PCRC_DECAR
ID PCRC_DECAR Reviewed; 236 AA.
AC Q47CW8;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Perchlorate reductase subunit gamma;
DE AltName: Full=Perchlorate reductase heme subunit;
DE Flags: Precursor;
GN Name=pcrC; OrderedLocusNames=Daro_2582;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
RN [2]
RP IDENTIFICATION, GENE NAME, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP BIOTECHNOLOGY.
RX PubMed=16030201; DOI=10.1128/jb.187.15.5090-5096.2005;
RA Bender K.S., Shang C., Chakraborty R., Belchik S.M., Coates J.D.,
RA Achenbach L.A.;
RT "Identification, characterization, and classification of genes encoding
RT perchlorate reductase.";
RL J. Bacteriol. 187:5090-5096(2005).
CC -!- FUNCTION: Component of the perchlorate reductase that catalyzes the
CC reduction of perchlorate to chlorite and allows anaerobic growth on
CC perchlorate as the sole electron acceptor. The gamma subunit may be
CC responsible for electron transfer to the beta subunit PcrB (Probable).
CC {ECO:0000305|PubMed:16030201}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 4 heme groups per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC {ECO:0000305|PubMed:16030201}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:16030201}.
CC -!- BIOTECHNOLOGY: Has potential use in bioremediation of waste sites
CC contaminated with perchlorate, a common component of solid rocket fuel
CC which is a widespread environmental contaminant in water systems in the
CC United States. {ECO:0000269|PubMed:16030201}.
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DR EMBL; CP000089; AAZ47313.1; -; Genomic_DNA.
DR RefSeq; WP_011288312.1; NC_007298.1.
DR AlphaFoldDB; Q47CW8; -.
DR SMR; Q47CW8; -.
DR STRING; 159087.Daro_2582; -.
DR EnsemblBacteria; AAZ47313; AAZ47313; Daro_2582.
DR KEGG; dar:Daro_2582; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_1179215_0_0_4; -.
DR OMA; HYKLEGV; -.
DR OrthoDB; 1643231at2; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR023155; Cyt_c-552/4.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF13435; Cytochrome_C554; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW Electron transport; Heme; Iron; Metal-binding; Periplasm; Signal;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..236
FT /note="Perchlorate reductase subunit gamma"
FT /id="PRO_5000100108"
FT BINDING 33
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 236 AA; 25466 MW; 454C167B4E801B8C CRC64;
MIKILALATL LISGFLPGVT VAQQAEYLGF RACTKCHDSQ GETWRASAHA KAFDSLKPNA
KSEAKTKAKL DPKKDYTQDK NCVGCHVTGY GEPGGFVSGA SLDDMKTLVG VTCESCHGAG
GKFRNLHGEA SDRLKNQGET SERKQLVTAG QNFDMEKACA RCHLNFEGST KHDAKAPFTP
FSPSVGSKYQ FDFQKSVMTT GAGNPIHTHF KLRGVFKGDP VPAVRAKLQE DAPEPE
