(data stored in SCRATCH zone)

SWISSPROT: D6XX71_BACIE

ID   D6XX71_BACIE            Unreviewed;       516 AA.
AC   D6XX71;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   SubName: Full=Alkyl hydroperoxide reductase, F subunit {ECO:0000313|EMBL:ADH97928.1};
GN   OrderedLocusNames=Bsel_0388 {ECO:0000313|EMBL:ADH97928.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97928.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97928.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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};
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DR   EMBL; CP001791; ADH97928.1; -; Genomic_DNA.
DR   RefSeq; WP_013171357.1; NC_014219.1.
DR   STRING; 439292.Bsel_0388; -.
DR   EnsemblBacteria; ADH97928; ADH97928; Bsel_0388.
DR   KEGG; bse:Bsel_0388; -.
DR   eggNOG; ENOG4108JU3; Bacteria.
DR   eggNOG; COG3634; LUCA.
DR   HOGENOM; HOG000169462; -.
DR   KO; K03387; -.
DR   OMA; VPLGHEF; -.
DR   OrthoDB; 692968at2; -.
DR   BioCyc; BSEL439292:G1GLR-418-MONOMER; -.
DR   Proteomes; UP000000271; 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 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; D6XX71.
DR   SWISS-2DPAGE; D6XX71.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
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:UP000000271}.
FT   DOMAIN      108    210       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
FT   NP_BIND     210    225       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   NP_BIND     349    363       NAD or NADP. {ECO:0000256|PIRSR:
FT                                PIRSR000238-1}.
FT   NP_BIND     469    479       FAD. {ECO:0000256|PIRSR:PIRSR000238-1}.
FT   DISULFID    337    340       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000238-2}.
SQ   SEQUENCE   516 AA;  55333 MW;  769B6E10C5133D42 CRC64;
     MVLDNAITQQ LKQYLDLLEG DLTFKLDAGS DANSDKLAGF VREVASMSPR ITVEEASLAR
     TPSFTVTRTG ENTGVTFAGV PLGHEFTSFV LAILQVSGRP PKVEEETLNQ MKQLEGDFTF
     ETYVSLSCQN CPEVVQALNM LSAVNPGVTN TMIDGAAFKD EVEARDVMAV PAVYLNGEFL
     GGGRMTIEDI LEKLGQGTDA SELDAKDPFD VLVVGGGPAG ASAAVYASRK GIRTGVVAER
     FGGQVQDTMS IENFISVKKT EGPKLVASLE EHVRDYSVDI MKSQRVKAVD KKDLFEVTLE
     NGAVLKSKSV ILSTGARWRN VGVPGEEAFK NNGVAYCPHC DGPLFEGKDV SVIGGGNSGV
     EAAIDLAGIV NHVYLLEFMP ELKADEVLQK KLHSLPNVTV ITNAQTTEIT GDKKVNGISY
     KDRVTEEDRH IPLQGVFVQI GLVPNTEFLD DSIETTRMGE IVVDQHGATN VPGLFAAGDC
     TNTPYKQIII SMGSGATASL GAFDYLIRSE EPVVSV
//

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