Reviewed, UniProtKB/Swiss-Prot P0A155 (AHPF_PSEPK)

Names and origin

Protein names

Recommended name:
    Alkyl hydroperoxide reductase subunit F
    EC=1.6.4.-

Gene names

Name:	ahpF
Ordered Locus Names:	PP_2440

Organism

Pseudomonas putida (strain KT2440) [Complete proteome] [HAMAP]

Taxonomic identifier

160488 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer By similarity.
Miscellaneous	The active site is a redox-active disulfide bond By similarity.
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	Disulfide bond
Technical term	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
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 – 520	520	Alkyl hydroperoxide reductase subunit F		PRO_0000166775
Regions
	Nucleotide binding	213 – 228	16	FAD By similarity
	Nucleotide binding	355 – 369	15	NAD or NADP By similarity
	Nucleotide binding	476 – 486	11	FAD By similarity
Amino acid modifications
	Disulfide bond	343 ↔ 346		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A155-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: 08FB3DE0D75C8A27	FASTA	520	55,350
	10 20 30 40 50 60 MLDATLKSQL KTYLERVTQP IEIVASLDDG AKSRELHDLL VEIASLSNLI TFSADGTDAR 70 80 90 100 110 120 RPSFSLNRPG ADISLRFAGI PMGHEFTSLV LALLQVGGHP SKASAEVIEQ IQALEGEFNF 130 140 150 160 170 180 ETYFSLSCQN CPDVVQALNL MAVLNPNVRH VAIDGALFQD EVESRKIMAV PSIYLNGEVF 190 200 210 220 230 240 GQGRMGLEEI LGKIDTNAGA RQAEKINAKE AFDVLVVGGG PAGAAAAIYA ARKGIRTGVA 250 260 270 280 290 300 AERFGGQVLD TLAIENFISV QETEGPKLAT ALEEHVKQYD VDIMNLQRGE ALIPAAEGGL 310 320 330 340 350 360 HEVRLAGGAS LKAKTVILAT GARWREMNVP GEQEYRGRGV AYCPHCDGPL FKGKRVAVIG 370 380 390 400 410 420 GGNSGVEAAI DLAGIVAQVT LIEFDSQLRA DAVLQRKLRS LPNVNVITSA LTTEVLGNGE 430 440 450 460 470 480 KVTGLRYKDR STDEQHEVAL EGIFVQIGLL PNTDWLKGTV ELSPRGEIIV DAKGQTSIPG 490 500 510 520 VFAAGDVTTV PYKQIVIAVG EGAKASLAAF DHLIRTSAPA

References

[1]

"Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440." Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., Madupu R., Nelson W.C., White O. , Peterson J.D., Khouri H.M., Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M. Environ. Microbiol. 4:799-808(2002) [PubMed: 12534463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE015451 Genomic DNA. Translation: AAN68052.1.
RefSeq	NP_744588.1.
3D structure databases
HSSP	HSSP built from PDB template 1FL2 based on UniProtKB P35340.
ModBase	Search...
Genome annotation databases
GeneID	1045609.
GenomeReviews	Gene locus PP_2440 in contig AE015451_GR.
KEGG	ppu:PP_2440.
NMPDR	fig|160488.1.peg.2418.
TIGR	PP_2440.
Phylogenomic databases
HOGENOM	P0A155.
OMA	P0A155. ELEGVFV.
Enzyme and pathway databases
BioCyc	PPUT160488:PP_2440-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	PF00070. Pyr_redox. 2 hits. 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_PSEPK

Accession

Primary (citable) accession number: P0A155
Secondary accession number(s): O82864

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	June 16, 2009
This is version 35 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)