(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZK64_PSEAB

ID   A0A0H2ZK64_PSEAB        Unreviewed;       521 AA.
AC   A0A0H2ZK64;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 10.
DE   SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:ABJ15096.1};
GN   Name=ahpF {ECO:0000313|EMBL:ABJ15096.1};
GN   OrderedLocusNames=PA14_01720 {ECO:0000313|EMBL:ABJ15096.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15096.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15096.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15096.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000238-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000238-1};
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003880}.
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DR   EMBL; CP000438; ABJ15096.1; -; Genomic_DNA.
DR   RefSeq; WP_003137023.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZK64; -.
DR   EnsemblBacteria; ABJ15096; ABJ15096; PA14_01720.
DR   KEGG; pau:PA14_01720; -.
DR   KO; K03387; -.
DR   OMA; VPLGHEF; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 4.
DR   InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF000238; AhpF; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   TIGRFAMs; TIGR03140; AhpF; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZK64.
DR   SWISS-2DPAGE; A0A0H2ZK64.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000238-2};
KW   FAD {ECO:0000256|PIRSR:PIRSR000238-1, ECO:0000256|RuleBase:RU003880};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW   NAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW   NADP {ECO:0000256|PIRSR:PIRSR000238-1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003880};
KW   Redox-active center {ECO:0000256|PIRSR:PIRSR000238-2,
KW   ECO:0000256|RuleBase:RU003880}.
FT   DOMAIN      108    207       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
FT   NP_BIND     213    228       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   NP_BIND     356    370       NAD or NADP. {ECO:0000256|PIRSR:
FT                                PIRSR000238-1}.
FT   NP_BIND     477    487       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   DISULFID    344    347       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000238-2}.
SQ   SEQUENCE   521 AA;  55824 MW;  4F2C1C1884539C95 CRC64;
     MLDANLKTQL KAYLEKVSQP FEIVASLDDS DKSRELLGLL QDIVGLTDKI TLKTDGSDAR
     KPSFSLNRPG ADIGLRFAGI PMGHEFTSLV LALLQVGGHP SKLDADVIEQ VKGIEGTFEF
     ETYFSLSCQN CPDVVQALNL MAVLNPNIRH VAIDGALFQD EVEARQIMSV PSIYLNGEVF
     GQGRMGVEEI LAKIDTGAAA RDAEKLTARD AFDVLVVGGG PAGAAAAIYA ARKGIRTGVA
     AERFGGQVLD TMAIENFISV QETDGPKLAR ALEEHVRHYE VDIMNLQRAS KLVPAKNTGE
     LHEVQFESGG SLKAKTLILA TGARWREMGV PGEQEYKAKG VCFCPHCDGP LFKGKRVAVI
     GGGNSGVEAA IDLAGIVAHV TLLEFDSKLR ADAVLQRKLY SLPNVEVITS ALTSEVKGDG
     QKVTGLVYKD RNSEEFKSIE LEGIFVQIGL LPNTEWLKGS VELSPRGEII VDARGETSLP
     GIFAAGDVTT VPYKQIVIAV GEGAKASLSA FDHLIRTSAP E
//

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