(data stored in SCRATCH zone)

SWISSPROT: B2UHJ6_RALPJ

ID   B2UHJ6_RALPJ            Unreviewed;       524 AA.
AC   B2UHJ6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   SubName: Full=Alkyl hydroperoxide reductase, F subunit {ECO:0000313|EMBL:ACD29047.1};
GN   OrderedLocusNames=Rpic_3942 {ECO:0000313|EMBL:ACD29047.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29047.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001069; ACD29047.1; -; Genomic_DNA.
DR   RefSeq; WP_012430076.1; NC_010678.1.
DR   STRING; 402626.Rpic_3942; -.
DR   EnsemblBacteria; ACD29047; ACD29047; Rpic_3942.
DR   GeneID; 6285143; -.
DR   KEGG; rpi:Rpic_3942; -.
DR   PATRIC; fig|402626.5.peg.181; -.
DR   eggNOG; ENOG4108JU3; Bacteria.
DR   eggNOG; COG3634; LUCA.
DR   HOGENOM; HOG000169462; -.
DR   KO; K03387; -.
DR   OMA; SRNIMAV; -.
DR   OrthoDB; 692968at2; -.
DR   BioCyc; RPIC402626:GH94-3943-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 2.
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 transfer 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; -; 2.
DR   InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF000238; AhpF; 1.
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   4: Predicted;
DR   PRODOM; B2UHJ6.
DR   SWISS-2DPAGE; B2UHJ6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000238-2};
KW   FAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000238-1};
KW   NAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW   NADP {ECO:0000256|PIRSR:PIRSR000238-1};
KW   Redox-active center {ECO:0000256|PIRSR:PIRSR000238-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   DOMAIN      109    208       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
FT   NP_BIND     214    229       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   NP_BIND     357    371       NAD or NADP. {ECO:0000256|PIRSR:
FT                                PIRSR000238-1}.
FT   NP_BIND     478    488       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   DISULFID    345    348       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000238-2}.
SQ   SEQUENCE   524 AA;  55852 MW;  EDA59DF99BE3EEA3 CRC64;
     MLDADVKAQL KAYLERLVQP IELVANVDDS EGSRDMMDLL RDVAEQSSMI VLTEQRDAAE
     RAPSFLIRRT GADVSVRFAA IPTGHEFTSL VLALLQVGGY APKLEADVIE QIRNIEGDFR
     FETYMSLTCQ NCPDVVQALN VMSVINPRIQ HVAIDGALYQ GEIEARQIMA VPTVFLNGET
     FGTGRMGVEE ILAKIDTGAA ARDAEKLAAK EAFDVLIVGG GPAGAAAAVY AARKGVRTGV
     VAERFGGQVL DTLGIENFIS VQETEGPKFA AALEQHVRQY DVDIMNTQRA VKLTPADKPG
     GFAEVTLANG AVLKGRSVIL STGARWRNVN VPGEQEYKNK GVAYCPHCDG PLFKGKRVAV
     IGGGNSGVEA AIDLAGLVSH VTLLEFASEL KADAVLVRKL QSLPNATIVT NAQTTEITGD
     GQKVNGLRYK SRVDGVEHTV ALEGVFVQIG LVPNTEWLDG ALERNRFGEI VVDARGQTSA
     EGVFAAGDAT TTPYKQIIIA TGDGAKAALS AFDHLIRVPL AEAA
//

If you have problems or comments...

PBIL Back to PBIL home page