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ARREH_ACIF2
ID   ARREH_ACIF2             Reviewed;         237 AA.
AC   B7J950;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=NADPH-dependent FMN reductase ArsH {ECO:0000303|PubMed:21617342};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21617342};
DE   AltName: Full=Arsenical resistance operon protein ArsH {ECO:0000305, ECO:0000312|EMBL:ACK78531.1};
GN   Name=arsH {ECO:0000312|EMBL:ACK78531.1};
GN   OrderedLocusNames=AFE_2857 {ECO:0000312|EMBL:ACK78531.1};
OS   Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS   / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=243159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC   {ECO:0000312|Proteomes:UP000001362};
RX   PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA   Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA   Eisen J.A., Holmes D.S.;
RT   "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT   industrial applications.";
RL   BMC Genomics 9:597-597(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBSTRATE SPECIFICITY, MUTAGENESIS OF GLU-104, AND 3D-STRUCTURE MODELING.
RC   STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC   {ECO:0000303|PubMed:21617342};
RX   PubMed=21617342; DOI=10.4014/jmb.1101.01020;
RA   Mo H., Chen Q., Du J., Tang L., Qin F., Miao B., Wu X., Zeng J.;
RT   "Ferric reductase activity of the ArsH protein from Acidithiobacillus
RT   ferrooxidans.";
RL   J. Microbiol. Biotechnol. 21:464-469(2011).
CC   -!- FUNCTION: Has NADPH-dependent FMN reductase activity and high NADPH-
CC       dependent ferric reductase activity with highest activity for Fe(3+) as
CC       substrate. No activity with NADH, iron trichloride, Cu(2+) or Ag(+).
CC       May be involved in cytosolic ferric iron assimilation as an NADPH-
CC       dependent ferric reductase in vivo. {ECO:0000269|PubMed:21617342}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:21617342};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=76 uM for NADPH {ECO:0000269|PubMed:21617342};
CC         KM=30 uM for Fe(3+) {ECO:0000269|PubMed:21617342};
CC         Vmax=21.6 umol/min/mg enzyme {ECO:0000269|PubMed:21617342};
CC       pH dependence:
CC         Optimum pH is 6.5 for the ferric reductase activity.
CC         {ECO:0000269|PubMed:21617342};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius for the ferric reductase
CC         activity. {ECO:0000269|PubMed:21617342};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q92R45}.
CC   -!- SIMILARITY: Belongs to the ArsH family. {ECO:0000305}.
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DR   EMBL; CP001219; ACK78531.1; -; Genomic_DNA.
DR   RefSeq; WP_009566875.1; NC_011761.1.
DR   AlphaFoldDB; B7J950; -.
DR   SMR; B7J950; -.
DR   STRING; 243159.AFE_2857; -.
DR   PaxDb; B7J950; -.
DR   EnsemblBacteria; ACK78531; ACK78531; AFE_2857.
DR   GeneID; 66433806; -.
DR   KEGG; afr:AFE_2857; -.
DR   eggNOG; COG0431; Bacteria.
DR   HOGENOM; CLU_055322_0_1_6; -.
DR   OMA; WSSPEMH; -.
DR   OrthoDB; 1818437at2; -.
DR   Proteomes; UP000001362; Chromosome.
DR   GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:UniProtKB.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IDA:UniProtKB.
DR   GO; GO:0010181; F:FMN binding; ISS:UniProtKB.
DR   GO; GO:0052873; F:FMN reductase (NADPH) activity; IDA:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR014063; Arsenate-R_ArsH.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   PANTHER; PTHR43590; PTHR43590; 1.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   TIGRFAMs; TIGR02690; resist_ArsH; 1.
PE   1: Evidence at protein level;
KW   Flavoprotein; FMN; NADP; Nucleotide-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..237
FT                   /note="NADPH-dependent FMN reductase ArsH"
FT                   /id="PRO_0000432219"
FT   BINDING         39..46
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4D4"
FT   BINDING         102..107
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000305|PubMed:21617342"
FT   MUTAGEN         104
FT                   /note="E->A: Loss of ferric reductase activity. Does not
FT                   bind FMN cofactor."
FT                   /evidence="ECO:0000269|PubMed:21617342"
FT   MUTAGEN         104
FT                   /note="E->D,Q: Strongly reduced ferric reductase activity.
FT                   Binds FMN cofactor."
FT                   /evidence="ECO:0000269|PubMed:21617342"
SQ   SEQUENCE   237 AA;  26871 MW;  31D17462108AE52C CRC64;
     MSGNLPNTDD VLLQVPDVRC LRSAAETDHP PRILLLYGSN RECSYSRLLT LEAERLLRYF
     GAETRVFHPT GLPLPDDAPV THPKVVELQE LVEWSEGQVW CSPERHGAMT GVFKSQVDWI
     PLNSGAIRPT QGKTLALMQV CGGSQSFNAV NQMRILGRWL RMLTIPNQSS VPKAFLEFDD
     GGRMKPSAYY DRVVDVMEEL MKFTLLTRGN SDYLVDRYSE RKESAEELSR RVNLQNL
 
 
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