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