CLRB_IDEDE
ID CLRB_IDEDE Reviewed; 328 AA.
AC P60069;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Chlorate reductase subunit beta;
DE AltName: Full=Chlorate reductase iron-sulfur subunit;
GN Name=clrB;
OS Ideonella dechloratans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Ideonella.
OX NCBI_TaxID=36863;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=12957948; DOI=10.1128/aem.69.9.5585-5592.2003;
RA Danielsson Thorell H., Stenklo K., Karlsson J., Nilsson T.;
RT "A gene cluster for chlorate metabolism in Ideonella dechloratans.";
RL Appl. Environ. Microbiol. 69:5585-5592(2003).
CC -!- FUNCTION: Electron transfer subunit of the terminal reductase during
CC anaerobic growth on chlorate. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 3 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC -!- SUBCELLULAR LOCATION: Periplasm. Note=Probably translocated together
CC with ClrA, which possesses a Tat-type signal.
CC -!- BIOTECHNOLOGY: Has potential use in bioremediation of waste sites
CC contaminated with chlorate, such as pulp and paper industry wastewater.
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DR EMBL; AJ566363; CAD97448.1; -; Genomic_DNA.
DR RefSeq; WP_013516314.1; NZ_VZPB01000026.1.
DR AlphaFoldDB; P60069; -.
DR SMR; P60069; -.
DR TCDB; 5.A.3.8.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PRIDE; P60069; -.
DR BioCyc; MetaCyc:MON-15698; -.
DR BRENDA; 1.97.1.1; 2756.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR CDD; cd10555; EBDH_beta; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017839; DMSO_Rdtase_II_Fe-S_su.
DR Pfam; PF13247; Fer4_11; 1.
DR TIGRFAMs; TIGR03478; DMSO_red_II_bet; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Periplasm; Repeat; Transport.
FT CHAIN 1..328
FT /note="Chlorate reductase subunit beta"
FT /id="PRO_0000159291"
FT DOMAIN 6..35
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 125..156
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 158..187
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 328 AA; 37002 MW; 2E9D4B310DD520DA CRC64;
MSQRQVAYVF DLNKCIGCHT CTMACKQLWT NRDGREYMYW NNVETRPGKG YPKNWEGKGG
GFDQEGKLKT NGIIPIMADY GGRIGDFNLN EVLLEGKADQ VVPHEKATWG PNWDEDEGKG
EFPNNHSFYL PRICNHCSNP ACLAACPTKA IYKRPEDGIV VVDQTRCRGY RYCVKACPYG
KMYFNLQKGK SEKCIGCYPR VEKGEAPACV KQCSGRIRFW GYRDDKNGPI YKLVEQWKVA
LPLHAEYGTE PNVFYVPPMN TTPPPFEEDG RLGDKPRIPI EDLEALFGPG VKQALATLGG
EMAKRRKAQA SELTDILIGF TNKDRYGV
