ID   CLRC_IDEDE              Reviewed;         239 AA.
AC   P60000;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2003, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Chlorate reductase subunit gamma;
DE   AltName: Full=Chlorate reductase heme subunit;
DE   Flags: Precursor;
GN   Name=clrC;
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: May transfer electrons to the iron-sulfur centers of ClrB.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000305};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000305};
CC   -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
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; CAD97450.1; -; Genomic_DNA.
DR   AlphaFoldDB; P60000; -.
DR   SMR; P60000; -.
DR   TCDB; 5.A.3.8.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR   BioCyc; MetaCyc:MON-15699; -.
DR   BRENDA; 1.97.1.1; 2756.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd09623; DOMON_EBDH; 1.
DR   InterPro; IPR019020; Cyt-c552/DMSO_Rdtase_haem-bd.
DR   InterPro; IPR017838; DMSO_Rdtase_II_haem_b-bd_su.
DR   SMART; SM00887; EB_dh; 1.
DR   TIGRFAMs; TIGR03477; DMSO_red_II_gam; 1.
PE   1: Evidence at protein level;
KW   Electron transport; Heme; Iron; Metal-binding; Periplasm; Signal;
KW   Transport.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..239
FT                   /note="Chlorate reductase subunit gamma"
FT                   /id="PRO_0000020948"
FT   BINDING         74
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255"
FT   BINDING         138
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   239 AA;  25500 MW;  DB471B3218ACD5A6 CRC64;
     MKTNILVKRM AVIGLAVAAA CTGAAAAAQG AVPQAQRIIR VLSVAGGDAA SPQAAVWKKA
     PTTQVTLLTA FPGHISIVGT AATQKLAAQA VRASGRLFVR LAWSDRTANT VMKDTDQFLD
     GAAVEFPVNG KVATLPFMGD PVNVVNVWHW RADGRTLNLL AKGFGTSTPV PTEDLRSASV
     RTGDGWEVVL SRPLRVKAEE GANLQGRRTM PIGFAAWDGE NQERDGLKAV TMEWWQLRF