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Protein

Alkyl hydroperoxide reductase subunit F

Gene

ahpF

Organism
Xanthomonas campestris pv. phaseoli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 bindingi356 – 370NAD or NADPBy similarityAdd BLAST15
Nucleotide bindingi477 – 487FADBy 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.-)
Gene namesi
Name:ahpF
OrganismiXanthomonas campestris pv. phaseoli
Taxonomic identifieri317013 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001667871 – 530Alkyl hydroperoxide reductase subunit FAdd BLAST530

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi344 ↔ 347Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiO06465.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO06465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
3.40.50.720. 1 hit.
3.50.50.60. 1 hit.
InterProiIPR012081. Alkyl_hydroperoxide_Rdtase_suF.
IPR023753. FAD/NAD-binding_dom.
IPR002109. Glutaredoxin.
IPR016040. NAD(P)-bd_dom.
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.

O06465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDANLKTQL TAYLERVTRP IQINASIDDS AGSREMLDLL EELVLLSDKI
60 70 80 90 100
SLDIHRDDNQ RKPSFALTTP GQDISLRFAG LPMGHEFTSL VLALLQVGGH
110 120 130 140 150
PSKAAAELIE QVQHLEGDYQ FETYFSLSCQ NCPDVVQALN LAAVLNPRIK
160 170 180 190 200
HVAIDGAWFQ DEVQARQIMS VPTVYLNGEL FDQGRMTLEQ IVAKLDTNAA
210 220 230 240 250
KRDAAKIAAK EAFDVLVVGG GPAGSAAAVY AARKGIRTGV AAERFGGQVL
260 270 280 290 300
DTMSIENFIS VPETEGPKMA AALEQHVRQY DVDIMNLQRA EQLIPAGADG
310 320 330 340 350
LIEIKLANGA SLKSKTVILS TGARWRQMNV PGEDQYKNKG VAYCPHCDGP
360 370 380 390 400
LFKGKRVAVI GGGNSGVEAA IDLAGIVAHV TLVEFDDKLR ADEVLQRKLR
410 420 430 440 450
SLHNVRIITS AQTTEVLGDG QKVTGLVYKD RTGGDIQHIE LEGVFVQIGL
460 470 480 490 500
LPNTEFLRGT VALSPRGEII VDDRGQTDVP GVFAAGDATT VPYKQIVIAM
510 520 530
GEGSKAALSA FDHLIRTSAP ATADSVAQAA
Length:530
Mass (Da):56,922
Last modified:July 1, 1997 - v1
Checksum:iABC1105C8A6FCD24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94336 Genomic DNA. Translation: AAC45426.1.
RefSeqiWP_039567731.1. NZ_JWTI02000066.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94336 Genomic DNA. Translation: AAC45426.1.
RefSeqiWP_039567731.1. NZ_JWTI02000066.1.

3D structure databases

ProteinModelPortaliO06465.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO06465.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
3.40.50.720. 1 hit.
3.50.50.60. 1 hit.
InterProiIPR012081. Alkyl_hydroperoxide_Rdtase_suF.
IPR023753. FAD/NAD-binding_dom.
IPR002109. Glutaredoxin.
IPR016040. NAD(P)-bd_dom.
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_XANCH
AccessioniPrimary (citable) accession number: O06465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 93 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.

Documents

  1. 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.