VCRA_DEHMV
ID VCRA_DEHMV Reviewed; 519 AA.
AC Q69GM4; D2BJ91;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Chloroethene reductive dehalogenase {ECO:0000305};
DE EC=1.21.99.- {ECO:0000269|PubMed:15294827};
DE AltName: Full=Vinyl chloride reductase {ECO:0000303|PubMed:15294827};
DE Short=VC reductase {ECO:0000303|PubMed:15294827};
DE AltName: Full=Vinyl chloride reductive dehalogenase {ECO:0000305};
DE Flags: Precursor;
GN Name=vcrA {ECO:0000303|PubMed:15294827};
GN OrderedLocusNames=DhcVS_1291 {ECO:0000312|EMBL:ACZ62391.1};
OS Dehalococcoides mccartyi (strain VS).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=311424;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 44-63; 83-94;
RP 136-148; 287-295 AND 322-329, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC STRAIN=VS;
RX PubMed=15294827; DOI=10.1128/aem.70.8.4880-4888.2004;
RA Muller J.A., Rosner B.M., Von Abendroth G., Meshulam-Simon G.,
RA McCarty P.L., Spormann A.M.;
RT "Molecular identification of the catabolic vinyl chloride reductase from
RT Dehalococcoides sp. strain VS and its environmental distribution.";
RL Appl. Environ. Microbiol. 70:4880-4888(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS;
RX PubMed=19893622; DOI=10.1371/journal.pgen.1000714;
RA McMurdie P.J., Behrens S.F., Muller J.A., Goke J., Ritalahti K.M.,
RA Wagner R., Goltsman E., Lapidus A., Holmes S., Loffler F.E., Spormann A.M.;
RT "Localized plasticity in the streamlined genomes of vinyl chloride
RT respiring Dehalococcoides.";
RL PLoS Genet. 5:E1000714-E1000714(2009).
CC -!- FUNCTION: Catalyzes the reductive dechlorination of chloroethene (or
CC vinyl chloride, VC) to ethene (PubMed:15294827). Can also reduce all
CC dichloroethene (DCE) isomers, but not tetrachloroethene (PCE) or
CC trichloroethene (TCE), at high rates (PubMed:15294827). Reduced methyl
CC viologen can act as the artificial electron donor (PubMed:15294827).
CC {ECO:0000269|PubMed:15294827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + chloroethene = A + chloride + ethene + H(+);
CC Xref=Rhea:RHEA:68004, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:17996, ChEBI:CHEBI:18153,
CC ChEBI:CHEBI:28509; Evidence={ECO:0000269|PubMed:15294827};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68005;
CC Evidence={ECO:0000269|PubMed:15294827};
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:15294827};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67997;
CC Evidence={ECO:0000269|PubMed:15294827};
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:15294827};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68001;
CC Evidence={ECO:0000269|PubMed:15294827};
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:0000250|UniProtKB:O68252};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15294827}.
CC -!- INDUCTION: Cotranscribed with vcrB and vcrC.
CC {ECO:0000269|PubMed:15294827}.
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:15294827}.
CC -!- SIMILARITY: Belongs to the PceA family. {ECO:0000305}.
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DR EMBL; AY322364; AAQ94119.1; -; Genomic_DNA.
DR EMBL; CP001827; ACZ62391.1; -; Genomic_DNA.
DR RefSeq; WP_012882535.1; NC_013552.1.
DR STRING; 311424.DhcVS_1291; -.
DR EnsemblBacteria; ACZ62391; ACZ62391; DhcVS_1291.
DR KEGG; dev:DhcVS_1291; -.
DR eggNOG; COG2768; Bacteria.
DR HOGENOM; CLU_036586_0_1_0; -.
DR OMA; KCESIFT; -.
DR Proteomes; UP000002506; 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; 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; 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; Signal.
FT SIGNAL 1..43
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:15294827"
FT CHAIN 44..519
FT /note="Chloroethene reductive dehalogenase"
FT /evidence="ECO:0000269|PubMed:15294827"
FT /id="PRO_0000454141"
FT DOMAIN 388..420
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 435..465
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 400
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 403
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 406
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 410
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 444
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 448
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 451
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 455
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 519 AA; 57534 MW; 256CEA048F44E488 CRC64;
MSKFHKTISR RDFMKGLGLA GAGIGAVAAS APVFHDIDEL VSSEANSTKD QPWYVKHREH
FDPTITVDWD IFDRYDGYQH KGVYEGPPDA PFTSWGNRLQ VRMSGEEQKK RILAAKKERF
PGWDGGLHGR GDQRADALFY AVTQPFPGSG EEGHGLFQPY PDQPGKFYAR WGLYGPPHDS
APPDGSVPKW EGTPEDNFLM LRAAAKYFGA GGVGALNLAD PKCKKLIYKK AQPMTLGKGT
YSEIGGPGMI DAKIYPKVPD HAVPINFKEA DYSYYNDAEW VIPTKCESIF TFTLPQPQEL
NKRTGGIAGA GSYTVYKDFA RVGTLVQMFI KYLGYHALYW PIGWGPGGCF TTFDGQGEQG
RTGAAIHWKF GSSQRGSERV ITDLPIAPTP PIDAGMFEFC KTCYICRDVC VSGGVHQEDE
PTWDSGNWWN VQGYLGYRTD WSGCHNQCGM CQSSCPFTYL GLENASLVHK IVKGVVANTT
VFNSFFTNME KALGYGDLTM ENSNWWKEEG PIYGFDPGT
