PCEA_DEHRP
ID PCEA_DEHRP Reviewed; 551 AA.
AC Q8GJ27;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Tetrachloroethene reductive dehalogenase {ECO:0000303|PubMed:12902251};
DE EC=1.21.99.5 {ECO:0000269|PubMed:12902251, ECO:0000269|PubMed:8636034, ECO:0000269|PubMed:9224702};
DE AltName: Full=TCE reductase {ECO:0000303|PubMed:8636034};
DE AltName: Full=Tetrachloroethene reductase {ECO:0000303|PubMed:9224702};
DE Short=PCE reductase {ECO:0000303|PubMed:8636034};
DE Flags: Precursor;
GN Name=pceA {ECO:0000303|PubMed:12902251};
OS Dehalobacter restrictus (strain DSM 9455 / PER-K23).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=871738;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-59, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=DSM 9455 / PER-K23;
RX PubMed=12902251; DOI=10.1128/aem.69.8.4628-4638.2003;
RA Maillard J., Schumacher W., Vazquez F., Regeard C., Hagen W.R.,
RA Holliger C.;
RT "Characterization of the corrinoid iron-sulfur protein tetrachloroethene
RT reductive dehalogenase of Dehalobacter restrictus.";
RL Appl. Environ. Microbiol. 69:4628-4638(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8636034; DOI=10.1128/jb.178.8.2328-2333.1996;
RA Schumacher W., Holliger C.;
RT "The proton/electron ration of the menaquinone-dependent electron transport
RT from dihydrogen to tetrachloroethene in 'Dehalobacter restrictus'.";
RL J. Bacteriol. 178:2328-2333(1996).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=DSM 9455 / PER-K23;
RX PubMed=9224702; DOI=10.1016/s0014-5793(97)00520-6;
RA Schumacher W., Holliger C., Zehnder A.J., Hagen W.R.;
RT "Redox chemistry of cobalamin and iron-sulfur cofactors in the
RT tetrachloroethene reductase of Dehalobacter restrictus.";
RL FEBS Lett. 409:421-425(1997).
CC -!- FUNCTION: Catalyzes the reductive dechlorination of tetrachloroethene
CC (PCE) to trichloroethene (TCE) and of trichloroethene to cis-1,2-
CC dichloroethene (DCE) (PubMed:8636034, PubMed:12902251). Can also use
CC trichlorofluoroethene, tetrachloromethane, hexachloroethane,
CC tetrachloroethane, trichloroethane and 1,1,1-trichloro-2,2,2-
CC trifluoroethane (PubMed:12902251). Menaquinone can act as the electron
CC donor (PubMed:8636034). Reduced methyl viologen can act as the
CC artificial electron donor (PubMed:9224702, PubMed:12902251).
CC {ECO:0000269|PubMed:12902251, ECO:0000269|PubMed:8636034,
CC ECO:0000269|PubMed:9224702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + chloride + H(+) + trichloroethene = AH2 +
CC tetrachloroethene; Xref=Rhea:RHEA:20353, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16602, ChEBI:CHEBI:17300,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:17996; EC=1.21.99.5;
CC Evidence={ECO:0000269|PubMed:12902251, ECO:0000269|PubMed:8636034,
CC ECO:0000269|PubMed:9224702};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20355;
CC Evidence={ECO:0000269|PubMed:12902251, ECO:0000269|PubMed:8636034,
CC ECO:0000269|PubMed:9224702};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + trichloroethene = (Z)-1,2-dichloroethene + A + chloride
CC + H(+); Xref=Rhea:RHEA:67992, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16602, ChEBI:CHEBI:17499, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:28805; Evidence={ECO:0000269|PubMed:12902251,
CC ECO:0000269|PubMed:8636034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67993;
CC Evidence={ECO:0000269|PubMed:12902251, ECO:0000269|PubMed:8636034};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:12902251, ECO:0000269|PubMed:9224702};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:12902251,
CC ECO:0000269|PubMed:9224702};
CC -!- COFACTOR:
CC Name=corrinoid; Xref=ChEBI:CHEBI:33913;
CC Evidence={ECO:0000269|PubMed:12902251, ECO:0000269|PubMed:9224702,
CC ECO:0000305|PubMed:8636034};
CC Note=The corrinoid is probably a cobalamin.
CC {ECO:0000269|PubMed:12902251, ECO:0000269|PubMed:9224702};
CC -!- ACTIVITY REGULATION: Activity is inhibited by ammonium ions
CC (PubMed:12902251). Photoreversibly inactivated by 1-iodopropane
CC (PubMed:8636034, PubMed:12902251). {ECO:0000269|PubMed:12902251,
CC ECO:0000269|PubMed:8636034}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.4 uM for tetrachloroethene {ECO:0000269|PubMed:12902251};
CC KM=23.7 uM for trichloroethene {ECO:0000269|PubMed:12902251};
CC KM=47 uM for reduced methyl viologen {ECO:0000269|PubMed:12902251};
CC pH dependence:
CC Optimum pH is 8.1. {ECO:0000269|PubMed:12902251};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12902251}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12902251,
CC ECO:0000269|PubMed:8636034, ECO:0000269|PubMed:9224702}; Peripheral
CC membrane protein {ECO:0000269|PubMed:8636034}; Cytoplasmic side
CC {ECO:0000269|PubMed:8636034}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|PubMed:12902251}.
CC -!- SIMILARITY: Belongs to the PceA family. {ECO:0000305}.
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DR EMBL; AJ439607; CAD28790.2; -; Genomic_DNA.
DR BRENDA; 1.21.99.5; 1852.
DR GO; GO:0005886; C:plasma membrane; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR012832; RDH.
DR InterPro; IPR028894; RDH_dom.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF13486; Dehalogenase; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR TIGRFAMs; TIGR02486; RDH; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Direct protein sequencing; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Oxidoreductase; Repeat; Signal.
FT SIGNAL 1..39
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:12902251"
FT CHAIN 40..551
FT /note="Tetrachloroethene reductive dehalogenase"
FT /evidence="ECO:0000269|PubMed:12902251"
FT /id="PRO_5004306095"
FT DOMAIN 411..440
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 478..496
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000305"
FT BINDING 420
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O68252"
FT BINDING 423
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O68252"
FT BINDING 426
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O68252"
FT BINDING 430
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O68252"
FT BINDING 467
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O68252"
FT BINDING 478
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O68252"
FT BINDING 481
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O68252"
FT BINDING 485
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O68252"
SQ SEQUENCE 551 AA; 61202 MW; BFDEF455ACC75209 CRC64;
MGEINRRNFL KASMLGAAAA AVASASAVKG MVSPLVADAA DIVAPITETS EFPYKVDAKY
QRYNSLKNFF EKTFDPEANK TPIKFHYDDV SKITGKKDTG KDLPTLNAER LGIKGRPATH
TETSILFQTQ HLGAMLTQRH NETGWTGLDE ALNAGAWAVE FDYSGFNAAG GGPGSVIPLY
PINPMTNEIA NEPVMVPGLY NWDNIDVESV RQQGQQWKFE SKEEASKMVK KATRLLGADL
VGIAPYDERW TYSTWGRKIL KPCKMPNGRT KYLPWDLPKM LSGGGVEVFG HAKFEPDWEK
YAGFKPKSVI VFVLEEDYEA IRTSPSVISS ATVGKSYSNM AEVAYKIAVF LRKLGYYAAP
CGNDTGLSVP MAVQAGLGEA GRNGLLITQK FGPRHRIAKV YTDLELAPDK PRKFGVREFC
RLCKKCADAC PAQAISHEKD PKVLQPEDCE VAENPYTEKW HLDSNRCGSF WAYNGSPCAN
CVAVCSWNKV ETWNHDVARI ATQIPLLQDA ARKFDEWFGY NGPVNPDERL ESGYVQNMVK
DFWNNPESIK Q
