PCRA_DECAR
ID PCRA_DECAR Reviewed; 927 AA.
AC Q47CW6;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Perchlorate reductase subunit alpha;
DE EC=1.97.1.-;
DE AltName: Full=Perchlorate reductase molybdenum subunit;
DE Flags: Precursor;
GN Name=pcrA; OrderedLocusNames=Daro_2584;
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, ROLE IN PERCHLORATE REDUCTION,
RP DISRUPTION PHENOTYPE, INDUCTION, 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. Is probably also able to
CC reduce chlorate to chlorite. The alpha subunit is likely the catalytic
CC subunit. {ECO:0000269|PubMed:16030201}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor 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 -!- INDUCTION: Transcription of pcrA occurs only under anaerobic
CC (per)chlorate-reducing conditions. The presence of oxygen completely
CC inhibits pcrA expression regardless of the presence of perchlorate,
CC chlorate, or nitrate. {ECO:0000269|PubMed:16030201}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- DISRUPTION PHENOTYPE: Deletion of the pcrA gene abolishes anaerobic
CC growth in both perchlorate and chlorate but not in nitrate, indicating
CC that the pcrABCD genes play a functional role in perchlorate reduction
CC separate from nitrate reduction. Deletion mutant strains are still able
CC to grow aerobically. {ECO:0000269|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}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; CP000089; AAZ47315.1; -; Genomic_DNA.
DR RefSeq; WP_011288314.1; NC_007298.1.
DR AlphaFoldDB; Q47CW6; -.
DR SMR; Q47CW6; -.
DR STRING; 159087.Daro_2584; -.
DR EnsemblBacteria; AAZ47315; AAZ47315; Daro_2584.
DR KEGG; dar:Daro_2584; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_13_3_4; -.
DR OMA; GGHHNSV; -.
DR OrthoDB; 88184at2; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
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 SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR03479; DMSO_red_II_alp; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW Periplasm; Signal.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 32..927
FT /note="Perchlorate reductase subunit alpha"
FT /id="PRO_5000100109"
FT DOMAIN 53..116
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 198
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:0000250"
SQ SEQUENCE 927 AA; 104799 MW; 0FCA68F7B43E0562 CRC64;
MVQMTRRGFL LASGATLLGS SLSFRTLAAA ADLSGAFEYS GWENFHRAQW SWDKKTRGAH
LINCTGACPH FVYSKEGVVI REEQSKDIAP MTGIPEYNPR GCNKGECAHD YMYGPHRLKY
PLIRVGERGE GKWRRASWDE ALDMIADKVV DTIKNHAPDC ISVYSPVPAV APVSFSAGHR
FAHYIGAHTH TFFDWYGDHP TGQTQTCGVQ GDTAETADWF NSKYIILWGA NPTQTRIPDA
HFLSEAQLNG TKIVSIAPDF NSSAIKVDKW IHPQPGTDGA LALSMAHVII KEKLYDAHNL
KEQTDLSYLV RSDTKRFLRE ADVVAGGSKD KFYLWDVRTG KPVIPKGCWG DQPEQKAPPV
AFMGRNTNTF PKGYIDLGDI DPALEGKFKI QLLDGKSIEV RPVFEILKSR IMADNTPEKA
AKITGVPAKS ITELAREYAT AKPSMIICGG GTQHWYYSDV LLRAMHLLTA LTGSEGKNGG
GLNHYIGQWK PTFLPGLVAL AFPEGPAKQR FCQTTIWTYI HAEVNDQILN SDVDTEKYLR
EAFASRQMPN LPRDGRDPKV FIIYRGNWLN QAKGQKYVLR NLWPKLELVV DINIRMDSTA
LYSDVVLPSA HWYEKLDLNV TEEHTFINMT EPAIKPMWES KTDWQIFLAL SKRVEMAANR
KGYQKFNDEQ FKWVRNLSNL WNQMTMDGKL AEDAAAAQYI LDNAPHSKGI TLDMLREKPQ
RFKANWTSSM KEGVPYTPFQ NFVVDKKPWP TLTGRQQFYL DHETFFDMGV ELPVYKAPID
ADKYPFRFNS PHSRHSIHST FKDSVLMLRL QRGGPSIDIS SIDAKTLGIK DNDWVEVWND
HGKVICRVKI RSGEQRGRVS MWHTPELYMD LIEGGSQSVC PVRITPTHLV GNYGHLVFRP
NYYGPGGTQR DVRVNMKRYI GATPMSF
