TCEA_DEHM1
ID TCEA_DEHM1 Reviewed; 554 AA.
AC Q3ZAB8; Q9KIP5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Trichloroethene reductive dehalogenase {ECO:0000303|PubMed:10671186};
DE Short=TCE-RDase {ECO:0000303|PubMed:10671186};
DE Short=TCE-reductive dehalogenase {ECO:0000303|PubMed:10671186};
DE EC=1.21.99.- {ECO:0000269|PubMed:10671186, ECO:0000269|PubMed:11097881};
DE Flags: Precursor;
GN Name=tceA {ECO:0000303|PubMed:11097881};
GN OrderedLocusNames=DET0079 {ECO:0000312|EMBL:AAW39060.1};
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 43-69 AND 215-232,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=11097881; DOI=10.1128/aem.66.12.5141-5147.2000;
RA Magnuson J.K., Romine M.F., Burris D.R., Kingsley M.T.;
RT "Trichloroethene reductive dehalogenase from Dehalococcoides ethenogenes:
RT sequence of tceA and substrate range characterization.";
RL Appl. Environ. Microbiol. 66:5141-5147(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=10671186; DOI=10.1128/aem.64.4.1270-1275.1998;
RA Magnuson J.K., Stern R.V., Gossett J.M., Zinder S.H., Burris D.R.;
RT "Reductive dechlorination of tetrachloroethene to ethene by a two-component
RT enzyme pathway.";
RL Appl. Environ. Microbiol. 64:1270-1275(1998).
CC -!- FUNCTION: Catalyzes the reductive dechlorination of trichloroethene
CC (TCE) to cis-1,2-dichloroethene (DCE) and of cis-1,2-dichloroethene to
CC chloroethene (PubMed:10671186, PubMed:11097881). The substrate
CC specificity is broad, and the enzyme can dehalogenate various
CC substrates, including 1,1-dichloroethene (1,1-DCE), 1,2-dichloroethane
CC and 1,2-dibromoethane (PubMed:10671186, PubMed:11097881). A variety of
CC other haloalkanes and haloalkenes containing three to five carbon atoms
CC are dehalogenated at lower rates (PubMed:11097881). Trans-1,2-
CC dichloroethene (trans-DCE) and chloroethene are degraded at rates which
CC are approximately 2 orders of magnitude lower (PubMed:10671186,
CC PubMed:11097881). Titanium(III) citrate and methyl viologen can be used
CC as reductants (PubMed:10671186, PubMed:11097881).
CC {ECO:0000269|PubMed:10671186, ECO:0000269|PubMed:11097881}.
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:10671186,
CC ECO:0000269|PubMed:11097881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67993;
CC Evidence={ECO:0000269|PubMed:10671186, ECO:0000269|PubMed:11097881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-1,2-dichloroethene + AH2 = A + chloride + chloroethene +
CC H(+); Xref=Rhea:RHEA:67996, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:17996, ChEBI:CHEBI:28509,
CC ChEBI:CHEBI:28805; Evidence={ECO:0000269|PubMed:10671186,
CC ECO:0000269|PubMed:11097881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67997;
CC Evidence={ECO:0000269|PubMed:10671186, ECO:0000269|PubMed:11097881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,1-dichloroethene + AH2 = A + chloride + chloroethene + H(+);
CC Xref=Rhea:RHEA:68000, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:17996, ChEBI:CHEBI:28509,
CC ChEBI:CHEBI:34031; Evidence={ECO:0000269|PubMed:10671186,
CC ECO:0000269|PubMed:11097881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68001;
CC Evidence={ECO:0000269|PubMed:10671186, ECO:0000269|PubMed:11097881};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000255|PROSITE-ProRule:PRU00711};
CC -!- COFACTOR:
CC Name=corrinoid; Xref=ChEBI:CHEBI:33913;
CC Evidence={ECO:0000269|PubMed:10671186};
CC -!- ACTIVITY REGULATION: Loses 93% of its activity upon incubation with 1-
CC iodopropane and titanium(III) citrate in the dark. Subsequent exposure
CC to light restores 80% of the original activity (PubMed:10671186).
CC Completely inhibited by 2 mM sodium sulfite or sodium dithionite, and
CC by 1 mM cuprous chloride (PubMed:10671186).
CC {ECO:0000269|PubMed:10671186}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10671186,
CC ECO:0000269|PubMed:11097881}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11097881}; Extracellular side
CC {ECO:0000305|PubMed:11097881}. Note=Membrane-bound.
CC {ECO:0000269|PubMed:10671186}.
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:11097881}.
CC -!- SIMILARITY: Belongs to the PceA family. {ECO:0000305}.
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DR EMBL; AF228507; AAF73916.1; -; Genomic_DNA.
DR EMBL; CP000027; AAW39060.1; -; Genomic_DNA.
DR RefSeq; WP_010935886.1; NC_002936.3.
DR SMR; Q3ZAB8; -.
DR STRING; 243164.DET0079; -.
DR EnsemblBacteria; AAW39060; AAW39060; DET0079.
DR KEGG; det:DET0079; -.
DR PATRIC; fig|243164.10.peg.72; -.
DR eggNOG; COG2768; Bacteria.
DR HOGENOM; CLU_036586_0_1_0; -.
DR OMA; KCESIFT; -.
DR OrthoDB; 323168at2; -.
DR Proteomes; UP000008289; Chromosome.
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 TIGRFAMs; TIGR02486; RDH; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
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; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..42
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:11097881"
FT CHAIN 43..554
FT /note="Trichloroethene reductive dehalogenase"
FT /evidence="ECO:0000269|PubMed:11097881"
FT /id="PRO_0000454140"
FT DOMAIN 425..457
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 471..500
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 437
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 440
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 443
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 447
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 480
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 483
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 486
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 490
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT CONFLICT 261
FT /note="V -> A (in Ref. 1; AAF73916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 62156 MW; 4AD0110420048EA2 CRC64;
MSEKYHSTVT RRDFMKRLGL AGAGAGALGA AVLAENNLPH EFKDVDDLLS AGKALEGDHA
NKVNNHPWWV TTRDHEDPTC NIDWSLIKRY SGWNNQGAYF LPEDYLSPTY TGRRHTIVDS
KLEIELQGKK YRDSAFIKSG IDWMKENIDP DYDPGELGYG DRREDALIYA ATNGSHNCWE
NPLYGRYEGS RPYLSMRTMN GINGLHEFGH ADIKTTNYPK WEGTPEENLL IMRTAARYFG
ASSVGAIKIT DNVKKIFYAK VQPFCLGPWY TITNMAEYIE YPVPVDNYAI PIVFEDIPAD
QGHYSYKRFG GDDKIAVPNA LDNIFTYTIM LPEKRFKYAH SIPMDPCSCI AYPLFTEVEA
RIQQFIAGLG YNSMGGGVEA WGPGSAFGNL SGLGEQSRVS SIIEPRYGSN TKGSLRMLTD
LPLAPTKPID AGIREFCKTC GICAEHCPTQ AISHEGPRYD SPHWDCVSGY EGWHLDYHKC
INCTICEAVC PFFTMSNNSW VHNLVKSTVA TTPVFNGFFK NMEGAFGYGP RYSPSRDEWW
ASENPIRGAS VDIF
