PFOR_DESAF
ID PFOR_DESAF Reviewed; 1232 AA.
AC P94692;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Pyruvate:ferredoxin oxidoreductase {ECO:0000303|PubMed:10048931};
DE Short=PFOR;
DE Short=POR {ECO:0000303|PubMed:7612653};
DE EC=1.2.7.1 {ECO:0000269|PubMed:7612653};
DE AltName: Full=Pyruvate synthase {ECO:0000305};
GN Name=por {ECO:0000312|EMBL:CAA70873.1};
OS Desulfocurvibacter africanus (Desulfovibrio africanus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=873 {ECO:0000312|EMBL:CAA70873.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18; 304-313;
RP 484-504 AND 1198-1216, AND FUNCTION.
RC STRAIN=ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi;
RX PubMed=9294422; DOI=10.1128/jb.179.18.5684-5692.1997;
RA Pieulle L., Magro V., Hatchikian E.C.;
RT "Isolation and analysis of the gene encoding the pyruvate-ferredoxin
RT oxidoreductase of Desulfovibrio africanus, production of the recombinant
RT enzyme in Escherichia coli, and effect of carboxy-terminal deletions on its
RT stability.";
RL J. Bacteriol. 179:5684-5692(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi;
RX PubMed=7612653; DOI=10.1016/0167-4838(95)00029-t;
RA Pieulle L., Guigliarelli B., Asso M., Dole F., Bernadac A.,
RA Hatchikian E.C.;
RT "Isolation and characterization of the pyruvate-ferredoxin oxidoreductase
RT from the sulfate-reducing bacterium Desulfovibrio africanus.";
RL Biochim. Biophys. Acta 1250:49-59(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 2-1232 IN COMPLEX WITH
RP IRON-SULFUR(4FE-4S); CALCIUM ION; MAGNESIUM ION; PYRUVATE AND
RP THIAMINEPYROPHOSPHATE, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=10048931; DOI=10.1038/5870;
RA Chabriere E., Charon M.H., Volbeda A., Pieulle L., Hatchikian E.C.,
RA Fontecilla-Camps J.C.;
RT "Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin
RT oxidoreductase, free and in complex with pyruvate.";
RL Nat. Struct. Biol. 6:182-190(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-1232 IN COMPLEX WITH CALCIUM;
RP IRON-SULFUR(4FE-4S); MAGNESIUM AND THIAMINEPYROPHOSPHATE ANALOG, AND
RP SUBUNIT.
RX PubMed=11752578; DOI=10.1126/science.1066198;
RA Chabriere E., Vernede X., Guigliarelli B., Charon M.H., Hatchikian E.C.,
RA Fontecilla-Camps J.C.;
RT "Crystal structure of the free radical intermediate of pyruvate:ferredoxin
RT oxidoreductase.";
RL Science 294:2559-2563(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 2-1232 IN COMPLEX WITH
RP IRON-SULFUR(4FE-4S); CALCIUM ION; MAGNESIUM ION; PYRUVATE AND
RP THIAMINEPYROPHOSPHATE, AND SUBUNIT.
RX PubMed=16472741; DOI=10.1016/j.str.2005.10.013;
RA Cavazza C., Contreras-Martel C., Pieulle L., Chabriere E., Hatchikian E.C.,
RA Fontecilla-Camps J.C.;
RT "Flexibility of thiamine diphosphate revealed by kinetic crystallographic
RT studies of the reaction of pyruvate-ferredoxin oxidoreductase with
RT pyruvate.";
RL Structure 14:217-224(2006).
CC -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC of pyruvate. Required for the transfer of electrons from pyruvate to
CC ferredoxin (PubMed:9294422, PubMed:7612653). Ferredoxin I and
CC ferredoxin II, which are single 4Fe-4S cluster ferredoxins are the most
CC effective electron carriers of POR (PubMed:7612653).
CC {ECO:0000269|PubMed:7612653}.
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:7612653};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10048931, ECO:0000269|PubMed:11752578,
CC ECO:0000269|PubMed:16472741, ECO:0000269|PubMed:7612653};
CC Note=Binds 3 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:10048931, ECO:0000269|PubMed:11752578,
CC ECO:0000269|PubMed:16472741, ECO:0000269|PubMed:7612653};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:10048931, ECO:0000269|PubMed:11752578,
CC ECO:0000269|PubMed:16472741};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000269|PubMed:10048931, ECO:0000269|PubMed:11752578,
CC ECO:0000269|PubMed:16472741};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10048931, ECO:0000269|PubMed:11752578,
CC ECO:0000269|PubMed:16472741};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:10048931,
CC ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10048931,
CC ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741,
CC ECO:0000269|PubMed:7612653}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7612653}.
CC -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; Y09702; CAA70873.1; -; Genomic_DNA.
DR PDB; 1B0P; X-ray; 2.31 A; A/B=2-1232.
DR PDB; 1KEK; X-ray; 1.90 A; A/B=2-1232.
DR PDB; 2C3M; X-ray; 1.84 A; A/B=2-1232.
DR PDB; 2C3O; X-ray; 2.70 A; A/B=2-1232.
DR PDB; 2C3P; X-ray; 2.33 A; A/B=2-1232.
DR PDB; 2C3U; X-ray; 2.32 A; A/B=2-1232.
DR PDB; 2C3Y; X-ray; 1.93 A; A/B=2-1232.
DR PDB; 2C42; X-ray; 1.78 A; A/B=2-1232.
DR PDB; 2PDA; X-ray; 3.00 A; A/B=2-1232.
DR PDB; 2UZA; X-ray; 2.42 A; A/B=2-1232.
DR PDB; 7PLM; EM; 2.90 A; A/B=1-1232.
DR PDBsum; 1B0P; -.
DR PDBsum; 1KEK; -.
DR PDBsum; 2C3M; -.
DR PDBsum; 2C3O; -.
DR PDBsum; 2C3P; -.
DR PDBsum; 2C3U; -.
DR PDBsum; 2C3Y; -.
DR PDBsum; 2C42; -.
DR PDBsum; 2PDA; -.
DR PDBsum; 2UZA; -.
DR PDBsum; 7PLM; -.
DR AlphaFoldDB; P94692; -.
DR SMR; P94692; -.
DR DIP; DIP-29036N; -.
DR DrugBank; DB02410; 2-Acetyl-3-[(4-Amino-2-Methyl-5-Pyrimidinyl)Methyl]-4-Methyl-5-(4,6,6-Trihydroxy-3,5-Dioxa-4,6-Diphosphahex-1-Yl)Thiazolium Inner Salt P,P'-Dioxide.
DR DrugBank; DB01987; Cocarboxylase.
DR DrugBank; DB00507; Nitazoxanide.
DR PRIDE; P94692; -.
DR EvolutionaryTrace; P94692; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Calcium; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Electron transport; Iron; Iron-sulfur; Magnesium;
KW Metal-binding; Oxidoreductase; Pyruvate; Thiamine pyrophosphate; Transport.
FT CHAIN 1..1232
FT /note="Pyruvate:ferredoxin oxidoreductase"
FT /id="PRO_0000430800"
FT DOMAIN 680..709
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 736..767
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 1197..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:16472741"
FT BINDING 64
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578"
FT BINDING 114
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:16472741"
FT BINDING 427..431
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q2RMD6"
FT BINDING 459
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q2RMD6"
FT BINDING 560
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q2RMD6"
FT BINDING 602
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q2RMD6"
FT BINDING 689
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 692
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 695
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 699
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 745
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 748
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 751
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 755
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 812
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 815
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 817
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 840
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 840
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 962..965
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 963
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 983
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 985
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 991..996
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 991
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 993
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 1056
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 1059
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 1061
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 1063
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578, ECO:0000269|PubMed:16472741"
FT BINDING 1071
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10048931,
FT ECO:0000269|PubMed:11752578"
FT SITE 31
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000303|PubMed:10048931"
FT SITE 64
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000303|PubMed:10048931"
FT SITE 114
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000303|PubMed:10048931"
FT SITE 996
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000303|PubMed:10048931"
FT DISULFID 1195..1212
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 87..102
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 146..163
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 173..178
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 233..254
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 297..307
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1B0P"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 372..383
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 418..425
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 430..444
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 463..473
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 492..496
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 500..503
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 519..525
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 528..536
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 546..552
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 560..570
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:1KEK"
FT HELIX 576..589
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 595..612
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 620..624
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 637..641
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 643..647
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 669..672
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 679..684
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 686..688
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 694..698
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 704..709
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 711..714
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 729..731
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 735..740
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 742..744
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 750..754
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 756..759
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 761..766
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 767..769
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 771..782
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:2C3M"
FT HELIX 796..799
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 818..828
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 832..836
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 840..846
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 872..898
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 899..901
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 904..916
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 920..933
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 934..936
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 940..946
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 947..951
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 956..962
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 963..967
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 968..970
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 971..979
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 985..990
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 992..994
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 995..998
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1025..1030
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 1033..1040
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 1042..1044
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1046..1058
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 1059..1061
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 1063..1068
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1072..1074
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1080..1082
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1083..1092
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 1094..1096
FT /evidence="ECO:0007829|PDB:2C3U"
FT STRAND 1099..1101
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1103..1107
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 1112..1115
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1124..1129
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1132..1140
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1142..1168
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 1188..1191
FT /evidence="ECO:0007829|PDB:2C42"
FT TURN 1201..1203
FT /evidence="ECO:0007829|PDB:2C42"
FT STRAND 1215..1217
FT /evidence="ECO:0007829|PDB:2C42"
FT HELIX 1220..1229
FT /evidence="ECO:0007829|PDB:2C42"
SQ SEQUENCE 1232 AA; 133680 MW; 55D84F536CCFFDBF CRC64;
MGKKMMTTDG NTATAHVAYA MSEVAAIYPI TPSSTMGEEA DDWAAQGRKN IFGQTLTIRE
MQSEAGAAGA VHGALAAGAL TTTFTASQGL LLMIPNMYKI SGELLPGVFH VTARAIAAHA
LSIFGDHQDI YAARQTGFAM LASSSVQEAH DMALVAHLAA IESNVPFMHF FDGFRTSHEI
QKIEVLDYAD MASLVNQKAL AEFRAKSMNP EHPHVRGTAQ NPDIYFQGRE AANPYYLKVP
GIVAEYMQKV ASLTGRSYKL FDYVGAPDAE RVIVSMGSSC ETIEEVINHL AAKGEKIGLI
KVRLYRPFVS EAFFAALPAS AKVITVLDRT KEPGAPGDPL YLDVCSAFVE RGEAMPKILA
GRYGLGSKEF SPAMVKSVYD NMSGAKKNHF TVGIEDDVTG TSLPVDNAFA DTTPKGTIQC
QFWGLGADGT VGANKQAIKI IGDNTDLFAQ GYFSYDSKKS GGITISHLRF GEKPIQSTYL
VNRADYVACH NPAYVGIYDI LEGIKDGGTF VLNSPWSSLE DMDKHLPSGI KRTIANKKLK
FYNIDAVKIA TDVGLGGRIN MIMQTAFFKL AGVLPFEKAV DLLKKSIHKA YGKKGEKIVK
MNTDAVDQAV TSLQEFKYPD SWKDAPAETK AEPMTNEFFK NVVKPILTQQ GDKLPVSAFE
ADGRFPLGTS QFEKRGVAIN VPQWVPENCI QCNQCAFVCP HSAILPVLAK EEELVGAPAN
FTALEAKGKE LKGYKFRIQI NTLDCMGCGN CADICPPKEK ALVMQPLDTQ RDAQVPNLEY
AARIPVKSEV LPRDSLKGSQ FQEPLMEFSG ACSGCGETPY VRVITQLFGE RMFIANATGC
SSIWGASAPS MPYKTNRLGQ GPAWGNSLFE DAAEYGFGMN MSMFARRTHL ADLAAKALES
DASGDVKEAL QGWLAGKNDP IKSKEYGDKL KKLLAGQKDG LLGQIAAMSD LYTKKSVWIF
GGDGWAYDIG YGGLDHVLAS GEDVNVFVMD TEVYSNTGGQ SSKATPTGAV AKFAAAGKRT
GKKDLARMVM TYGYVYVATV SMGYSKQQFL KVLKEAESFP GPSLVIAYAT CINQGLRKGM
GKSQDVMNTA VKSGYWPLFR YDPRLAAQGK NPFQLDSKAP DGSVEEFLMA QNRFAVLDRS
FPEDAKRLRA QVAHELDVRF KELEHMAATN IFESFAPAGG KADGSVDFGE GAEFCTRDDT
PMMARPDSGE ACDQNRAGTS EQQGDLSKRT KK
