PCEA_SULMU
ID PCEA_SULMU Reviewed; 501 AA.
AC O68252;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Tetrachloroethene reductive dehalogenase {ECO:0000303|PubMed:8663199};
DE EC=1.21.99.5 {ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164, ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:8663199};
DE AltName: Full=PCE dehalogenase {ECO:0000303|PubMed:12420164};
DE Flags: Precursor;
GN Name=pceA {ECO:0000303|PubMed:9696761};
GN ORFNames=SMN_1516 {ECO:0000312|EMBL:QEH06286.1};
OS Sulfurospirillum multivorans (Dehalospirillum multivorans).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurospirillaceae; Sulfurospirillum.
OX NCBI_TaxID=66821;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9696761; DOI=10.1128/jb.180.16.4140-4145.1998;
RA Neumann A., Wohlfarth G., Diekert G.;
RT "Tetrachloroethene dehalogenase from Dehalospirillum multivorans: cloning,
RT sequencing of the encoding genes, and expression of the pceA gene in
RT Escherichia coli.";
RL J. Bacteriol. 180:4140-4145(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15119 / N;
RA Goris T., Esken J., Gadkari J., Bischler T., Foerstner K., Sharma C.M.,
RA Diekert G., Schubert T.;
RT "Organohalide respiration in Sulfurospirillum species is regulated by a
RT two-component system as unraveled by comparative genomics, and
RT transcriptomics, and regulator binding studies.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=8663199; DOI=10.1074/jbc.271.28.16515;
RA Neumann A., Wohlfarth G., Diekert G.;
RT "Purification and characterization of tetrachloroethene reductive
RT dehalogenase from Dehalospirillum multivorans.";
RL J. Biol. Chem. 271:16515-16519(1996).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11976751; DOI=10.1007/s00203-002-0409-3;
RA Neumann A., Siebert A., Trescher T., Reinhardt S., Wohlfarth G.,
RA Diekert G.;
RT "Tetrachloroethene reductive dehalogenase of Dehalospirillum multivorans:
RT substrate specificity of the native enzyme and its corrinoid cofactor.";
RL Arch. Microbiol. 177:420-426(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND LACK OF ACTIVITY IN STRAIN N.
RC STRAIN=DSM 12446 / K, and DSM 15119 / N;
RX PubMed=12420164; DOI=10.1007/s00203-002-0473-8;
RA Siebert A., Neumann A., Schubert T., Diekert G.;
RT "A non-dechlorinating strain of Dehalospirillum multivorans: evidence for a
RT key role of the corrinoid cofactor in the synthesis of an active
RT tetrachloroethene dehalogenase.";
RL Arch. Microbiol. 178:443-449(2002).
RN [6]
RP COFACTOR.
RX DOI=10.1002/hlca.200390313;
RA Kraeutler B., Fieber W., Ostermann S., Fasching M., Ongania K.-H.,
RA Gruber K., Kratky C., Mikl C., Siebert A., Diekert G.;
RT "The cofactor of tetrachloroethene reductive dehalogenase of
RT Dehalospirillum multivorans is norpseudo-B12, a new type of a natural
RT corrinoid.";
RL Helv. Chim. Acta 86:3698-3716(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC STRAIN=DSM 12446 / K;
RX PubMed=16802174; DOI=10.1007/s00203-006-0125-5;
RA John M., Schmitz R.P., Westermann M., Richter W., Diekert G.;
RT "Growth substrate dependent localization of tetrachloroethene reductive
RT dehalogenase in Sulfurospirillum multivorans.";
RL Arch. Microbiol. 186:99-106(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=DSM 12446 / K;
RX PubMed=24433392; DOI=10.1111/1462-2920.12268;
RA Keller S., Ruetz M., Kunze C., Kraeutler B., Diekert G., Schubert T.;
RT "Exogenous 5,6-dimethylbenzimidazole caused production of a non-functional
RT tetrachloroethene reductive dehalogenase in Sulfurospirillum multivorans.";
RL Environ. Microbiol. 16:3361-3369(2014).
RN [9]
RP BIOTECHNOLOGY.
RC STRAIN=DSM 12446 / K;
RX PubMed=29228161; DOI=10.1093/femsec/fix176;
RA Gadkari J., Goris T., Schiffmann C.L., Rubick R., Adrian L., Schubert T.,
RA Diekert G.;
RT "Reductive tetrachloroethene dehalogenation in the presence of oxygen by
RT Sulfurospirillum multivorans: physiological studies and proteome
RT analysis.";
RL FEMS Microbiol. Ecol. 94:0-0(2018).
RN [10] {ECO:0007744|PDB:5M2G, ECO:0007744|PDB:5M8U, ECO:0007744|PDB:5M8W, ECO:0007744|PDB:5MA2}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 38-501 IN COMPLEXES WITH
RP IRON-SULFUR CLUSTERS; NORPSEUDO-B12 AND SUBSTRATES, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28671181; DOI=10.1038/ncomms15858;
RA Kunze C., Bommer M., Hagen W.R., Uksa M., Dobbek H., Schubert T.,
RA Diekert G.;
RT "Cobamide-mediated enzymatic reductive dehalogenation via long-range
RT electron transfer.";
RL Nat. Commun. 8:15858-15858(2017).
RN [11] {ECO:0007744|PDB:5OBP}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 38-501 IN COMPLEX WITH
RP IRON-SULFUR CLUSTER AND HYDROXYBENZIMIDAZOLYL NORCOBAMIDE, AND COFACTOR.
RC STRAIN=DSM 12446 / K;
RX PubMed=29378885; DOI=10.1128/jb.00584-17;
RA Keller S., Kunze C., Bommer M., Paetz C., Menezes R.C., Svatos A.,
RA Dobbek H., Schubert T.;
RT "Selective utilization of benzimidazolyl-norcobamides as cofactors by the
RT tetrachloroethene reductive dehalogenase of Sulfurospirillum multivorans.";
RL J. Bacteriol. 200:0-0(2018).
CC -!- FUNCTION: Catalyzes the reductive dechlorination of tetrachloroethene
CC (PCE) to trichloroethene (TCE) and of trichloroethene to cis-1,2-
CC dichloroethene (DCE) (PubMed:8663199, PubMed:11976751, PubMed:12420164,
CC PubMed:24433392, PubMed:28671181). In addition, trans-1,3-
CC dichloropropene, 1,1,3-trichloropropene and 2,3-dichloropropene are
CC reduced to a mixture of mono-chloropropenes, 1,1-dichloropropene, and
CC 2-chloropropene, respectively (PubMed:11976751). Is also able to
CC convert brominated phenols such as 4-bromophenol (4-BP), 2,4-
CC dibromophenol (2,4-DBP) and 2,4,6-tribromophenol (2,4,6-TBP)
CC (PubMed:28671181). Utilizes formate or pyruvate as electron donors
CC (PubMed:16802174, PubMed:24433392). Titanium(III) citrate could also
CC serve as electron donor (PubMed:11976751). Reduced methyl viologen can
CC act as the artificial electron donor (PubMed:8663199, PubMed:11976751,
CC PubMed:12420164). {ECO:0000269|PubMed:11976751,
CC ECO:0000269|PubMed:12420164, ECO:0000269|PubMed:16802174,
CC ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181,
CC ECO:0000269|PubMed:8663199}.
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:11976751, ECO:0000269|PubMed:12420164,
CC ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181,
CC ECO:0000269|PubMed:8663199};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20355;
CC Evidence={ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164,
CC ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181,
CC ECO:0000269|PubMed:8663199};
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:11976751,
CC ECO:0000269|PubMed:12420164, ECO:0000269|PubMed:24433392,
CC ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:8663199};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67993;
CC Evidence={ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164,
CC ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181,
CC ECO:0000269|PubMed:8663199};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:29378885,
CC ECO:0000269|PubMed:8663199};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:28671181,
CC ECO:0000269|PubMed:29378885, ECO:0000269|PubMed:8663199};
CC -!- COFACTOR:
CC Name=corrinoid; Xref=ChEBI:CHEBI:33913;
CC Evidence={ECO:0000269|PubMed:11976751, ECO:0000269|PubMed:12420164,
CC ECO:0000269|PubMed:24433392, ECO:0000269|PubMed:28671181,
CC ECO:0000269|PubMed:8663199, ECO:0000269|Ref.6};
CC Note=The corrinoid cofactor is norpseudovitamin B12 (norpseudo-B12), a
CC natural B12 cofactor that lacks a characteristic methyl group of the
CC cobamide structure (Ref.6, PubMed:24433392, PubMed:28671181). In vitro,
CC can function with singly substituted benzimidazolyl-norcobamides
CC cofactors (PubMed:29378885). {ECO:0000269|PubMed:24433392,
CC ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:29378885,
CC ECO:0000269|Ref.6};
CC -!- ACTIVITY REGULATION: Both the processed and unprocessed enzymes are
CC catalytically active (PubMed:16802174). PCE-dependent growth and PceA
CC activity are inhibited in the presence of high concentrations of 5,6-
CC dimethylbenzimidazole (DMB), probably due to the formation a DMB-
CC containing nor-B12 cofactor (PubMed:24433392). Dechlorination of PCE is
CC stimulated by ammonium ions (PubMed:8663199, PubMed:28671181). Activity
CC is inhibited by chlorinated methanes (PubMed:8663199).
CC {ECO:0000269|PubMed:16802174, ECO:0000269|PubMed:24433392,
CC ECO:0000269|PubMed:28671181, ECO:0000269|PubMed:8663199}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.20 mM for tetrachloroethene (with reduced methyl viologen as
CC electron donor) {ECO:0000269|PubMed:8663199};
CC KM=200 uM for tetrachloroethene (with reduced methyl viologen as
CC electron donor) {ECO:0000269|PubMed:11976751};
CC KM=0.24 mM for trichloroethene (with reduced methyl viologen as
CC electron donor) {ECO:0000269|PubMed:8663199};
CC KM=240 uM for trichloroethene (with reduced methyl viologen as
CC electron donor) {ECO:0000269|PubMed:11976751};
CC KM=250 uM for trans-1,3-dichloropropene (with reduced methyl viologen
CC as electron donor) {ECO:0000269|PubMed:11976751};
CC KM=250 uM for 1,1,3-trichloropropene (with reduced methyl viologen as
CC electron donor) {ECO:0000269|PubMed:11976751};
CC KM=600 uM for 2,3-dichloropropene (with reduced methyl viologen as
CC electron donor) {ECO:0000269|PubMed:11976751};
CC KM=99 uM for 4-BP {ECO:0000269|PubMed:28671181};
CC KM=95 uM for 2,4-DBP {ECO:0000269|PubMed:28671181};
CC KM=158 uM for 2,4,6-TBP {ECO:0000269|PubMed:28671181};
CC pH dependence:
CC Optimum pH is about 8.0. {ECO:0000269|PubMed:8663199};
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius.
CC {ECO:0000269|PubMed:8663199};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8663199}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16802174,
CC ECO:0000269|PubMed:8663199, ECO:0000269|PubMed:9696761}. Cell inner
CC membrane {ECO:0000269|PubMed:16802174}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16802174}; Cytoplasmic side
CC {ECO:0000269|PubMed:16802174}. Cell inner membrane
CC {ECO:0000269|PubMed:16802174}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16802174}; Periplasmic side
CC {ECO:0000269|PubMed:16802174}. Note=The localization of the enzyme is
CC dependent on the electron acceptor utilized. When the cells are grown
CC with pyruvate plus fumarate, a major part of the enzyme is either
CC localized in the cytoplasm or membrane associated facing the cytoplasm.
CC In cells grown on pyruvate or formate as electron donors and PCE as
CC electron acceptor, most of the enzyme is detected at the periplasmic
CC side of the cytoplasmic membrane. {ECO:0000269|PubMed:16802174}.
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 -!- BIOTECHNOLOGY: Chlorinated ethenes are widely occurring as groundwater
CC contaminants and PceA may play an important role in the degradation of
CC these chlorinated environmental pollutants. S.multivorans enzyme can
CC dechlorinate PCE in the presence of oxygen concentrations equal to or
CC below 0.19 mg/L, which enhances the applicability to use S.multivorans
CC for bioremediation, e.g. at oxic/anoxic interphases. Higher levels of
CC oxygen impair PCE dechlorination by inhibiting or inactivating involved
CC enzymes. {ECO:0000269|PubMed:29228161}.
CC -!- MISCELLANEOUS: The pceA gene is detected in cells of strain N, but this
CC strain cannot dechlorinate PCE. The inability of strain N to
CC dechlorinate PCE is probably due to the absence in this strain of the
CC specific PCE dehalogenase corrinoid cofactor.
CC {ECO:0000269|PubMed:12420164}.
CC -!- SIMILARITY: Belongs to the PceA family. {ECO:0000305}.
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DR EMBL; AF022812; AAC60788.1; -; Genomic_DNA.
DR EMBL; CP042966; QEH06286.1; -; Genomic_DNA.
DR PDB; 5M2G; X-ray; 1.80 A; A/B=38-501.
DR PDB; 5M8U; X-ray; 1.90 A; A/B=38-501.
DR PDB; 5M8W; X-ray; 2.28 A; A/B=38-501.
DR PDB; 5MA2; X-ray; 1.88 A; A/B=38-501.
DR PDB; 5OBP; X-ray; 1.59 A; A/B=38-501.
DR PDBsum; 5M2G; -.
DR PDBsum; 5M8U; -.
DR PDBsum; 5M8W; -.
DR PDBsum; 5MA2; -.
DR PDBsum; 5OBP; -.
DR SMR; O68252; -.
DR STRING; 1150621.SMUL_1531; -.
DR GO; GO:0005737; C:cytoplasm; 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 Pfam; PF13486; Dehalogenase; 1.
DR TIGRFAMs; TIGR02486; RDH; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Repeat; Signal.
FT SIGNAL 1..37
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 38..501
FT /note="Tetrachloroethene reductive dehalogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT /id="PRO_0000453974"
FT DOMAIN 356..386
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 420..439
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 74
FT /ligand="corrinoid"
FT /ligand_id="ChEBI:CHEBI:33913"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 207
FT /ligand="corrinoid"
FT /ligand_id="ChEBI:CHEBI:33913"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 309..314
FT /ligand="corrinoid"
FT /ligand_id="ChEBI:CHEBI:33913"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 329..332
FT /ligand="corrinoid"
FT /ligand_id="ChEBI:CHEBI:33913"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 341..343
FT /ligand="corrinoid"
FT /ligand_id="ChEBI:CHEBI:33913"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 366
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 369
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 372
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 376
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 394..401
FT /ligand="corrinoid"
FT /ligand_id="ChEBI:CHEBI:33913"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 409
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 419
FT /ligand="corrinoid"
FT /ligand_id="ChEBI:CHEBI:33913"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 420
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 423
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT BINDING 427
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28671181,
FT ECO:0000269|PubMed:29378885, ECO:0000312|PDB:5M2G,
FT ECO:0000312|PDB:5M8U, ECO:0000312|PDB:5M8W,
FT ECO:0000312|PDB:5MA2, ECO:0000312|PDB:5OBP"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5OBP"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5OBP"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5OBP"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:5OBP"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:5OBP"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 273..299
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5M2G"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5OBP"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:5OBP"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 469..473
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:5OBP"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 487..490
FT /evidence="ECO:0007829|PDB:5OBP"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:5OBP"
SQ SEQUENCE 501 AA; 55887 MW; 41AAF2558082A989 CRC64;
MEKKKKPELS RRDFGKLIIG GGAAATIAPF GVPGANAAEK EKNAAEIRQQ FAMTAGSPII
VNDKLERYAE VRTAFTHPTS FFKPNYKGEV KPWFLSAYDE KVRQIENGEN GPKMKAKNVG
EARAGRALEA AGWTLDINYG NIYPNRFFML WSGETMTNTQ LWAPVGLDRR PPDTTDPVEL
TNYVKFAARM AGADLVGVAR LNRNWVYSEA VTIPADVPYE QSLHKEIEKP IVFKDVPLPI
ETDDELIIPN TCENVIVAGI AMNREMMQTA PNSMACATTA FCYSRMCMFD MWLCQFIRYM
GYYAIPSCNG VGQSVAFAVE AGLGQASRMG ACITPEFGPN VRLTKVFTNM PLVPDKPIDF
GVTEFCETCK KCARECPSKA ITEGPRTFEG RSIHNQSGKL QWQNDYNKCL GYWPESGGYC
GVCVAVCPFT KGNIWIHDGV EWLIDNTRFL DPLMLGMDDA LGYGAKRNIT EVWDGKINTY
GLDADHFRDT VSFRKDRVKK S
