ID Q8ZPG3_SALTY Unreviewed; 502 AA.
AC Q8ZPG3;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000256|ARBA:ARBA00020059};
GN OrderedLocusNames=STM1546 {ECO:0000313|EMBL:AAL20465.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL20465.1, ECO:0000313|Proteomes:UP000001014};
RN [1] {ECO:0000313|EMBL:AAL20465.1, ECO:0000313|Proteomes:UP000001014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720
RC {ECO:0000313|Proteomes:UP000001014};
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Serves to protect the cell against DNA damage by alkyl
CC hydroperoxides. It can use either NADH or NADPH as electron donor for
CC direct reduction of redox dyes or of alkyl hydroperoxides when combined
CC with the AhpC protein. {ECO:0000256|ARBA:ARBA00024806}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; AE006468; AAL20465.1; -; Genomic_DNA.
DR RefSeq; NP_460506.1; NC_003197.2.
DR RefSeq; WP_000199411.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPG3; -.
DR SMR; Q8ZPG3; -.
DR STRING; 99287.STM1546; -.
DR PaxDb; 99287-STM1546; -.
DR GeneID; 1253064; -.
DR KEGG; stm:STM1546; -.
DR PATRIC; fig|99287.12.peg.1634; -.
DR HOGENOM; CLU_009665_20_3_6; -.
DR OMA; YPQDRHE; -.
DR PhylomeDB; Q8ZPG3; -.
DR BioCyc; SENT99287:STM1546-MONOMER; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 3.30.70.2450; -; 1.
DR Gene3D; 3.40.30.120; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:AAL20465.1};
KW Oxidoreductase {ECO:0000313|EMBL:AAL20465.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001014}.
FT DOMAIN 7..346
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 502 AA; 55739 MW; FCAE10973ECEEB90 CRC64;
MTRYTTTDVL ICGAGVTGLT LAIELARHGV SFRLIEKRTT PFIGSRGKGI QPRTQEIFED
LGILNKVVAA GGLYPRLRTY RHDGSYVDSD IAHHTKPTHA EPYHLPLMVP QNVTETIMRE
QLKAWGHRVE FGCELRHFAQ TPRTVTAYVA GPAGEEVIIA HYLIGADGGG SFVRKKLGVS
FPGRTLGIHA LVADASLSGL NRDVWHHFND GDMARMITIC PLAGTQLFQI QALLAPDDSQ
NFSADVLTAF LTERIGRTDV RIHSIPWVSK YQMNARIAEH YRVGKVFLAG DAAHVHPPTG
GQGLNTSIQD AYNLGWKMAA SLRGAGEELL DSYEQERRPI AESLLHLSTR LLDSQKQRGI
KRERDVQQLD IQYTNSPLAH TLPERQHGLQ AGERAPDAPL LGAGGQSLRL FQLLQGPDWN
LLAYETHGKV IDARRGLRIH HIGEQDELID TLGHFRESYH LAPGQCVLIR PDGYVGAFFH
GKQSNDIENY LSRFAIGIKD EY
//
