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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 22916FADBy similarityAdd
BLAST
Nucleotide bindingi357 – 37115NAD or NADPBy similarityAdd
BLAST
Nucleotide bindingi478 – 48811FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP

Enzyme and pathway databases

BioCyciSENT99287:GCTI-612-MONOMER.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Alkyl hydroperoxide reductase subunit FPRO_0000166777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Beta strandi21 – 266Combined sources
Helixi31 – 4414Combined sources
Beta strandi50 – 545Combined sources
Beta strandi58 – 603Combined sources
Beta strandi62 – 687Combined sources
Beta strandi77 – 804Combined sources
Helixi84 – 863Combined sources
Helixi87 – 9711Combined sources
Helixi106 – 1149Combined sources
Beta strandi119 – 1257Combined sources
Helixi132 – 14514Combined sources
Beta strandi149 – 1557Combined sources
Turni156 – 1583Combined sources
Helixi160 – 1656Combined sources
Beta strandi170 – 1767Combined sources
Beta strandi179 – 1846Combined sources
Helixi188 – 1958Combined sources
Helixi202 – 2087Combined sources
Beta strandi213 – 2186Combined sources
Helixi222 – 23312Combined sources
Beta strandi238 – 2414Combined sources
Helixi247 – 2493Combined sources
Beta strandi261 – 2644Combined sources
Helixi266 – 27813Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi303 – 3075Combined sources
Beta strandi312 – 3209Combined sources
Beta strandi324 – 3263Combined sources
Turni332 – 34110Combined sources
Helixi350 – 3534Combined sources
Beta strandi356 – 3616Combined sources
Helixi365 – 37713Combined sources
Beta strandi378 – 3847Combined sources
Beta strandi386 – 3894Combined sources
Helixi394 – 4007Combined sources
Beta strandi406 – 4094Combined sources
Beta strandi411 – 4199Combined sources
Beta strandi421 – 43111Combined sources
Turni432 – 4343Combined sources
Beta strandi437 – 4415Combined sources
Beta strandi443 – 4475Combined sources
Beta strandi451 – 4544Combined sources
Helixi456 – 4583Combined sources
Turni459 – 4613Combined sources
Beta strandi483 – 4853Combined sources
Helixi497 – 51822Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP19480.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 208100GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91Q → N AA sequence (PubMed:2643600).Curated
Sequence conflicti15 – 151E → DR AA sequence (PubMed:2643600).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1HYUX-ray2.00A1-521[»]
1ZYNX-ray2.30A/B1-202[»]
1ZYPX-ray2.40A/B1-202[»]
ProteinModelPortaliP19480.
SMRiP19480. Positions 1-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-2906N.
STRINGi99287.STM0609.

Chemistry

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.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-612-MONOMER.

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: September 7, 2016
This is version 137 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.