ARRB_SHESA
ID ARRB_SHESA Reviewed; 234 AA.
AC Q7WTT9;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Arsenate respiratory reductase iron-sulfur subunit ArrB {ECO:0000305};
DE AltName: Full=Arsenate respiratory reductase small subunit {ECO:0000305};
DE Short=ARR small subunit {ECO:0000305};
GN Name=arrB {ECO:0000303|PubMed:12939408};
GN OrderedLocusNames=Shewana3_2340 {ECO:0000312|EMBL:ABK48569.1};
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, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
RP 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) IN COMPLEXES WITH ARRA; IRON-SULFUR
RP (4FE-4S); MOLYBDENUM ION; MOLYBDOPTERIN; ARSENITE AND ARSENATE, FUNCTION,
RP COFACTOR, ACTIVITY REGULATION, 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). ArrB is
CC probably the electron transfer subunit (PubMed:30104376). The
CC periplasmic localization of this complex may allow the cell to couple
CC arsenate reduction to energy production before arsenate can be
CC transported to the cell cytoplasm and enter the ars detoxification
CC pathway, an energy-requiring process (PubMed:17951391).
CC {ECO:0000269|PubMed:12939408, ECO:0000269|PubMed:17951391,
CC 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 4 [4Fe-4S] cluster. {ECO:0000269|PubMed:30104376};
CC -!- ACTIVITY REGULATION: Phosphate is a competitive inhibitor.
CC {ECO:0000269|PubMed:30104376}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
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 -!- 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}.
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DR EMBL; AY271310; AAQ01673.1; -; Genomic_DNA.
DR EMBL; CP000469; ABK48569.1; -; Genomic_DNA.
DR RefSeq; WP_011717271.1; NC_008577.1.
DR PDB; 6CZ7; X-ray; 1.62 A; B/D=1-234.
DR PDB; 6CZ8; X-ray; 1.78 A; B/D=1-234.
DR PDB; 6CZ9; X-ray; 1.80 A; B/D=1-234.
DR PDB; 6CZA; X-ray; 1.71 A; B/D=1-234.
DR PDBsum; 6CZ7; -.
DR PDBsum; 6CZ8; -.
DR PDBsum; 6CZ9; -.
DR PDBsum; 6CZA; -.
DR SMR; Q7WTT9; -.
DR STRING; 94122.Shewana3_2340; -.
DR EnsemblBacteria; ABK48569; ABK48569; Shewana3_2340.
DR GeneID; 45044327; -.
DR KEGG; shn:Shewana3_2340; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_1_0_6; -.
DR OMA; CENTPCL; -.
DR OrthoDB; 1762646at2; -.
DR BioCyc; MetaCyc:MON-10762; -.
DR Proteomes; UP000002589; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF13247; Fer4_11; 2.
DR Pfam; PF12800; Fer4_4; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Periplasm; Repeat; Transport.
FT CHAIN 1..234
FT /note="Arsenate respiratory reductase iron-sulfur subunit
FT ArrB"
FT /id="PRO_0000456241"
FT DOMAIN 3..32
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 48..79
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 80..109
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
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 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
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 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
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 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
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 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
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 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
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 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
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 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
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 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
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 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
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 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
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 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
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 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
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 167
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
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 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
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 183
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:30104376,
FT ECO:0007744|PDB:6CZ7, ECO:0007744|PDB:6CZ8,
FT ECO:0007744|PDB:6CZ9, ECO:0007744|PDB:6CZA"
SQ SEQUENCE 234 AA; 25733 MW; 8B06F21ACED61D04 CRC64;
MRLGMVIDLQ KCVGCGGCSL ACKTENNTND GIHWSHHIAT TEGTFPDVKY TYIPTLCNHC
DDAPCVKVCP TGAMHKDKRG LTLQNNDECI GCKKCMNACP YGVISFNAAT PHRRWQDDSE
VVANGTVSPL MLLKRTGATA TPNENPERGD TYPMIRPKRT TEKCTFCDHR LDKGLNPACV
DACPSEARVI GDLDDPQSKV SQLIKLHKPM QLKPEAGTGP RVFYIRSFGV KTAY
