ARREH_SHIFL
ID ARREH_SHIFL Reviewed; 255 AA.
AC Q7UC03; E3XY12;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=NADPH-dependent FMN reductase ArsH {ECO:0000305};
DE EC=1.-.-.- {ECO:0000269|PubMed:17962405};
DE AltName: Full=Arsenical resistance operon protein ArsH {ECO:0000305, ECO:0000312|EMBL:AAP17869.1, ECO:0000312|EMBL:EFS15380.1};
GN Name=arsH {ECO:0000303|PubMed:17962405, ECO:0000312|EMBL:EFS15380.1};
GN OrderedLocusNames=S2709 {ECO:0000312|EMBL:AAP17869.1};
GN ORFNames=SF2457T_0606 {ECO:0000312|EMBL:EFS15380.1};
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a
RC {ECO:0000312|Proteomes:UP000002673};
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a {ECO:0000312|EMBL:EFS15380.1};
RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA Santana-Cruz I., Liu X.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:2FZV}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APO FORM, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a {ECO:0000303|PubMed:17962405};
RX PubMed=17962405; DOI=10.1110/ps.073029607;
RA Vorontsov I.I., Minasov G., Brunzelle J.S., Shuvalova L., Kiryukhina O.,
RA Collart F.R., Anderson W.F.;
RT "Crystal structure of an apo form of Shigella flexneri ArsH protein with an
RT NADPH-dependent FMN reductase activity.";
RL Protein Sci. 16:2483-2490(2007).
CC -!- FUNCTION: Has NADPH-dependent FMN reductase activity and very low
CC azoreductase activity. No activity with NADH.
CC {ECO:0000269|PubMed:17962405}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:17962405};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17962405}.
CC -!- SIMILARITY: Belongs to the ArsH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFS15380.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014073; AAP17869.1; -; Genomic_DNA.
DR EMBL; ADUV01000006; EFS15380.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001239389.1; NZ_QWTR01000038.1.
DR PDB; 2FZV; X-ray; 1.70 A; A/B/C/D=1-255.
DR PDBsum; 2FZV; -.
DR AlphaFoldDB; Q7UC03; -.
DR SMR; Q7UC03; -.
DR EnsemblBacteria; AAP17869; AAP17869; S2709.
DR KEGG; sfx:S2709; -.
DR PATRIC; fig|198215.9.peg.575; -.
DR HOGENOM; CLU_055322_0_1_6; -.
DR OMA; YKFTLLV; -.
DR EvolutionaryTrace; Q7UC03; -.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0050446; F:azobenzene reductase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA: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.
FT CHAIN 1..255
FT /note="NADPH-dependent FMN reductase ArsH"
FT /id="PRO_0000432221"
FT BINDING 43..50
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9I4D4"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2FZV"
FT TURN 24..28
FT /evidence="ECO:0007829|PDB:2FZV"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2FZV"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:2FZV"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:2FZV"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:2FZV"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:2FZV"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:2FZV"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:2FZV"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 193..212
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:2FZV"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:2FZV"
SQ SEQUENCE 255 AA; 28400 MW; 80740B0559A33296 CRC64;
MRLRHLSDPD SLPALDKSFA IERPALGLAP DAPPVRILLL YGSLRARSFS RLAVEEAARL
LQFFGAETRI FDPSDLPLPD QVQSDDHPAV KELRALSEWS EGQVWCSPER HGQITSVMKA
QIDHLPLEMA GIRPTQGRTL AVMQVSGGSQ SFNAVNTLRL LGRWMRMFTI PNQSSIAKAF
QEFDAAGRMK PSPYYDRIAD VMEELVRFTA LVRPHREALT DRYSERKAAG HVIDEATDLS
SIAIAPQPLP ESETS
