PCEA_DESHA
ID PCEA_DESHA Reviewed; 551 AA.
AC Q848J2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Tetrachloroethene reductive dehalogenase {ECO:0000303|PubMed:9575235};
DE EC=1.21.99.5 {ECO:0000269|PubMed:9575235};
DE Flags: Precursor;
GN Name=pceA {ECO:0000303|Ref.1};
OS Desulfitobacterium hafniense (Desulfitobacterium frappieri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=49338;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCE-S;
RA Neumann A., Reinhardt S., Diekert G.;
RT "Tetrachloroethene reductive dehalogenase operon from Desulfitobacterium
RT strain PCE-S.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 40-60, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=PCE-S;
RX PubMed=9575235; DOI=10.1007/s002030050602;
RA Miller E., Wohlfarth G., Diekert G.;
RT "Purification and characterization of the tetrachloroethene reductive
RT dehalogenase of strain PCE-S.";
RL Arch. Microbiol. 169:497-502(1998).
CC -!- FUNCTION: Catalyzes the reductive dechlorination of tetrachloroethene
CC (PCE) to trichloroethene (TCE) and of trichloroethene to cis-1,2-
CC dichloroethene (DCE) (PubMed:9575235). Reduced methyl viologen can act
CC as the artificial electron donor (PubMed:9575235).
CC {ECO:0000269|PubMed:9575235}.
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:9575235};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20355;
CC Evidence={ECO:0000269|PubMed:9575235};
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:9575235};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67993;
CC Evidence={ECO:0000269|PubMed:9575235};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:9575235};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:9575235};
CC -!- COFACTOR:
CC Name=corrinoid; Xref=ChEBI:CHEBI:33913;
CC Evidence={ECO:0000269|PubMed:9575235};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for tetrachloroethene (with reduced methyl viologen as
CC electron donor) {ECO:0000269|PubMed:9575235};
CC KM=4 uM for trichloroethene (with reduced methyl viologen as electron
CC donor) {ECO:0000269|PubMed:9575235};
CC KM=0.3 mM for methyl viologen {ECO:0000269|PubMed:9575235};
CC pH dependence:
CC Optimum pH is about 7.2. {ECO:0000269|PubMed:9575235};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:9575235};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9575235};
CC Peripheral membrane protein {ECO:0000269|PubMed:9575235}.
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:9575235}.
CC -!- SIMILARITY: Belongs to the PceA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY216592; AAO60101.1; -; Genomic_DNA.
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:9575235"
FT CHAIN 40..551
FT /note="Tetrachloroethene reductive dehalogenase"
FT /evidence="ECO:0000269|PubMed:9575235"
FT /id="PRO_5004299602"
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"
FT CONFLICT 59
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305|PubMed:9575235"
SQ SEQUENCE 551 AA; 61241 MW; 11E6FBC92727A3DA CRC64;
MGEINRRNFL KASMLGAAAA AVASASVVKG VVSPLVADAA DIVAPITETS EFPYKVDAKY
QRYNSLKNFF EKTFDPEENK TPIKFHYDDV SKITGKKDTG KDLPMLNAER LGIKGRPATH
TETSILFHTQ HLGAMLTQRH NETGWTGLDE ALNAGAWAVE FDYSGFNAAG GGPGSAIPLY
PINPMTNEIA NEPVMVPGLY NWDNIDVESV RQQGQQWKFE SKEEASKILK KATRLLGADL
VGIAPYDERW TYSTWGRKIQ KPCKMPNGRT KYLPWDLPKM LSGGGVEVFG HAKFEPDWEK
YAGFKPKSVI VFVLEEDYEA IRTSPSVISS ATVGKSYSNM AEVAYKIAVF LRKLGYYAAP
CGNDTGISVP MAVQAGLGEA GRNGLLITQK FGPRHRIAKV YTDLELAPDK PRKFGVREFC
RLCKKCADAC PAQAISHEKD PKVLQPEDCE ASENPYTEKW HVDSERCGSF WAYNGSPCSN
CVAVCSWNKV ETWNHDVARV ATQIPLLQDA ARKFDEWFGY SGPVNPDERL ESGYVQNMVK
DFWNNPESIK Q
