ARREH_RHIME
ID ARREH_RHIME Reviewed; 241 AA.
AC Q92R45;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=NADPH-dependent FMN reductase ArsH {ECO:0000305};
DE EC=1.-.-.- {ECO:0000269|PubMed:17673204};
DE AltName: Full=Arsenical resistance operon protein ArsH {ECO:0000305};
GN Name=arsH {ECO:0000303|PubMed:16199569, ECO:0000312|EMBL:CAC45653.1};
GN OrderedLocusNames=R01074 {ECO:0000312|EMBL:CAC45653.1};
GN ORFNames=SMc02650 {ECO:0000312|EMBL:CAC45653.1};
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000312|Proteomes:UP000001976};
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000312|Proteomes:UP000001976};
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [3]
RP GENE NAME, AND DISRUPTION PHENOTYPE.
RC STRAIN=1021 {ECO:0000303|PubMed:16199569};
RX PubMed=16199569; DOI=10.1128/jb.187.20.6991-6997.2005;
RA Yang H.C., Cheng J., Finan T.M., Rosen B.P., Bhattacharjee H.;
RT "Novel pathway for arsenic detoxification in the legume symbiont
RT Sinorhizobium meliloti.";
RL J. Bacteriol. 187:6991-6997(2005).
RN [4] {ECO:0007744|PDB:2Q62}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=1021 {ECO:0000303|PubMed:17673204};
RX PubMed=17673204; DOI=10.1016/j.febslet.2007.07.039;
RA Ye J., Yang H.C., Rosen B.P., Bhattacharjee H.;
RT "Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti.";
RL FEBS Lett. 581:3996-4000(2007).
CC -!- FUNCTION: Has NADPH-dependent FMN reductase activity. No activity with
CC NADH. May play a role in resistance to heavy metal toxicity.
CC {ECO:0000269|PubMed:17673204}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:17673204};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for NADPH {ECO:0000269|PubMed:17673204};
CC Vmax=70 umol/min/mg enzyme {ECO:0000269|PubMed:17673204};
CC Note=Concentration of FMN required for half-maximal activation is 7.5
CC uM. {ECO:0000269|PubMed:17673204};
CC pH dependence:
CC Optimum pH is between 6.5-7.5. {ECO:0000269|PubMed:17673204};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17673204}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to low levels of AsO4(3-) and to a
CC lesser degree to As(5+). {ECO:0000269|PubMed:16199569}.
CC -!- SIMILARITY: Belongs to the ArsH family. {ECO:0000305}.
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DR EMBL; AL591688; CAC45653.1; -; Genomic_DNA.
DR RefSeq; NP_385180.1; NC_003047.1.
DR RefSeq; WP_010969023.1; NC_003047.1.
DR PDB; 2Q62; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-241.
DR PDBsum; 2Q62; -.
DR AlphaFoldDB; Q92R45; -.
DR SMR; Q92R45; -.
DR STRING; 266834.SMc02650; -.
DR EnsemblBacteria; CAC45653; CAC45653; SMc02650.
DR GeneID; 61602534; -.
DR KEGG; sme:SMc02650; -.
DR PATRIC; fig|266834.11.peg.2480; -.
DR eggNOG; COG0431; Bacteria.
DR HOGENOM; CLU_055322_0_1_5; -.
DR OMA; WSSPEMH; -.
DR EvolutionaryTrace; Q92R45; -.
DR Proteomes; UP000001976; Chromosome.
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; 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 3D-structure; Flavoprotein; FMN; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..241
FT /note="NADPH-dependent FMN reductase ArsH"
FT /id="PRO_0000432220"
FT BINDING 43..50
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9I4D4"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:2Q62"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:2Q62"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:2Q62"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:2Q62"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:2Q62"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:2Q62"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:2Q62"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 192..211
FT /evidence="ECO:0007829|PDB:2Q62"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:2Q62"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:2Q62"
SQ SEQUENCE 241 AA; 27083 MW; 3DC4F5B734A23FB3 CRC64;
MSDDDSSHDL PAANLQQLRL PDSASLRPAF STHRPRILIL YGSLRTVSYS RLLAEEARRL
LEFFGAEVKV FDPSGLPLPD AAPVSHPKVQ ELRELSIWSE GQVWVSPERH GAMTGIMKAQ
IDWIPLSTGS IRPTQGKTLA VMQVSGGSQS FNAVNQMRIL GRWMRMITIP NQSSVAKAFQ
EFDANGRMKP SSYYDRVVDV MEELVKFTLL TRDCSAYLTD RYSERKESAA ELEHRVTLKS
V
