PCEA_DESHY
ID PCEA_DESHY Reviewed; 551 AA.
AC Q8L172;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Tetrachloroethene reductive dehalogenase {ECO:0000303|PubMed:22961902};
DE EC=1.21.99.5 {ECO:0000269|PubMed:12057934, ECO:0000269|PubMed:24814779};
DE AltName: Full=PceA reductive dehalogenase {ECO:0000303|PubMed:12057934};
DE Flags: Precursor;
GN Name=pceA {ECO:0000303|PubMed:12057934};
GN OrderedLocusNames=DSY2839 {ECO:0000312|EMBL:BAE84628.1};
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-59; 73-80; 85-92;
RP 102-114; 273-279; 301-305 AND 400-410, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC STRAIN=Y51;
RX PubMed=12057934; DOI=10.1128/jb.184.13.3419-3428.2002;
RA Suyama A., Yamashita M., Yoshino S., Furukawa K.;
RT "Molecular characterization of the PceA reductive dehalogenase of
RT desulfitobacterium sp. strain Y51.";
RL J. Bacteriol. 184:3419-3425(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPERON STRUCTURE.
RC STRAIN=Y51;
RX PubMed=16133337; DOI=10.1007/s00253-005-0112-9;
RA Futagami T., Tsuboi Y., Suyama A., Goto M., Furukawa K.;
RT "Emergence of two types of nondechlorinating variants in the
RT tetrachloroethene-halorespiring Desulfitobacterium sp. strain Y51.";
RL Appl. Microbiol. Biotechnol. 70:720-728(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
RN [4]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Y51;
RX PubMed=16957221; DOI=10.1128/aem.00979-06;
RA Futagami T., Yamaguchi T., Nakayama S., Goto M., Furukawa K.;
RT "Effects of chloromethanes on growth of and deletion of the pce gene
RT cluster in dehalorespiring Desulfitobacterium hafniense strain Y51.";
RL Appl. Environ. Microbiol. 72:5998-6003(2006).
RN [5]
RP COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=Y51;
RX PubMed=22961902; DOI=10.1128/aem.02173-12;
RA Reinhold A., Westermann M., Seifert J., von Bergen M., Schubert T.,
RA Diekert G.;
RT "Impact of vitamin B12 on formation of the tetrachloroethene reductive
RT dehalogenase in Desulfitobacterium hafniense strain Y51.";
RL Appl. Environ. Microbiol. 78:8025-8032(2012).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND EXPRESSION IN
RP S.BLATTAE.
RC STRAIN=Y51;
RX PubMed=24814779; DOI=10.1128/aem.00881-14;
RA Mac Nelly A., Kai M., Svatos A., Diekert G., Schubert T.;
RT "Functional heterologous production of reductive dehalogenases from
RT Desulfitobacterium hafniense strains.";
RL Appl. Environ. Microbiol. 80:4313-4322(2014).
CC -!- FUNCTION: Catalyzes the reductive dechlorination of tetrachloroethene
CC (PCE) to trichloroethene (TCE) and of trichloroethene to cis-1,2-
CC dichloroethene (DCE) (PubMed:12057934, PubMed:24814779). Can also use
CC various chlorinated ethanes such as tetrachloroethane,
CC pentachloroethane and hexachloroethane (PubMed:12057934). Reduced
CC methyl viologen can act as the artificial electron donor
CC (PubMed:12057934). {ECO:0000269|PubMed:12057934,
CC ECO:0000269|PubMed:24814779}.
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:12057934, ECO:0000269|PubMed:24814779};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20355;
CC Evidence={ECO:0000269|PubMed:12057934, ECO:0000269|PubMed:24814779};
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:12057934,
CC ECO:0000269|PubMed:24814779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67993;
CC Evidence={ECO:0000269|PubMed:12057934, ECO:0000269|PubMed:24814779};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:O68252};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:O68252};
CC -!- COFACTOR:
CC Name=corrinoid; Xref=ChEBI:CHEBI:33913;
CC Evidence={ECO:0000269|PubMed:12057934, ECO:0000269|PubMed:22961902};
CC -!- ACTIVITY REGULATION: PceT is required as a chaperone for prePceA
CC maturation (PubMed:22961902, PubMed:24814779). In the absence or
CC presence of exogenous vitamin B12, the intracellular corrinoid level
CC decreases in fumarate-grown cells and the PceA precursor forms
CC catalytically inactive, corrinoid-free multiprotein aggregates
CC (PubMed:22961902). Exogenous vitamin B12 is not incorporated into the
CC PceA precursor, even though it affects the transposition of the pce
CC gene cluster (PubMed:22961902). {ECO:0000269|PubMed:22961902,
CC ECO:0000269|PubMed:24814779}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=105 uM for tetrachloroethene {ECO:0000269|PubMed:12057934};
CC KM=535 uM for trichloroethene {ECO:0000269|PubMed:12057934};
CC KM=125 uM for hexachloroethane {ECO:0000269|PubMed:12057934};
CC KM=619 uM for pentachloroethane {ECO:0000269|PubMed:12057934};
CC KM=336 uM for 1,1,2,2-tetrachloroethane
CC {ECO:0000269|PubMed:12057934};
CC KM=785 uM for 1,1,1,2-tetrachloroethane
CC {ECO:0000269|PubMed:12057934};
CC Vmax=164 nmol/min/mg enzyme with tetrachloroethene as substrate
CC {ECO:0000269|PubMed:12057934};
CC Vmax=811 nmol/min/mg enzyme with trichloroethene as substrate
CC {ECO:0000269|PubMed:12057934};
CC Vmax=148 nmol/min/mg enzyme with hexachloroethane as substrate
CC {ECO:0000269|PubMed:12057934};
CC Vmax=876 nmol/min/mg enzyme with pentachloroethane as substrate
CC {ECO:0000269|PubMed:12057934};
CC Vmax=42 nmol/min/mg enzyme with 1,1,2,2-tetrachloroethane as
CC substrate {ECO:0000269|PubMed:12057934};
CC Vmax=772 nmol/min/mg enzyme with 1,1,1,2-tetrachloroethane as
CC substrate {ECO:0000269|PubMed:12057934};
CC pH dependence:
CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:12057934};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:12057934};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22961902}. Cell
CC membrane {ECO:0000269|PubMed:22961902}. Secreted
CC {ECO:0000269|PubMed:12057934, ECO:0000269|PubMed:22961902}. Note=In the
CC presence of PCE, the PceA cofactor-free precursor is formed and
CC localizes in the cytoplasm (PubMed:22961902). After incorporation of
CC the corrinoid cofactor and assembly and incorporation of the iron-
CC sulfur clusters, the precursor protein is correctly folded and probably
CC exported to the exoplasm via the TAT system (PubMed:22961902). In the
CC absence of PCE, PceA is detected in large aggregates localized in the
CC cytoplasm (PubMed:22961902). {ECO:0000269|PubMed:22961902}.
CC -!- INDUCTION: Expression is highly induced in the presence of PCE and TCE
CC (PubMed:12057934). Located in the pceABCT gene cluster that is flanked
CC by insertion sequences including transposase genes (PubMed:16133337).
CC PceA, pceB and pceC are cotranscribed (PubMed:16957221). PCE-depleted
CC cells grown for several subcultivation steps on fumarate as an
CC alternative electron acceptor lost the tetrachloroethene-reductive
CC dehalogenase (PceA) activity by the transposition of the pce gene
CC cluster (PubMed:22961902). Exogenous vitamin B12 hampers the
CC transposition of the pce gene cluster (PubMed:22961902).
CC {ECO:0000269|PubMed:12057934, ECO:0000269|PubMed:16133337,
CC ECO:0000269|PubMed:16957221, ECO:0000269|PubMed:22961902}.
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:12057934}.
CC -!- DISRUPTION PHENOTYPE: Chloroform inhibits the growth of the wild-type
CC strain, but not the growth of the PCE-nondechlorinating small deletion
CC (SD) and large deletion (LD) variants, where the former fails to
CC transcribe the pceABC genes caused by a deletion of the promoter and
CC the latter lost the entire pceABCT gene cluster.
CC {ECO:0000269|PubMed:16957221}.
CC -!- SIMILARITY: Belongs to the PceA family. {ECO:0000305}.
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DR EMBL; AB070709; BAC00915.1; -; Genomic_DNA.
DR EMBL; AY706985; AAW80323.1; -; Genomic_DNA.
DR EMBL; AP008230; BAE84628.1; -; Genomic_DNA.
DR RefSeq; WP_011460641.1; NC_007907.1.
DR STRING; 138119.DSY2839; -.
DR EnsemblBacteria; BAE84628; BAE84628; DSY2839.
DR KEGG; dsy:DSY2839; -.
DR eggNOG; COG1600; Bacteria.
DR HOGENOM; CLU_036586_0_0_9; -.
DR OMA; WEKYAGF; -.
DR OrthoDB; 1478472at2; -.
DR BioCyc; MetaCyc:MON-5146; -.
DR BRENDA; 1.21.99.5; 1880.
DR Proteomes; UP000001946; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Cytoplasm; Direct protein sequencing; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..39
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:12057934"
FT CHAIN 40..551
FT /note="Tetrachloroethene reductive dehalogenase"
FT /evidence="ECO:0000269|PubMed:12057934"
FT /id="PRO_5008973249"
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; 61285 MW; FB635899BC4E5F55 CRC64;
MGEINRRNFL KVSILGAAAA AVASASAVKG MVSPLVADAA DIVAPITETS EFPYKVDAKY
QRYNSLKNFF EKTFDPEANK TPIKFHYDDV SKITGKKDTG KDLPTLNAER LGIKGRPATH
TETSILFHTQ HLGAMLTQRH NETGWTGLDE ALNAGAWAVE FDYSGFNATG GGPGSVIPLY
PINPMTNEIA NEPVMVPGLY NWDNIDVESV RQQGQQWKFE SKEEASKIVK KATRLLGADL
VGIAPYDERW TYSTWGRKIY KPCKMPNGRT KYLPWDLPKM LSGGGVEVFG HAKFEPDWEK
YAGFKPKSVI VFVLEEDYEA IRTSPSVISS ATVGKSYSNM AEVAYKIAVF LRKLGYYAAP
CGNDTGISVP MAVQAGLGEA GRNGLLITQK FGPRHRIAKV YTDLELAPDK PRKFGVREFC
RLCKKCADAC PAQAISHEKD PKVLQPEDCE VAENPYTEKW HLDSNRCGSF WAYNGSPCSN
CVAVCSWNKV ETWNHDVARV ATQIPLLQDA ARKFDEWFGY NGPVNPDERL ESGYVQNMVK
DFWNNPESIK Q
