PIKC_STRVZ
ID PIKC_STRVZ Reviewed; 416 AA.
AC O87605;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cytochrome P450 monooxygenase PikC {ECO:0000303|PubMed:9831532};
DE EC=1.14.15.33 {ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
DE AltName: Full=Cytochrome P450 monooxygenase PicK {ECO:0000303|PubMed:9778370};
DE AltName: Full=Narbomycin C-12 hydroxylase {ECO:0000303|PubMed:9778370};
DE AltName: Full=Pikromycin synthase CYP107L1;
GN Name=pikC {ECO:0000303|PubMed:9770448, ECO:0000303|PubMed:9831532};
GN Synonyms=picK {ECO:0000303|PubMed:9778370};
OS Streptomyces venezuelae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=54571 {ECO:0000312|EMBL:AAC64105.1};
RN [1] {ECO:0000312|EMBL:AAC64105.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140
RC {ECO:0000303|PubMed:9778370};
RX PubMed=9778370; DOI=10.1021/bi981699c;
RA Betlach M.C., Kealey J.T., Ashley G.W., McDaniel R.;
RT "Characterization of the macrolide P-450 hydroxylase from Streptomyces
RT venezuelae which converts narbomycin to picromycin.";
RL Biochemistry 37:14937-14942(1998).
RN [2] {ECO:0000312|EMBL:AAC68886.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP PATHWAY, DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140
RC {ECO:0000303|PubMed:9831532};
RX PubMed=9831532; DOI=10.1016/s1074-5521(98)90293-9;
RA Xue Y., Wilson D., Zhao L., Liu H., Sherman D.H.;
RT "Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the
RT pikC-encoded cytochrome P450 in Streptomyces venezuelae.";
RL Chem. Biol. 5:661-667(1998).
RN [3] {ECO:0000312|EMBL:AAC68886.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140
RC {ECO:0000303|PubMed:9770448};
RX PubMed=9770448; DOI=10.1073/pnas.95.21.12111;
RA Xue Y., Zhao L., Liu H.W., Sherman D.H.;
RT "A gene cluster for macrolide antibiotic biosynthesis in Streptomyces
RT venezuelae: architecture of metabolic diversity.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME; YC-17 AND
RP NARBOMYCIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND
RP MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94.
RX PubMed=16825192; DOI=10.1074/jbc.m605478200;
RA Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R.,
RA Podust L.M.;
RT "The structural basis for substrate anchoring, active site selectivity, and
RT product formation by P450 PikC from Streptomyces venezuelae.";
RL J. Biol. Chem. 281:26289-26297(2006).
RN [5] {ECO:0000312|PDB:2VZ7, ECO:0000312|PDB:2VZM}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEXES WITH
RP HEME; NARBOMYCIN AND YC-17, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP PATHWAY, AND MUTAGENESIS OF ASP-50; GLU-85 AND GLU-94.
RX PubMed=19124459; DOI=10.1074/jbc.m807592200;
RA Li S., Ouellet H., Sherman D.H., Podust L.M.;
RT "Analysis of transient and catalytic desosamine-binding pockets in
RT cytochrome P-450 PikC from Streptomyces venezuelae.";
RL J. Biol. Chem. 284:5723-5730(2009).
RN [6] {ECO:0000312|PDB:2WHW, ECO:0000312|PDB:2WI9}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RX PubMed=19833867; DOI=10.1073/pnas.0907203106;
RA Li S., Chaulagain M.R., Knauff A.R., Podust L.M., Montgomery J.,
RA Sherman D.H.;
RT "Selective oxidation of carbolide C-H bonds by an engineered macrolide P450
RT mono-oxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18463-18468(2009).
RN [7] {ECO:0000312|PDB:3ZK5, ECO:0000312|PDB:4B7S}
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF MUTANT ASN-50 IN COMPLEX WITH
RP HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RX PubMed=24627965; DOI=10.1021/ja5016052;
RA Negretti S., Narayan A.R., Chiou K.C., Kells P.M., Stachowski J.L.,
RA Hansen D.A., Podust L.M., Montgomery J., Sherman D.H.;
RT "Directing group-controlled regioselectivity in an enzymatic C-H bond
RT oxygenation.";
RL J. Am. Chem. Soc. 136:4901-4904(2014).
CC -!- FUNCTION: Catalyzes the hydroxylation of narbomycin to give rise to
CC pikromycin, and of 10-deoxymethymycin (YC-17) to give rise to
CC methymycin and neomethymycin during macrolide antibiotic biosynthesis.
CC In addition, produces low amounts of neopicromycin, novapikromycin and
CC novamethymycin. Requires the participation of a ferredoxin and a
CC ferredoxin reductase for the transfer of electrons from NADPH to the
CC monooxygenase. {ECO:0000269|PubMed:16825192,
CC ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867,
CC ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9778370,
CC ECO:0000269|PubMed:9831532}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + narbomycin + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC H2O + 2 oxidized [2Fe-2S]-[ferredoxin] + pikromycin;
CC Xref=Rhea:RHEA:39887, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:76800,
CC ChEBI:CHEBI:76801; EC=1.14.15.33;
CC Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459,
CC ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965,
CC ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + narbomycin + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC H2O + neopikromycin + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:40531, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:76801,
CC ChEBI:CHEBI:77350; EC=1.14.15.33;
CC Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459,
CC ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965,
CC ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H(+) + narbomycin + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] =
CC 2 H2O + novapikromycin + 4 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:40535, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:76801,
CC ChEBI:CHEBI:77351; EC=1.14.15.33;
CC Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459,
CC ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965,
CC ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=10-deoxymethymycin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = H2O + methymycin + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:40539, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:63307,
CC ChEBI:CHEBI:77352; EC=1.14.15.33;
CC Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459,
CC ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965,
CC ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=10-deoxymethymycin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = H2O + neomethymycin + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:40543, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:63307,
CC ChEBI:CHEBI:77353; EC=1.14.15.33;
CC Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459,
CC ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965,
CC ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=10-deoxymethymycin + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-
CC [ferredoxin] = 2 H2O + novamethymycin + 4 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:40547, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:63307,
CC ChEBI:CHEBI:77354; EC=1.14.15.33;
CC Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459,
CC ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965,
CC ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459,
CC ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965,
CC ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for narbomycin {ECO:0000269|PubMed:9778370};
CC KM=20.4 uM for 10-deoxymethymycin {ECO:0000269|PubMed:9831532};
CC KM=44 uM for narbomycin {ECO:0000269|PubMed:9831532};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:16825192,
CC ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867,
CC ECO:0000269|PubMed:24627965, ECO:0000269|PubMed:9770448,
CC ECO:0000269|PubMed:9778370, ECO:0000269|PubMed:9831532}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of methymycin,
CC neomethymycin and pikromycin and leads to the accumulation of their
CC precursors. {ECO:0000269|PubMed:9770448, ECO:0000269|PubMed:9831532}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000255|RuleBase:RU000461, ECO:0000303|PubMed:9778370,
CC ECO:0000303|PubMed:9831532, ECO:0000305}.
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DR EMBL; AF087022; AAC64105.1; -; Genomic_DNA.
DR EMBL; AF079139; AAC68886.1; -; Genomic_DNA.
DR PDB; 2BVJ; X-ray; 2.10 A; A/B=1-416.
DR PDB; 2C6H; X-ray; 2.35 A; A/B=1-416.
DR PDB; 2C7X; X-ray; 1.75 A; A=1-416.
DR PDB; 2CA0; X-ray; 2.85 A; A/B=1-416.
DR PDB; 2CD8; X-ray; 1.70 A; A/B=1-416.
DR PDB; 2VZ7; X-ray; 3.20 A; A/B=1-416.
DR PDB; 2VZM; X-ray; 1.85 A; A/B=1-416.
DR PDB; 2WHW; X-ray; 2.20 A; A/B=1-416.
DR PDB; 2WI9; X-ray; 2.00 A; A/B=1-416.
DR PDB; 3ZK5; X-ray; 1.89 A; A/B=1-416.
DR PDB; 3ZPI; X-ray; 1.63 A; A/B=1-416.
DR PDB; 4B7D; X-ray; 1.89 A; A/B=1-416.
DR PDB; 4B7S; X-ray; 1.84 A; A/B=1-416.
DR PDB; 4BF4; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-416.
DR PDB; 4UMZ; X-ray; 2.32 A; A/B=1-416.
DR PDBsum; 2BVJ; -.
DR PDBsum; 2C6H; -.
DR PDBsum; 2C7X; -.
DR PDBsum; 2CA0; -.
DR PDBsum; 2CD8; -.
DR PDBsum; 2VZ7; -.
DR PDBsum; 2VZM; -.
DR PDBsum; 2WHW; -.
DR PDBsum; 2WI9; -.
DR PDBsum; 3ZK5; -.
DR PDBsum; 3ZPI; -.
DR PDBsum; 4B7D; -.
DR PDBsum; 4B7S; -.
DR PDBsum; 4BF4; -.
DR PDBsum; 4UMZ; -.
DR AlphaFoldDB; O87605; -.
DR SMR; O87605; -.
DR KEGG; ag:AAC68886; -.
DR BioCyc; MetaCyc:MON-18405; -.
DR BRENDA; 1.14.15.33; 6106.
DR EvolutionaryTrace; O87605; -.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Heme; Iron; Metal-binding;
KW Monooxygenase; Oxidoreductase.
FT CHAIN 1..416
FT /note="Cytochrome P450 monooxygenase PikC"
FT /id="PRO_0000430718"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16825192,
FT ECO:0000269|PubMed:19124459"
FT BINDING 187..191
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16825192,
FT ECO:0000269|PubMed:19124459"
FT BINDING 238..246
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16825192,
FT ECO:0000269|PubMed:19124459"
FT BINDING 354
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:16825192,
FT ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867,
FT ECO:0000269|PubMed:24627965, ECO:0000312|PDB:2C6H,
FT ECO:0000312|PDB:2C7X, ECO:0000312|PDB:2CA0,
FT ECO:0000312|PDB:2CD8, ECO:0000312|PDB:2VZ7,
FT ECO:0000312|PDB:2VZM, ECO:0000312|PDB:2WHW,
FT ECO:0000312|PDB:2WI9, ECO:0000312|PDB:3ZK5,
FT ECO:0000312|PDB:4B7D, ECO:0000312|PDB:4B7S,
FT ECO:0000312|PDB:4BF4"
FT MUTAGEN 50
FT /note="D->A: Mildly reduces activity with YC-17 and
FT narbomycin."
FT /evidence="ECO:0000269|PubMed:16825192"
FT MUTAGEN 50
FT /note="D->N: Increases affinity for narbomycin and YC-17.
FT Mildly increases activity YC-17 and narbomycin."
FT /evidence="ECO:0000269|PubMed:16825192,
FT ECO:0000269|PubMed:19124459"
FT MUTAGEN 85
FT /note="E->A: Strongly reduces activity with narbomycin, but
FT has only minor effect on activity with YC-17. Loss of
FT activity with YC-17 and narbomycin; when associated with A-
FT 94."
FT /evidence="ECO:0000269|PubMed:16825192"
FT MUTAGEN 85
FT /note="E->Q: Reduces affinity for narbomycin and YC-17.
FT Strongly reduces activity with narbomycin and YC-17."
FT /evidence="ECO:0000269|PubMed:16825192,
FT ECO:0000269|PubMed:19124459"
FT MUTAGEN 94
FT /note="E->A: Strongly reduces activity with YC-17, but has
FT only minor effect on activity with narbomycin. Loss of
FT activity with YC-17 and narbomycin; when associated with A-
FT 85."
FT /evidence="ECO:0000269|PubMed:16825192"
FT MUTAGEN 94
FT /note="E->Q: Strongly reduces affinity for narbomycin and
FT YC-17. Strongly reduces activity with narbomycin and YC-
FT 17."
FT /evidence="ECO:0000269|PubMed:16825192,
FT ECO:0000269|PubMed:19124459"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2CA0"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2VZ7"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:3ZPI"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 184..205
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:3ZPI"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 230..243
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:3ZPI"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:3ZPI"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:2CA0"
FT HELIX 357..374
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2C7X"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:3ZPI"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2C7X"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:3ZPI"
SQ SEQUENCE 416 AA; 46038 MW; B7392C742045F06B CRC64;
MRRTQQGTTA SPPVLDLGAL GQDFAADPYP TYARLRAEGP AHRVRTPEGD EVWLVVGYDR
ARAVLADPRF SKDWRNSTTP LTEAEAALNH NMLESDPPRH TRLRKLVARE FTMRRVELLR
PRVQEIVDGL VDAMLAAPDG RADLMESLAW PLPITVISEL LGVPEPDRAA FRVWTDAFVF
PDDPAQAQTA MAEMSGYLSR LIDSKRGQDG EDLLSALVRT SDEDGSRLTS EELLGMAHIL
LVAGHETTVN LIANGMYALL SHPDQLAALR ADMTLLDGAV EEMLRYEGPV ESATYRFPVE
PVDLDGTVIP AGDTVLVVLA DAHRTPERFP DPHRFDIRRD TAGHLAFGHG IHFCIGAPLA
RLEARIAVRA LLERCPDLAL DVSPGELVWY PNPMIRGLKA LPIRWRRGRE AGRRTG
