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Perchlorate reductase subunit alpha (EC 1.97.1.-) (Perchlorate reductase molybdenum subunit)

 PCRA_DECAR              Reviewed;         927 AA.
Q47CW6;
26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
13-SEP-2005, sequence version 1.
23-MAY-2018, entry version 81.
RecName: Full=Perchlorate reductase subunit alpha;
EC=1.97.1.-;
AltName: Full=Perchlorate reductase molybdenum subunit;
Flags: Precursor;
Name=pcrA; OrderedLocusNames=Daro_2584;
Dechloromonas aromatica (strain RCB).
Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
Azonexaceae; Dechloromonas.
NCBI_TaxID=159087;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RCB;
PubMed=19650930; DOI=10.1186/1471-2164-10-351;
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
Lapidus A.;
"Metabolic analysis of the soil microbe Dechloromonas aromatica str.
RCB: indications of a surprisingly complex life-style and cryptic
anaerobic pathways for aromatic degradation.";
BMC Genomics 10:351-351(2009).
[2]
IDENTIFICATION, GENE NAME, FUNCTION, ROLE IN PERCHLORATE REDUCTION,
DISRUPTION PHENOTYPE, INDUCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
BIOTECHNOLOGY.
PubMed=16030201; DOI=10.1128/JB.187.15.5090-5096.2005;
Bender K.S., Shang C., Chakraborty R., Belchik S.M., Coates J.D.,
Achenbach L.A.;
"Identification, characterization, and classification of genes
encoding perchlorate reductase.";
J. Bacteriol. 187:5090-5096(2005).
-!- FUNCTION: Component of the perchlorate reductase that catalyzes
the reduction of perchlorate to chlorite and allows anaerobic
growth on perchlorate as the sole electron acceptor. Is probably
also able to reduce chlorate to chlorite. The alpha subunit is
likely the catalytic subunit. {ECO:0000269|PubMed:16030201}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
-!- COFACTOR:
Name=Mo-bis(molybdopterin guanine dinucleotide);
Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
(Mo-bis-MGD) cofactor per subunit. {ECO:0000250};
-!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
{ECO:0000305|PubMed:16030201}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:16030201}.
-!- INDUCTION: Transcription of pcrA occurs only under anaerobic
(per)chlorate-reducing conditions. The presence of oxygen
completely inhibits pcrA expression regardless of the presence of
perchlorate, chlorate, or nitrate. {ECO:0000269|PubMed:16030201}.
-!- PTM: Predicted to be exported by the Tat system. The position of
the signal peptide cleavage has not been experimentally proven.
-!- DISRUPTION PHENOTYPE: Deletion of the pcrA gene abolishes
anaerobic growth in both perchlorate and chlorate but not in
nitrate, indicating that the pcrABCD genes play a functional role
in perchlorate reduction separate from nitrate reduction. Deletion
mutant strains are still able to grow aerobically.
{ECO:0000269|PubMed:16030201}.
-!- BIOTECHNOLOGY: Has potential use in bioremediation of waste sites
contaminated with perchlorate, a common component of solid rocket
fuel which is a widespread environmental contaminant in water
systems in the United States. {ECO:0000269|PubMed:16030201}.
-!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
oxidoreductase family. {ECO:0000305}.
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EMBL; CP000089; AAZ47315.1; -; Genomic_DNA.
RefSeq; WP_011288314.1; NC_007298.1.
ProteinModelPortal; Q47CW6; -.
SMR; Q47CW6; -.
STRING; 159087.Daro_2584; -.
PRIDE; Q47CW6; -.
EnsemblBacteria; AAZ47315; AAZ47315; Daro_2584.
KEGG; dar:Daro_2584; -.
eggNOG; ENOG4108JIG; Bacteria.
eggNOG; COG0243; LUCA.
HOGENOM; HOG000237342; -.
KO; K17050; -.
OMA; QGTDSAM; -.
OrthoDB; POG091H0DLT; -.
BioCyc; DARO159087:G1G4R-2667-MONOMER; -.
Proteomes; UP000000550; Chromosome.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
InterPro; IPR006657; MoPterin_dinucl-bd_dom.
InterPro; IPR006656; Mopterin_OxRdtase.
InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
InterPro; IPR006311; TAT_signal.
Pfam; PF00384; Molybdopterin; 1.
Pfam; PF01568; Molydop_binding; 1.
SUPFAM; SSF50692; SSF50692; 1.
TIGRFAMs; TIGR03479; DMSO_red_II_alp; 1.
PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
Molybdenum; Oxidoreductase; Periplasm; Reference proteome; Signal.
SIGNAL 1 31 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648}.
CHAIN 32 927 Perchlorate reductase subunit alpha.
/FTId=PRO_5000100109.
DOMAIN 53 116 4Fe-4S Mo/W bis-MGD-type.
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 60 60 Iron-sulfur (4Fe-4S); via pros nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 64 64 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 68 68 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 102 102 Iron-sulfur (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 198 198 Molybdenum. {ECO:0000250}.
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


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