ARREH_SYNY3
ID ARREH_SYNY3 Reviewed; 206 AA.
AC P74312;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=NADPH-dependent quinone reductase ArsH {ECO:0000305|PubMed:22304305};
DE EC=1.6.5.2 {ECO:0000269|PubMed:22304305};
DE AltName: Full=Arsenical resistance operon protein ArsH {ECO:0000303|PubMed:12949088};
GN Name=arsH {ECO:0000303|PubMed:12949088}; OrderedLocusNames=slr0945;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1] {ECO:0000312|EMBL:BAA18406.1, ECO:0000312|Proteomes:UP000001425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa {ECO:0000312|Proteomes:UP000001425};
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP GENE NAME, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa {ECO:0000303|PubMed:12949088};
RX PubMed=12949088; DOI=10.1128/jb.185.18.5363-5371.2003;
RA Lopez-Maury L., Florencio F.J., Reyes J.C.;
RT "Arsenic sensing and resistance system in the cyanobacterium Synechocystis
RT sp. strain PCC 6803.";
RL J. Bacteriol. 185:5363-5371(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, REACTION MECHANISM,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22304305; DOI=10.1021/bi201904p;
RA Hervas M., Lopez-Maury L., Leon P., Sanchez-Riego A.M., Florencio F.J.,
RA Navarro J.A.;
RT "ArsH from the cyanobacterium Synechocystis sp. PCC 6803 is an efficient
RT NADPH-dependent quinone reductase.";
RL Biochemistry 51:1178-1187(2012).
RN [4]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=24699748; DOI=10.1107/s2053230x14004865;
RA Zhang X., Xue X.M., Yan Y., Ye J.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of ArsH from Synechocystis sp. strain PCC 6803.";
RL Acta Crystallogr. F 70:497-500(2014).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24861149; DOI=10.1111/1574-6968.12481;
RA Xue X.M., Yan Y., Xu H.J., Wang N., Zhang X., Ye J.;
RT "ArsH from Synechocystis sp. PCC 6803 reduces chromate and ferric iron.";
RL FEMS Microbiol. Lett. 356:105-112(2014).
CC -!- FUNCTION: Has high NADPH-dependent quinone reductase activity with a
CC preference for quinones with hydrophobic substituents. Reduces also
CC CrO4(2-) and Fe(3+). Somewhat active with NADH. May be involved in
CC response to oxidative stress caused by arsenic.
CC {ECO:0000269|PubMed:22304305, ECO:0000269|PubMed:24861149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000269|PubMed:22304305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000269|PubMed:22304305};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:22304305};
CC -!- ACTIVITY REGULATION: Inhibited by NADP(+) and weakly by dicoumarol.
CC {ECO:0000269|PubMed:22304305}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31.5 uM for NADPH {ECO:0000269|PubMed:22304305};
CC KM=1.2 uM for dibromothymoquinone {ECO:0000269|PubMed:22304305};
CC KM=1.3 uM for 2,5-dimethyl-p-benzoquinone
CC {ECO:0000269|PubMed:22304305};
CC KM=2.8 uM for duroquinone {ECO:0000269|PubMed:22304305};
CC KM=5.7 uM for menadione {ECO:0000269|PubMed:22304305};
CC KM=23.7 uM for lawsone {ECO:0000269|PubMed:22304305};
CC KM=11.9 uM for coenzyme Q10 (approximate value)
CC {ECO:0000269|PubMed:22304305};
CC KM=34.5 uM for anthraquinone-2-sulfonate
CC {ECO:0000269|PubMed:22304305};
CC KM=600 uM for methyl-red {ECO:0000269|PubMed:22304305};
CC Redox potential:
CC E(0) is -181 +/- 2 mV at pH 7.5. {ECO:0000269|PubMed:22304305};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:24699748}.
CC -!- INDUCTION: By arsenite and arsenate ions, but not by CrO4(2-) or
CC Fe(3+). {ECO:0000269|PubMed:24861149}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:12949088). Sensitive
CC to the oxidizing agent menadione in the presence of arsenite ion
CC (PubMed:22304305). Decreased arsenic and chromium accumulation
CC (PubMed:24861149). {ECO:0000269|PubMed:12949088,
CC ECO:0000269|PubMed:22304305, ECO:0000269|PubMed:24861149}.
CC -!- SIMILARITY: Belongs to the ArsH family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18406.1; -; Genomic_DNA.
DR PIR; S76147; S76147.
DR AlphaFoldDB; P74312; -.
DR SMR; P74312; -.
DR IntAct; P74312; 2.
DR STRING; 1148.1653493; -.
DR PaxDb; P74312; -.
DR EnsemblBacteria; BAA18406; BAA18406; BAA18406.
DR KEGG; syn:slr0945; -.
DR eggNOG; COG0431; Bacteria.
DR InParanoid; P74312; -.
DR OMA; WSSPEMH; -.
DR PhylomeDB; P74312; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; ISS:UniProtKB.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:UniProtKB.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0010038; P:response to metal ion; IMP: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..206
FT /note="NADPH-dependent quinone reductase ArsH"
FT /id="PRO_0000432222"
FT BINDING 16..23
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9I4D4"
SQ SEQUENCE 206 AA; 23736 MW; 8EDF40AAF53F69DC CRC64;
MTDFNHPPRI LFLYGSLRER SYSRLLAEEA GRIITTMGAE TKFFDPRELP LRGQVLDSHP
KVQELLELSQ WSEGQVWSSP EMHGNITGIL KNQIDWIPLE IGSIRPTQGR TLAVMQVSGG
SQSFNAVNTM RILGRWMRMF TIPNQSSVAK AYQEFHEDGT MKDSPYRDRV VDVMEELYKF
TLLLRDKVDY LTDRHSERKA KVNTDG
