ARRA_SHESA
ID ARRA_SHESA Reviewed; 854 AA.
AC Q7WTU0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Arsenate respiratory reductase molybdopterin-containing subunit ArrA {ECO:0000305};
DE EC=1.20.99.1 {ECO:0000269|PubMed:17951391};
DE AltName: Full=Arsenate respiratory reductase large subunit {ECO:0000305};
DE Short=ARR large subunit {ECO:0000305};
DE Flags: Precursor;
GN Name=arrA {ECO:0000303|PubMed:12939408};
GN OrderedLocusNames=Shewana3_2341 {ECO:0000312|EMBL:ABK48570.1};
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ANA-3;
RX PubMed=12939408; DOI=10.1073/pnas.1834303100;
RA Saltikov C.W., Newman D.K.;
RT "Genetic identification of a respiratory arsenate reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10983-10988(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION.
RC STRAIN=ANA-3;
RX PubMed=16237022; DOI=10.1128/jb.187.21.7390-7396.2005;
RA Saltikov C.W., Wildman R.A. Jr., Newman D.K.;
RT "Expression dynamics of arsenic respiration and detoxification in
RT Shewanella sp. strain ANA-3.";
RL J. Bacteriol. 187:7390-7396(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ANA-3;
RX PubMed=17951391; DOI=10.1128/jb.01110-07;
RA Malasarn D., Keeffe J.R., Newman D.K.;
RT "Characterization of the arsenate respiratory reductase from Shewanella sp.
RT strain ANA-3.";
RL J. Bacteriol. 190:135-142(2008).
RN [5] {ECO:0007744|PDB:6CZ7, ECO:0007744|PDB:6CZ8, ECO:0007744|PDB:6CZ9, ECO:0007744|PDB:6CZA}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 42-854 IN COMPLEXES WITH ARRB;
RP IRON-SULFUR (4FE-4S); MOLYBDENUM ION; MOLYBDOPTERIN; ARSENITE AND ARSENATE,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=30104376; DOI=10.1073/pnas.1807984115;
RA Glasser N.R., Oyala P.H., Osborne T.H., Santini J.M., Newman D.K.;
RT "Structural and mechanistic analysis of the arsenate respiratory reductase
RT provides insight into environmental arsenic transformations.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E8614-E8623(2018).
CC -!- FUNCTION: Component of the arsenate respiratory reductase (Arr)
CC complex, which catalyzes the reduction of arsenate (As(V)) to arsenite
CC (As(III)) (PubMed:12939408, PubMed:17951391, PubMed:30104376). ArrA is
CC the arsenate-binding subunit (PubMed:30104376). The periplasmic
CC localization of this complex may allow the cell to couple arsenate
CC reduction to energy production before arsenate can be transported to
CC the cell cytoplasm and enter the ars detoxification pathway, an energy-
CC requiring process (PubMed:17951391). {ECO:0000269|PubMed:12939408,
CC ECO:0000269|PubMed:17951391, ECO:0000269|PubMed:30104376}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + arsenite + H2O = AH2 + arsenate + H(+);
CC Xref=Rhea:RHEA:18449, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29242,
CC ChEBI:CHEBI:48597; EC=1.20.99.1;
CC Evidence={ECO:0000269|PubMed:17951391, ECO:0000269|PubMed:30104376};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:30104376, ECO:0000305|PubMed:17951391};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:30104376};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Evidence={ECO:0000269|PubMed:17951391, ECO:0000269|PubMed:30104376};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:30104376};
CC -!- ACTIVITY REGULATION: Phosphate is a competitive inhibitor.
CC {ECO:0000269|PubMed:30104376}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for arsenate {ECO:0000269|PubMed:17951391};
CC KM=44.6 uM for arsenate {ECO:0000269|PubMed:30104376};
CC Vmax=11111 umol/min/mg enzyme {ECO:0000269|PubMed:17951391};
CC Note=kcat is 9810 sec(-1). {ECO:0000269|PubMed:30104376};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:30104376};
CC -!- SUBUNIT: Heterodimer composed of one large subunit (ArrA) and one small
CC subunit (ArrB). {ECO:0000269|PubMed:17951391,
CC ECO:0000269|PubMed:30104376}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:17951391}.
CC -!- INDUCTION: The arrA-arrB operon is induced under anaerobic conditions
CC in the presence of nanomolar concentrations of arsenite or low
CC micromolar concentrations of arsenate (PubMed:16237022). Expression is
CC repressed under aerobic conditions and in the presence of nitrate
CC (PubMed:16237022). The peak of expression occurs during the exponential
CC phase of growth (PubMed:16237022). {ECO:0000269|PubMed:16237022}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants are incapable of growing on
CC arsenate, but are still able to grow on a wide variety of other
CC electron acceptors as efficiently as the wild-type.
CC {ECO:0000269|PubMed:12939408}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AY271310; AAQ01672.1; -; Genomic_DNA.
DR EMBL; CP000469; ABK48570.1; -; Genomic_DNA.
DR RefSeq; WP_011717272.1; NC_008577.1.
DR PDB; 6CZ7; X-ray; 1.62 A; A/C=42-854.
DR PDB; 6CZ8; X-ray; 1.78 A; A/C=42-854.
DR PDB; 6CZ9; X-ray; 1.80 A; A/C=42-854.
DR PDB; 6CZA; X-ray; 1.71 A; A/C=42-854.
DR PDBsum; 6CZ7; -.
DR PDBsum; 6CZ8; -.
DR PDBsum; 6CZ9; -.
DR PDBsum; 6CZA; -.
DR SMR; Q7WTU0; -.
DR STRING; 94122.Shewana3_2341; -.
DR EnsemblBacteria; ABK48570; ABK48570; Shewana3_2341.
DR GeneID; 45044328; -.
DR KEGG; shn:Shewana3_2341; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; ISHSSIC; -.
DR OrthoDB; 88184at2; -.
DR BioCyc; MetaCyc:MON-10761; -.
DR Proteomes; UP000002589; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037946; MopB_CT_Tetrathionate.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..41
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 42..854
FT /note="Arsenate respiratory reductase molybdopterin-
FT containing subunit ArrA"
FT /id="PRO_0000456239"
FT DOMAIN 54..110
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ7, ECO:0007744|PDB:6CZ8,
FT ECO:0007744|PDB:6CZ9, ECO:0007744|PDB:6CZA"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ7, ECO:0007744|PDB:6CZ8,
FT ECO:0007744|PDB:6CZ9, ECO:0007744|PDB:6CZA"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ7, ECO:0007744|PDB:6CZ8,
FT ECO:0007744|PDB:6CZ9, ECO:0007744|PDB:6CZA"
FT BINDING 96
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ7, ECO:0007744|PDB:6CZ8,
FT ECO:0007744|PDB:6CZ9, ECO:0007744|PDB:6CZA"
FT BINDING 165
FT /ligand="arsenite"
FT /ligand_id="ChEBI:CHEBI:29242"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ9"
FT BINDING 166
FT /ligand="arsenate"
FT /ligand_id="ChEBI:CHEBI:48597"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ8"
FT BINDING 189
FT /ligand="arsenite"
FT /ligand_id="ChEBI:CHEBI:29242"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ9"
FT BINDING 190
FT /ligand="arsenate"
FT /ligand_id="ChEBI:CHEBI:48597"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ8"
FT BINDING 193
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ7, ECO:0007744|PDB:6CZ8,
FT ECO:0007744|PDB:6CZ9, ECO:0007744|PDB:6CZA"
FT BINDING 198
FT /ligand="arsenate"
FT /ligand_id="ChEBI:CHEBI:48597"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ8"
FT BINDING 210
FT /ligand="arsenite"
FT /ligand_id="ChEBI:CHEBI:29242"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ9"
SQ SEQUENCE 854 AA; 95212 MW; 69BB6A033C81F004 CRC64;
MKKENQVNLG RRQLLKSTAA GTVLTGIGGT LSFTPIVEGI AAELPAPLRR TGVGEWLATT
CQGCTSWCAK QIYVMDGRAL KVRGNPNSGV HGMSSCPRQH LSLQQVYDPD RLRTPMMRTN
PKKGRDQDPK FVPISWDKAL DMLADKIIAL RVANEPHKYA LLRGRYSHIN DLLYKKMTNL
IGSPNNISHS SVCAEAHKMG PYYLDGNWGY NQYDVKNAKF ILSFGADPIA SNRQVSFYSQ
TWGDSLDHAK VVVVDPRLSA SAAKAHKWIP IEPGQDSVLA LAIAHVALVE GVWHKPFVGD
FIEGKNLFKA GKTVSVESFK ETHTYGLVEW WNQALKDYTP EWASKITGID PKTIIAIAKD
MGAAAPAVQV WTSRGAVMQA RGTYTSISCH ALNGLFGGID SKGGLFPGNK TPLLKEYPEA
KAYMDEIAAK GVKKEKIDQR GRLEFPALAK GKSGGGVITA NAANGIRNQD PYEIKVMLAY
FNNFNFSNPE GQRWDEALSK VDFMAHITTN VSEFSWFADV LLPSSHHMFE KWGVLDSIGN
GVAQISIQQP SIKRLWDTRI DESEIPYMLA KKLADKGFDA PWRYINEQIV DPETGKPAAD
EAEFAKLMVR YLTAPLWKED ASKYGDKLSS WDEFVQKGVW NSSPYKLEAR WGKFKTETTK
FEFYSKTLEK ALQSHADKHK VSIDEVMKAC DYQARGHLAF IPHYEEPYRF GDESEFPLLL
VDQKSRLNKE GRTANSPWYY EFKDVDPGDV ANEDVAKFNP IDGKKFGLKD GDEIRITSPV
GMLTCKAKLW EGVRPGTVAK CFGQGHWAYG RYASAKFGVT PRGGSNNDLI ADRYDRLSGA
SAFYGHIRVR VEKV
