GenomeNet

Database: UniProt
Entry: A0A0U1Q1Q0_9BURK
LinkDB: A0A0U1Q1Q0_9BURK
Original site: A0A0U1Q1Q0_9BURK 
ID   A0A0U1Q1Q0_9BURK        Unreviewed;       518 AA.
AC   A0A0U1Q1Q0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Alkyl hydroperoxide reductase {ECO:0000313|EMBL:KKW68688.1};
GN   ORFNames=AAV94_03975 {ECO:0000313|EMBL:KKW68688.1};
OS   Lampropedia cohaerens.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Lampropedia.
OX   NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW68688.1, ECO:0000313|Proteomes:UP000050580};
RN   [1] {ECO:0000313|EMBL:KKW68688.1, ECO:0000313|Proteomes:UP000050580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT6 {ECO:0000313|EMBL:KKW68688.1,
RC   ECO:0000313|Proteomes:UP000050580};
RA   Tripathi C., Rani P., Mahato N.K., Lal R.;
RT   "Draft genome sequence of Lampropedia sp. CT6, isolated from the microbial
RT   mat of a hot water spring, located at Manikaran, India.";
RL   Submitted (MAY-2015) 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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKW68688.1}.
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; LBNQ01000016; KKW68688.1; -; Genomic_DNA.
DR   RefSeq; WP_046741035.1; NZ_LBNQ01000016.1.
DR   AlphaFoldDB; A0A0U1Q1Q0; -.
DR   STRING; 1610491.AAV94_03975; -.
DR   PATRIC; fig|1610491.3.peg.848; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000050580; Unassembled WGS sequence.
DR   GO; GO:0008785; F:alkyl hydroperoxide reductase 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:0000302; P:response to reactive oxygen species; IEA:InterPro.
DR   CDD; cd03026; AhpF_NTD_C; 1.
DR   CDD; cd02974; AhpF_NTD_N; 1.
DR   Gene3D; 3.40.30.80; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR044141; AhpF_NTD_C.
DR   InterPro; IPR044142; AhpF_NTD_N.
DR   InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR03140; AhpF; 1.
DR   PANTHER; PTHR48105:SF6; ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF000238; AhpF; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR000238-2}; FAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000238-1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000238-1};
KW   NADP {ECO:0000256|PIRSR:PIRSR000238-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR000238-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050580}.
FT   DOMAIN          125..190
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13192"
FT   DOMAIN          212..504
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   BINDING         213..228
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT   BINDING         356..370
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT   BINDING         478..488
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT   DISULFID        344..347
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ   SEQUENCE   518 AA;  55625 MW;  95A8FA33AE9B07B1 CRC64;
     MLDDALKTQL KAYLERLTKP VELVASLDDS EGAREMLQLL EEIREQSDKI TVRTDGNDAR
     KPSFLITNPG IDTSLRFAGV PLGHEFTSLV LALLQVGGHP SKEPQELQEQ IKALEGPLHF
     ETYYSITCHN CPDVIQALNL MTVLNPNITH TAIDGALYQN EIEAREIMGV PTVYLNGEHF
     GQGRMELAEI VARLDTGAAA KAAKAISEKE PFDVLIVGGG PAGAAAAIYA ARKGIRTGVA
     AERFGGQVLD TLDIENYISV PKTDGPKFAA ALETHVKDYD VDIMNLQTAS KLIPAQTQGG
     LHEVQFESGA SLKAKTVILA TGARWRNMNV PGEQEYRTKG VTYCPHCDGP LFKGKRVAVI
     GGGNSGVEAA IDLAGVVAHV TLLEFADKLR ADQVLQKKLH SLPNVDVLFN AQTTEVLGKD
     GKVVGLAYKN RVTGEDLRLD LEGVFVQIGL LPNTNWLKGV VELSSPMGEI VIDSHGRTSV
     PGVFAAGDCT TVPYKQIVIA AGEGAKAALS AFDYLIRA
//
DBGET integrated database retrieval system