Reviewed, UniProtKB/Swiss-Prot Q5HRY2 (AHPF_STAEQ)

Names and origin

Protein names

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

Gene names

Name:	ahpF
Ordered Locus Names:	SERP0059

Organism

Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]

Taxonomic identifier

176279 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	507 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.
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	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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 507	507	Alkyl hydroperoxide reductase subunit F		PRO_0000166786
Regions
	Nucleotide binding	207 – 222	16	FAD By similarity
	Nucleotide binding	347 – 361	15	NAD or NADP By similarity
	Nucleotide binding	467 – 477	11	FAD By similarity
Amino acid modifications
	Disulfide bond	335 ↔ 338		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HRY2-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: A0E424F17328DCC9	FASTA	507	54,688
	10 20 30 40 50 60 MLNADLKQQL QQLLELMEGD VEFVASLGSD DKSNELKELL NEMAEMSAHI TITEKSLKRT 70 80 90 100 110 120 PSFSVNRPGE ETGITFAGIP LGHEFNSLVL AILQVSGRAP KEKQSIIDQI KGLEGPFHFE 130 140 150 160 170 180 TFVSLTCQKC PDVVQALNLM SVINPNITHT MIDGAVFREE SENIMAVPAV FLDGQEFGNG 190 200 210 220 230 240 RMTVQDILTK LGSTQDASEF NDKDPYDVLI VGGGPASGSA AIYTARKGLR TGIVADRIGG 250 260 270 280 290 300 QVNDTAGIEN FITVKETTGS EFSSNLAEHI AQYDIDTMTG IRATNIEKTD SAIRVTLEND 310 320 330 340 350 360 AVLESKTVII STGASWRKLN IPGEDRLINK GVAFCPHCDG PLFENKDVAV IGGGNSGVEA 370 380 390 400 410 420 AIDLAGIVKH VTLFEYASEL KADSVLQERL RSLPNVDIKT SAKTTEVIGD DYVTGISYED 430 440 450 460 470 480 MTTGESQVVN LDGIFVQIGL VPNTSWLQNA VELNERGEVM INRDNATNVP GIFAAGDVTD 490 500 QKNKQIIISM GAGANAALNA FDYIIRN

References

[1]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000029 Genomic DNA. Translation: AAW53450.1.
RefSeq	YP_187657.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3242974.
GenomeReviews	Gene locus SERP0059 in contig CP000029_GR.
KEGG	ser:SERP0059.
NMPDR	fig|176279.3.peg.288.
TIGR	SERP0059.
Phylogenomic databases
HOGENOM	Q5HRY2.
OMA	Q5HRY2. ELEGVFV.
Enzyme and pathway databases
BioCyc	SEPI176279:SERP0059-MON.
Family and domain databases
InterPro	IPR012081. Alkyl_hydroperoxide_Rdtase_suF. IPR013027. FAD_pyr_nucl-diS_OxRdtase. 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. 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	PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AHPF_STAEQ

Accession

Primary (citable) accession number: Q5HRY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	February 15, 2005
Last modified:	June 16, 2009
This is version 33 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)