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PCRB_DECAR
ID   PCRB_DECAR              Reviewed;         333 AA.
AC   Q47CW7;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Perchlorate reductase subunit beta;
DE   AltName: Full=Perchlorate reductase iron-sulfur subunit;
GN   Name=pcrB; OrderedLocusNames=Daro_2583;
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 beta subunit may be
CC       responsible for electron transfer to the catalytic alpha subunit PcrA
CC       (Probable). {ECO:0000305|PubMed:16030201}.
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       {ECO:0000305|PubMed:16030201}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:16030201}.
CC       Note=Probably translocated together with PcrA, which possesses a Tat-
CC       type signal.
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; AAZ47314.1; -; Genomic_DNA.
DR   RefSeq; WP_011288313.1; NC_007298.1.
DR   AlphaFoldDB; Q47CW7; -.
DR   SMR; Q47CW7; -.
DR   STRING; 159087.Daro_2583; -.
DR   EnsemblBacteria; AAZ47314; AAZ47314; Daro_2583.
DR   KEGG; dar:Daro_2583; -.
DR   eggNOG; COG1140; Bacteria.
DR   HOGENOM; CLU_043374_5_2_4; -.
DR   OMA; NHCTHPS; -.
DR   OrthoDB; 1762646at2; -.
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..333
FT                   /note="Perchlorate reductase subunit beta"
FT                   /id="PRO_0000422921"
FT   DOMAIN          12..40
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          128..159
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          161..190
FT                   /note="4Fe-4S ferredoxin-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   REGION          101..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         21
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
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         140
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
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         200
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  37099 MW;  8BEA9A7ACC8219B9 CRC64;
     MANVMKAPKR QLTYVTDLNK CIGCQTCTVA CKKLWTTGPG QDFMYWRNVE TTPGLGYPRN
     WQTKGGGYKN GELQKGKIPP MIDYGIPFEF DYAGRLFEGK KERVRPSPTP RSAPNWDEDQ
     GAGEYPNNSF FYLPRMCNHC TKPACLEACP NEAIYKREQD GIVVIHQDKC KGAQACVQSC
     PYAKPYFNPV ANKANKCIGC FPRIEQGVAP GCVAQCVGRA MHVGFIDDTN SSVHKLIRLY
     KVALPLHPEF GTEPNVFYVP PVLGPRMELP NGELSTDPKI PLAQLEGLFG KQVRDVLAIL
     QTEREKKMKG LASDLMDVLI GRRSADMMIS PLT
 
 
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