources4
Beta strandi356 – 361Combined sources6
Helixi365 – 377Combined sources13
Beta strandi378 – 384Combined sources7
Beta strandi386 – 389Combined sources4
Helixi394 – 400Combined sources7
Beta strandi406 – 409Combined sources4
Beta strandi411 – 419Combined sources9
Beta strandi421 – 431Combined sources11
Turni432 – 434Combined sources3
Beta strandi437 – 441Combined sources5
Beta strandi443 – 447Combined sources5
Beta strandi451 – 454Combined sources4
Helixi456 – 458Combined sources3
Turni459 – 461Combined sources3
Beta strandi483 – 485Combined sources3
Helixi497 – 518Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HYUX-ray2.00A1-521[»]
1ZYNX-ray2.30A/B1-202[»]
1ZYPX-ray2.40A/B1-202[»]
ProteinModelPortaliP19480.
SMRiP19480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19480.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini109 – 208GlutaredoxinPROSITE-ProRule annotationAdd BLAST100

Sequence similaritiesi

Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4108JU3. Bacteria.
COG3634. LUCA.
HOGENOMiHOG000169462.
KOiK03387.
OMAiAVRKPSF.
PhylomeDBiP19480.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
3.50.50.60. 3 hits.
InterProiIPR012081. Alkyl_hydroperoxide_Rdtase_suF.
IPR023753. FAD/NAD-binding_dom.
IPR002109. Glutaredoxin.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF13192. Thioredoxin_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000238. AhpF. 1 hit.
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR03140. AhpF. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19480-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDTNMKTQL RAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV
60 70 80 90 100
TFKEDNTLPV RKPSFLITNP GSQQGPRFAG SPLGHEFTSL VLALLWTGGH
110 120 130 140 150
PSKEAQSLLE QIRDIDGDFE FETYYSLSCH NCPDVVQALN LMAVLNPRIK
160 170 180 190 200
HTAIDGGTFQ NEITERNVMG VPAVFVNGKE FGQGRMTLTE IVAKVDTGAE
210 220 230 240 250
KRAAEALNKR DAYDVLIVGS GPAGAAAAVY SARKGIRTGL MGERFGGQVL
260 270 280 290 300
DTVDIENYIS VPKTEGQKLA GALKAHVSDY DVDVIDSQSA SKLVPAATEG
310 320 330 340 350
GLHQIETASG AVLKARSIII ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG
360 370 380 390 400
PLFKGKRVAV IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKV
410 420 430 440 450
RSLKNVDIIL NAQTTEVKGD GSKVVGLEYR DRVSGDIHSV ALAGIFVQIG
460 470 480 490 500
LLPNTHWLEG ALERNRMGEI IIDAKCETSV KGVFAAGDCT TVPYKQIIIA
510 520
TGEGAKASLS AFDYLIRTKI A
Length:521
Mass (Da):55,950
Last modified:February 1, 1991 - v1
Checksum:i813DEA1398DAE26F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9Q → N AA sequence (PubMed:2643600).Curated1
Sequence conflicti15E → DR AA sequence (PubMed:2643600).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05478 Unassigned DNA. Translation: AAA16432.1.
AE006468 Genomic DNA. Translation: AAL19560.1.
PIRiB35441.
RefSeqiNP_459601.1. NC_003197.1.
WP_000887644.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19560; AAL19560; STM0609.
GeneIDi1252129.
KEGGistm:STM0609.
PATRICi32379563. VBISalEnt20916_0641.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05478 Unassigned DNA. Translation: AAA16432.1.
AE006468 Genomic DNA. Translation: AAL19560.1.
PIRiB35441.
RefSeqiNP_459601.1. NC_003197.1.
WP_000887644.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HYUX-ray2.00A1-521[»]
1ZYNX-ray2.30A/B1-202[»]
1ZYPX-ray2.40A/B1-202[»]
ProteinModelPortaliP19480.
SMRiP19480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-2906N.
STRINGi99287.STM0609.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PaxDbiP19480.
PRIDEiP19480.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19560; AAL19560; STM0609.
GeneIDi1252129.
KEGGistm:STM0609.
PATRICi32379563. VBISalEnt20916_0641.

Phylogenomic databases

eggNOGiENOG4108JU3. Bacteria.
COG3634. LUCA.
HOGENOMiHOG000169462.
KOiK03387.
OMAiAVRKPSF.
PhylomeDBiP19480.

Miscellaneous databases

EvolutionaryTraceiP19480.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
3.50.50.60. 3 hits.
InterProiIPR012081. Alkyl_hydroperoxide_Rdtase_suF.
IPR023753. FAD/NAD-binding_dom.
IPR002109. Glutaredoxin.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF13192. Thioredoxin_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000238. AhpF. 1 hit.
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR03140. AhpF. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAHPF_SALTY
AccessioniPrimary (citable) accession number: P19480
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.