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AHPF_SALTY
ID   AHPF_SALTY              Reviewed;         521 AA.
AC   P19480;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
DE   AltName: Full=Alkyl hydroperoxide reductase F52A protein;
GN   Name=ahpF; OrderedLocusNames=STM0609;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2191951; DOI=10.1016/s0021-9258(18)86980-0;
RA   Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N.;
RT   "Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and
RT   homology to thioredoxin reductase and other flavoprotein disulfide
RT   oxidoreductases.";
RL   J. Biol. Chem. 265:10535-10540(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-25.
RC   STRAIN=oxyR1;
RX   PubMed=2643600; DOI=10.1016/s0021-9258(18)94214-6;
RA   Jacobson F.S., Morgan R.W., Christman M.F., Ames B.N.;
RT   "An alkyl hydroperoxide reductase from Salmonella typhimurium involved in
RT   the defense of DNA against oxidative damage. Purification and properties.";
RL   J. Biol. Chem. 264:1488-1496(1989).
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.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; J05478; AAA16432.1; -; Unassigned_DNA.
DR   EMBL; AE006468; AAL19560.1; -; Genomic_DNA.
DR   PIR; B35441; B35441.
DR   RefSeq; NP_459601.1; NC_003197.2.
DR   RefSeq; WP_000887644.1; NC_003197.2.
DR   PDB; 1HYU; X-ray; 2.00 A; A=1-521.
DR   PDB; 1ZYN; X-ray; 2.30 A; A/B=1-202.
DR   PDB; 1ZYP; X-ray; 2.40 A; A/B=1-202.
DR   PDBsum; 1HYU; -.
DR   PDBsum; 1ZYN; -.
DR   PDBsum; 1ZYP; -.
DR   AlphaFoldDB; P19480; -.
DR   BMRB; P19480; -.
DR   SMR; P19480; -.
DR   DIP; DIP-2906N; -.
DR   STRING; 99287.STM0609; -.
DR   DrugBank; DB03147; Flavin adenine dinucleotide.
DR   PaxDb; P19480; -.
DR   PRIDE; P19480; -.
DR   EnsemblBacteria; AAL19560; AAL19560; STM0609.
DR   GeneID; 1252129; -.
DR   KEGG; stm:STM0609; -.
DR   PATRIC; fig|99287.12.peg.641; -.
DR   HOGENOM; CLU_031864_0_0_6; -.
DR   OMA; VTVFEFM; -.
DR   PhylomeDB; P19480; -.
DR   BioCyc; SENT99287:STM0609-MON; -.
DR   EvolutionaryTrace; P19480; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; 3.50.50.60; -; 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   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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   NAD; NADP; Oxidoreductase; Redox-active center; Reference proteome.
FT   CHAIN           1..521
FT                   /note="Alkyl hydroperoxide reductase subunit F"
FT                   /id="PRO_0000166777"
FT   DOMAIN          109..208
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   BINDING         214..229
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         357..371
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         478..488
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        345..348
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        9
FT                   /note="Q -> N (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="E -> DR (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           31..44
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          62..68
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           87..97
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           106..114
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           132..145
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          149..155
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           160..165
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          170..176
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          179..184
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           188..195
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           202..208
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          213..218
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           222..233
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          261..264
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           266..278
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          282..285
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          303..307
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          312..320
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          324..326
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   TURN            332..341
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           350..353
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          356..361
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           365..377
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          378..384
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          386..389
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           394..400
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          406..409
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          411..419
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          421..431
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   TURN            432..434
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          437..441
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          443..447
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          451..454
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           456..458
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   TURN            459..461
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   STRAND          483..485
FT                   /evidence="ECO:0007829|PDB:1HYU"
FT   HELIX           497..518
FT                   /evidence="ECO:0007829|PDB:1HYU"
SQ   SEQUENCE   521 AA;  55950 MW;  813DEA1398DAE26F CRC64;
     MLDTNMKTQL RAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV TFKEDNTLPV
     RKPSFLITNP GSQQGPRFAG SPLGHEFTSL VLALLWTGGH PSKEAQSLLE QIRDIDGDFE
     FETYYSLSCH NCPDVVQALN LMAVLNPRIK HTAIDGGTFQ NEITERNVMG VPAVFVNGKE
     FGQGRMTLTE IVAKVDTGAE KRAAEALNKR DAYDVLIVGS GPAGAAAAVY SARKGIRTGL
     MGERFGGQVL DTVDIENYIS VPKTEGQKLA GALKAHVSDY DVDVIDSQSA SKLVPAATEG
     GLHQIETASG AVLKARSIII ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG PLFKGKRVAV
     IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKV RSLKNVDIIL NAQTTEVKGD
     GSKVVGLEYR DRVSGDIHSV ALAGIFVQIG LLPNTHWLEG ALERNRMGEI IIDAKCETSV
     KGVFAAGDCT TVPYKQIIIA TGEGAKASLS AFDYLIRTKI A
 
 
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