PFOR_MOOTA
ID PFOR_MOOTA Reviewed; 1171 AA.
AC Q2RMD6;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Pyruvate:ferredoxin oxidoreductase {ECO:0000303|PubMed:9214293};
DE Short=PFOR {ECO:0000303|PubMed:9214293};
DE EC=1.2.7.1 {ECO:0000269|PubMed:10878009, ECO:0000305|PubMed:9214293};
DE AltName: Full=Pyruvate synthase {ECO:0000303|PubMed:10878009};
GN OrderedLocusNames=Moth_0064 {ECO:0000312|EMBL:ABC18403.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION
RP MECHANISM.
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=9214293; DOI=10.1021/bi970403k;
RA Menon S., Ragsdale S.W.;
RT "Mechanism of the Clostridium thermoaceticum pyruvate:ferredoxin
RT oxidoreductase: evidence for the common catalytic intermediacy of the
RT hydroxyethylthiamine pyropyrosphate radical.";
RL Biochemistry 36:8484-8494(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP IDENTIFICATION OF PHYSIOLOGICAL ELECTRON CARRIER FOR THE REACTIONS.
RX PubMed=10878009; DOI=10.1074/jbc.m003291200;
RA Furdui C., Ragsdale S.W.;
RT "The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis
RT during autotrophic growth by the Wood-Ljungdahl pathway.";
RL J. Biol. Chem. 275:28494-28499(2000).
RN [4] {ECO:0007744|PDB:6CIN, ECO:0007744|PDB:6CIO, ECO:0007744|PDB:6CIP}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEXES WITH [4FE-4S] CLUSTERS;
RP THIAMINE PYROPHOSPHATE; LACTYL-TPP AND ACETYL-TPP INTERMEDIATES; MAGNESIUM
RP AND COA, FUNCTION, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=29581263; DOI=10.1073/pnas.1722329115;
RA Chen P.Y.-T., Aman H., Can M., Ragsdale S.W., Drennan C.L.;
RT "Binding site for coenzyme A revealed in the structure of
RT pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3846-3851(2018).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of pyruvate to
CC acetyl-CoA and carbon dioxide. The two electrons that are generated as
CC a result of pyruvate decarboxylation are used in the reduction of low
CC potential ferredoxins, which provide reducing equivalents for central
CC metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of
CC pyruvate from acetyl-CoA and carbon dioxide. Appears to function
CC physiologically in both directions (PubMed:10878009). The oxidation of
CC pyruvate by PFOR is required to connect glycolysis and the Wood-
CC Ljungdahl pathway of reductive acetogenesis. The conversion of acetyl-
CC CoA to pyruvate links the Wood-Ljungdahl pathway of autotrophic CO2
CC fixation to the reductive tricarboxylic acid cycle (PubMed:10878009,
CC PubMed:29581263). Can use methyl viologen as electron carrier in vitro
CC (PubMed:9214293, PubMed:29581263). {ECO:0000269|PubMed:10878009,
CC ECO:0000269|PubMed:29581263, ECO:0000269|PubMed:9214293,
CC ECO:0000305|PubMed:10878009, ECO:0000305|PubMed:29581263}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA
CC + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:12765,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=1.2.7.1;
CC Evidence={ECO:0000269|PubMed:10878009, ECO:0000305|PubMed:9214293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12766;
CC Evidence={ECO:0000269|PubMed:10878009};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12767;
CC Evidence={ECO:0000269|PubMed:10878009};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:29581263};
CC Note=Binds 3 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:29581263};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:29581263};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000269|PubMed:29581263};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29581263};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:29581263};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 uM for acetyl-CoA {ECO:0000269|PubMed:10878009};
CC KM=2.0 mM for CO2 {ECO:0000269|PubMed:10878009};
CC KM=0.30 mM for pyruvate {ECO:0000269|PubMed:10878009};
CC KM=0.32 uM for oxidized ferredoxin {ECO:0000269|PubMed:10878009};
CC KM=0.27 uM for reduced ferredoxin {ECO:0000269|PubMed:10878009};
CC KM=9.4 uM for oxidized rubredoxin {ECO:0000269|PubMed:10878009};
CC KM=1.1 mM for methyl viologen (in the oxidative decarboxylation of
CC pyruvate) {ECO:0000269|PubMed:29581263};
CC Vmax=1.6 umol/min/mg enzyme for the synthesis of pyruvate from
CC acetyl-CoA and CO2 with methyl viologen as electron donor
CC {ECO:0000269|PubMed:10878009};
CC Vmax=1.0 umol/min/mg enzyme for the synthesis of pyruvate with
CC reduced ferredoxin as electron donor {ECO:0000269|PubMed:10878009};
CC Vmax=14.2 umol/min/mg enzyme for the oxidative decarboxylation of
CC pyruvate with methyl viologen as electron acceptor
CC {ECO:0000269|PubMed:10878009};
CC Vmax=14.8 umol/min/mg enzyme for the oxidative decarboxylation of
CC pyruvate with oxidized ferredoxin as electron acceptor
CC {ECO:0000269|PubMed:10878009};
CC Vmax=9.9 umol/min/mg enzyme for the oxidative decarboxylation of
CC pyruvate with oxidized rubredoxin as electron acceptor
CC {ECO:0000269|PubMed:10878009};
CC Note=kcat is 3.2 sec(-1) for the synthesis of pyruvate from acetyl-
CC CoA and CO2 with methyl viologen as electron donor (PubMed:10878009).
CC kcat is 2.0 sec(-1) for the synthesis of pyruvate from acetyl-CoA and
CC CO2 with reduced ferredoxin as electron donor (PubMed:10878009). kcat
CC is 28 sec(-1) for the oxidative decarboxylation of pyruvate with
CC methyl viologen as electron acceptor (PubMed:10878009). kcat is 33
CC sec(-1) for the oxidative decarboxylation of pyruvate with methyl
CC viologen as electron acceptor (PubMed:29581263). kcat is 29.6 sec(-1)
CC for the oxidative decarboxylation of pyruvate with oxidized
CC ferredoxin as electron acceptor (PubMed:10878009). kcat is 19.8 sec(-
CC 1) for the oxidative decarboxylation of pyruvate with oxidized
CC rubredoxin as electron acceptor (PubMed:10878009).
CC {ECO:0000269|PubMed:10878009, ECO:0000269|PubMed:29581263};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29581263}.
CC -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; CP000232; ABC18403.1; -; Genomic_DNA.
DR RefSeq; WP_011391612.1; NC_007644.1.
DR RefSeq; YP_428946.1; NC_007644.1.
DR PDB; 6CIN; X-ray; 2.60 A; A/B/C/D/E/F=1-1171.
DR PDB; 6CIO; X-ray; 3.00 A; A/B/C/D/E/F=1-1171.
DR PDB; 6CIP; X-ray; 3.19 A; A/B/C/D/E/F=1-1171.
DR PDB; 6CIQ; X-ray; 3.30 A; A/B/C=1-1171.
DR PDBsum; 6CIN; -.
DR PDBsum; 6CIO; -.
DR PDBsum; 6CIP; -.
DR PDBsum; 6CIQ; -.
DR AlphaFoldDB; Q2RMD6; -.
DR SMR; Q2RMD6; -.
DR STRING; 264732.Moth_0064; -.
DR EnsemblBacteria; ABC18403; ABC18403; Moth_0064.
DR GeneID; 61288830; -.
DR KEGG; mta:Moth_0064; -.
DR PATRIC; fig|264732.11.peg.68; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_002569_0_0_9; -.
DR OMA; NTVMQVC; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.920.10; -; 1.
DR Gene3D; 4.10.780.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR011895; Pyrv_flavodox_OxRed.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR Pfam; PF10371; EKR; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR PIRSF; PIRSF000159; NifJ; 1.
DR SMART; SM00890; EKR; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR SUPFAM; SSF53323; SSF53323; 1.
DR TIGRFAMs; TIGR02176; pyruv_ox_red; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Magnesium;
KW Metal-binding; Oxidoreductase; Pyruvate; Transport.
FT CHAIN 1..1171
FT /note="Pyruvate:ferredoxin oxidoreductase"
FT /id="PRO_0000446263"
FT DOMAIN 677..706
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 733..764
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 29
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000305|PubMed:29581263,
FT ECO:0000312|PDB:6CIO"
FT BINDING 112
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000305|PubMed:29581263,
FT ECO:0000312|PDB:6CIO"
FT BINDING 424..428
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIQ"
FT BINDING 456
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIQ"
FT BINDING 556
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIQ"
FT BINDING 598
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIQ"
FT BINDING 686
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 689
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 692
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 696
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 742
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 745
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 748
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 752
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 809
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 812
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 814
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIO"
FT BINDING 837
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 837
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 967..969
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 967
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 995..1000
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 995
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 997
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT BINDING 1000
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000305|PubMed:29581263,
FT ECO:0000312|PDB:6CIO"
FT BINDING 1075
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29581263,
FT ECO:0000312|PDB:6CIN"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:6CIO"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 144..161
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 231..252
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 295..305
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 308..313
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6CIO"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 427..441
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 460..470
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 482..487
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 497..500
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 524..532
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 542..549
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 556..567
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 572..587
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 588..590
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 592..608
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:6CIP"
FT HELIX 616..620
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 634..638
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 640..644
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 653..655
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 676..681
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 691..695
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 701..706
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 708..711
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 727..730
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 732..737
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 739..741
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 747..751
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 758..763
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 764..779
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 793..797
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 815..825
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 826..828
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 829..833
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 837..842
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 860..862
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 869..895
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 901..913
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 917..936
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 940..951
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 952..955
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 960..966
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 967..971
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 972..974
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 975..984
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 989..994
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 996..998
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 999..1002
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 1029..1034
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 1037..1044
FT /evidence="ECO:0007829|PDB:6CIN"
FT TURN 1046..1048
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 1050..1062
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 1063..1065
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 1067..1072
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 1076..1078
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 1082..1084
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 1085..1094
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 1101..1103
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 1105..1109
FT /evidence="ECO:0007829|PDB:6CIN"
FT STRAND 1114..1118
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 1126..1130
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 1134..1137
FT /evidence="ECO:0007829|PDB:6CIN"
FT HELIX 1148..1169
FT /evidence="ECO:0007829|PDB:6CIN"
SQ SEQUENCE 1171 AA; 127277 MW; 3F171E506F8D9B6E CRC64;
MPKQTLDGNT AAAHVAYAMS EVATIYPITP SSPMAEIADE WAAHGRKNIF GKTLQVAEMQ
SEAGAAGAVH GSLAAGALTT TFTASQGLLL MIPNMYKIAG ELLPCVFHVA ARALSTHALS
IFGDHADVMA ARQTGFAMLS SASVQEVMDL ALVAHLATLK ARVPFVHFFD GFRTSHEVQK
IDVIEYEDMA KLVDWDAIRA FRQRALNPEH PHQRGTAQNP DIYFQSREAA NPYYLATPGI
VAQVMEQVAG LTGRHYHLFD YAGAPDAERV IVSMGSSCEV IEETVNYLVE KGEKVGLIKV
RLFRPFSAEH FLKVLPASVK RIAVLDRTKE PGSLGEPLYE DVQTVLAEHG KNILVVGGRY
GLGSKEFNPS MVKAVFDNLA ATTPKNKFTV GITDDVTHTS LEIKEHIDTS PKGTFRCKFF
GLGSDGTVGA NKNSIKIIGD HTDMYAQGYF VYDSKKSGGV TISHLRFGKQ PIQSAYLIDQ
ADLIACHNPS YVGRYNLLEG IKPGGIFLLN STWSAEEMDS RLPADMKRTI ATKKLKFYNI
DAVKIAQEIG LGSRINVIMQ TAFFKIANVI PVDEAIKYIK DSIVKTYGKK GDKILNMNFA
AVDRALEALE EIKYPASWAD AVDEAAATVT EEPEFIQKVL RPINALKGDE LPVSTFTPDG
VFPVGTTKYE KRGIAVNIPQ WQPENCIQCN QCSLVCPHAA IRPYLAKPAD LAGAPETFVT
KDAIGKEAAG LKFRIQVSPL DCTGCGNCAD VCPAKVKALT MVPLEEVTAV EEANYNFAEQ
LPEVKVNFNP ATVKGSQFRQ PLLEFSGACA GCGETPYVKL VTQLFGDRMI IANATGCSSI
WGGSAPACPY TVNRQGHGPA WASSLFEDNA EFGYGMALAV AKRQDELATA ISKALEAPVS
AAFKAACEGW LAGKDDADRS REYGDRIKAL LPGEISQASG EVKDLLLDID RQKDYLTKKS
IWIIGGDGWA YDIGYGGLDH VLASGANVNV LVLDTEVYSN TGGQSSKATQ TGAVARFAAG
GKFTKKKDLG LMAMSYGYVY VASVAMGASH SQLMKALIEA EKYDGPSLII AYAPCINHGI
NMTYSQREAK KAVEAGYWPL YRYNPQLAQE GKNPFILDYK TPTASFRDFL MGEIRYTSLK
KQFPEKAEQL FAKAEADAKA RLEQYKKLAE G
