PCEA2_DESHA
ID PCEA2_DESHA Reviewed; 551 AA.
AC Q8GJ31;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Tetrachloroethene reductive dehalogenase {ECO:0000303|PubMed:12902251};
DE EC=1.21.99.5 {ECO:0000250|UniProtKB:Q848J2};
DE Flags: Precursor;
GN Name=pceA {ECO:0000303|PubMed:12902251};
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=TCE1;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=TCE1;
RX PubMed=15643941; DOI=10.1111/j.1462-2920.2004.00671.x;
RA Maillard J., Regeard C., Holliger C.;
RT "Isolation and characterization of Tn-Dha1, a transposon containing the
RT tetrachloroethene reductive dehalogenase of Desulfitobacterium hafniense
RT strain TCE1.";
RL Environ. Microbiol. 7:107-117(2005).
CC -!- FUNCTION: Catalyzes the reductive dechlorination of tetrachloroethene
CC (PCE) to trichloroethene (TCE) and of trichloroethene to cis-1,2-
CC dichloroethene (DCE). {ECO:0000250|UniProtKB:Q848J2}.
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:0000250|UniProtKB:Q848J2};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20355;
CC Evidence={ECO:0000250|UniProtKB:Q848J2};
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:0000250|UniProtKB:Q848J2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67993;
CC Evidence={ECO:0000250|UniProtKB:Q848J2};
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:0000250|UniProtKB:Q848J2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q848J2};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q848J2}.
CC -!- INDUCTION: Coexpressed with pceB. {ECO:0000269|PubMed:15643941}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC -!- SIMILARITY: Belongs to the PceA family. {ECO:0000305}.
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DR EMBL; AJ439608; CAD28792.1; -; Genomic_DNA.
DR BRENDA; 1.21.99.5; 1880.
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 2: Evidence at transcript level;
KW 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Repeat; Signal.
FT SIGNAL 1..39
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 40..551
FT /note="Tetrachloroethene reductive dehalogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT /id="PRO_5004307762"
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; 61299 MW; FB63588EB723FE85 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 ETWNHDVARI ATQIPLLQDA ARKFDEWFGY NGPVNPDERL ESGYVQNMVK
DFWNNPESIK Q
