CP124_MYCTU
ID CP124_MYCTU Reviewed; 428 AA.
AC P9WPP3; L0TBS5; P0A516; Q50696;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Methyl-branched lipid omega-hydroxylase {ECO:0000303|PubMed:19933331};
DE EC=1.14.15.14 {ECO:0000269|PubMed:19933331};
DE AltName: Full=Cholest-4-en-3-one C26-monooxygenase {ECO:0000303|PubMed:20843794};
DE AltName: Full=Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] {ECO:0000303|PubMed:20843794};
DE AltName: Full=Cholesterol C26-monooxygenase {ECO:0000303|PubMed:20843794};
DE AltName: Full=Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming] {ECO:0000303|PubMed:20843794};
DE AltName: Full=Cytochrome P450 124 {ECO:0000303|PubMed:19933331};
DE AltName: Full=Steroid C26-monooxygenase {ECO:0000303|PubMed:20843794};
DE EC=1.14.15.28 {ECO:0000269|PubMed:20843794};
DE AltName: Full=Steroid C27-monooxygenase {ECO:0000303|PubMed:20843794};
GN Name=cyp124; OrderedLocusNames=Rv2266; ORFNames=MTCY339.44c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=20843794; DOI=10.1074/jbc.m110.161117;
RA Johnston J.B., Ouellet H., Ortiz de Montellano P.R.;
RT "Functional redundancy of steroid C26-monooxygenase activity in
RT Mycobacterium tuberculosis revealed by biochemical and genetic analyses.";
RL J. Biol. Chem. 285:36352-36360(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH
RP (3R,7S,11S)-3,7,11,15-TETRAMETHYLHEXADECANOIC ACID (PHYTANIC ACID) AND
RP HEME, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=H37Rv;
RX PubMed=19933331; DOI=10.1073/pnas.0907398106;
RA Johnston J.B., Kells P.M., Podust L.M., Ortiz de Montellano P.R.;
RT "Biochemical and structural characterization of CYP124: a methyl-branched
RT lipid omega-hydroxylase from Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20687-20692(2009).
CC -!- FUNCTION: Primarily hydroxylates the omega-carbon of a number of
CC methyl-branched lipids, including (2E,6E)-farnesol, phytanate,
CC geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl diphosphate
CC (PubMed:19933331). Also catalyzes the sequential oxidation of the
CC terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-
CC en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to
CC finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate
CC (PubMed:20843794). Cyp124 catalyzes preferentially the oxidation of
CC (25R)-26-hydroxycholest-4-en-3-one diastereomer (PubMed:20843794). Also
CC able to sequentially oxidize cholesterol itself, not only cholest-4-en-
CC 3-one (PubMed:20843794). {ECO:0000269|PubMed:19933331,
CC ECO:0000269|PubMed:20843794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a methyl-branched lipid + O2 + 2 reduced ferredoxin [iron-
CC sulfur] cluster + 2 H(+) = an omega-hydroxy-methyl-branched lipid +
CC H2O + 2 oxidized ferredoxin [iron-sulfur] cluster.; EC=1.14.15.14;
CC Evidence={ECO:0000269|PubMed:19933331};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-
CC [ferredoxin] = (25R)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized
CC [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:49996, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:71570; EC=1.14.15.28;
CC Evidence={ECO:0000269|PubMed:20843794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-methylhexadecanoate + H(+) + NADPH + O2 = H2O + NADP(+) +
CC omega-hydroxy-15-methyl-hexadecanoate; Xref=Rhea:RHEA:43956,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:70838,
CC ChEBI:CHEBI:83914; Evidence={ECO:0000269|PubMed:19933331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43957;
CC Evidence={ECO:0000269|PubMed:19933331};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,7,11,15-tetramethylhexadecanoate + H(+) + NADPH + O2 = H2O +
CC NADP(+) + omega-hydroxy-3,7,11,15-tetramethyl-hexadecanoate;
CC Xref=Rhea:RHEA:43952, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:37257, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:83916;
CC Evidence={ECO:0000269|PubMed:19933331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43953;
CC Evidence={ECO:0000269|PubMed:19933331};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H(+) + NADPH + O2 = (2E,6E)-
CC omega-hydroxy-farnesyl diphosphate + H2O + NADP(+);
CC Xref=Rhea:RHEA:43988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83958, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:19933331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43989;
CC Evidence={ECO:0000269|PubMed:19933331};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesol + H(+) + NADPH + O2 = (2E,6E)-omega-hydroxy-
CC farnesol + H2O + NADP(+); Xref=Rhea:RHEA:43984, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16619,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83951;
CC Evidence={ECO:0000269|PubMed:19933331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43985;
CC Evidence={ECO:0000269|PubMed:19933331};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeraniol + H(+) + NADPH + O2 = 16-hydroxy-
CC (2E,6E,10E)-geranylgeraniol + H2O + NADP(+); Xref=Rhea:RHEA:43992,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:46762, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83953; Evidence={ECO:0000269|PubMed:19933331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43993;
CC Evidence={ECO:0000269|PubMed:19933331};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeraniol + H(+) + 2 NADPH + 2 O2 =
CC (2E,6E,10E)-geranylgeranate + 3 H2O + 2 NADP(+);
CC Xref=Rhea:RHEA:46108, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:46762, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:83952;
CC Evidence={ECO:0000269|PubMed:19933331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46109;
CC Evidence={ECO:0000269|PubMed:19933331};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholest-4-en-3-one + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = (25R)-3-oxocholest-4-en-26-ol + H2O + 2 oxidized [2Fe-
CC 2S]-[ferredoxin]; Xref=Rhea:RHEA:43912, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:83861;
CC Evidence={ECO:0000269|PubMed:20843794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43913;
CC Evidence={ECO:0000269|PubMed:20843794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + H(+) + NADPH + O2 = 26-hydroxycholesterol + H2O
CC + NADP(+); Xref=Rhea:RHEA:43836, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:17703, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:20843794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43837;
CC Evidence={ECO:0000269|PubMed:20843794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=26-hydroxycholesterol + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = (3beta)-hydroxy-cholest-5-en-26-al + 2 H2O + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:43840, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17703,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:84145;
CC Evidence={ECO:0000269|PubMed:20843794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43841;
CC Evidence={ECO:0000269|PubMed:20843794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3beta)-hydroxy-cholest-5-en-26-al + NADPH + O2 = (3beta)-
CC hydroxy-cholest-5-en-26-oate + H2O + NADP(+); Xref=Rhea:RHEA:43844,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:84145, ChEBI:CHEBI:84146;
CC Evidence={ECO:0000269|PubMed:20843794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43845;
CC Evidence={ECO:0000269|PubMed:20843794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3-oxocholest-4-en-26-ol + 2 H(+) + O2 + 2 reduced [2Fe-
CC 2S]-[ferredoxin] = (25R)-3-oxocholest-4-en-26-al + 2 H2O + 2 oxidized
CC [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:43916, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:83861, ChEBI:CHEBI:83862;
CC Evidence={ECO:0000269|PubMed:20843794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43917;
CC Evidence={ECO:0000269|PubMed:20843794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3-oxocholest-4-en-26-al + H(+) + O2 + 2 reduced [2Fe-
CC 2S]-[ferredoxin] = (25R)-3-oxocholest-4-en-26-oate + H2O + 2 oxidized
CC [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:43920, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:71570, ChEBI:CHEBI:83862;
CC Evidence={ECO:0000269|PubMed:20843794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43921;
CC Evidence={ECO:0000269|PubMed:20843794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25S)-3-oxocholest-4-en-26-ol + 2 H(+) + O2 + 2 reduced [2Fe-
CC 2S]-[ferredoxin] = (25S)-3-oxocholest-4-en-26-al + 2 H2O + 2 oxidized
CC [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:51568, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:83860, ChEBI:CHEBI:83863;
CC Evidence={ECO:0000269|PubMed:20843794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51569;
CC Evidence={ECO:0000269|PubMed:20843794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25S)-3-oxocholest-4-en-26-al + H(+) + O2 + 2 reduced [2Fe-
CC 2S]-[ferredoxin] = (25S)-3-oxocholest-4-en-26-oate + H2O + 2 oxidized
CC [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:51572, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:71541, ChEBI:CHEBI:83863;
CC Evidence={ECO:0000269|PubMed:20843794};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51573;
CC Evidence={ECO:0000269|PubMed:20843794};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:19933331, ECO:0000269|PubMed:20843794};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 uM for 15-methylpalmitate {ECO:0000269|PubMed:19933331};
CC KM=11.6 uM for cholesterol {ECO:0000269|PubMed:20843794};
CC KM=20.8 uM for cholest-4-en-3-one {ECO:0000269|PubMed:20843794};
CC KM=54 uM for phytanate {ECO:0000269|PubMed:19933331};
CC KM=36 uM for (2E,6E)-farnesol {ECO:0000269|PubMed:19933331};
CC KM=32 uM for geranylgeraniol {ECO:0000269|PubMed:19933331};
CC Note=kcat is 11.7 min(-1) for cholesterol as substrate. kcat is 1.5
CC min(-1) for cholest-4-en-3-one as substrate.
CC {ECO:0000269|PubMed:20843794};
CC -!- PATHWAY: Lipid metabolism; branched-chain fatty acid metabolism.
CC {ECO:0000305|PubMed:19933331}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45047.1; -; Genomic_DNA.
DR PIR; F70729; F70729.
DR RefSeq; NP_216782.1; NC_000962.3.
DR RefSeq; WP_003411654.1; NZ_NVQJ01000008.1.
DR PDB; 2WM4; X-ray; 2.11 A; A=1-428.
DR PDB; 2WM5; X-ray; 1.50 A; A=1-428.
DR PDB; 6T0F; X-ray; 1.65 A; A/B/C/D=1-428.
DR PDB; 6T0G; X-ray; 1.30 A; A=1-428.
DR PDB; 6T0H; X-ray; 1.18 A; A=1-428.
DR PDB; 6T0J; X-ray; 1.25 A; A=1-428.
DR PDB; 6T0K; X-ray; 1.18 A; A=1-428.
DR PDB; 6T0L; X-ray; 1.80 A; A=1-428.
DR PDBsum; 2WM4; -.
DR PDBsum; 2WM5; -.
DR PDBsum; 6T0F; -.
DR PDBsum; 6T0G; -.
DR PDBsum; 6T0H; -.
DR PDBsum; 6T0J; -.
DR PDBsum; 6T0K; -.
DR PDBsum; 6T0L; -.
DR AlphaFoldDB; P9WPP3; -.
DR SMR; P9WPP3; -.
DR STRING; 83332.Rv2266; -.
DR SwissLipids; SLP:000001010; -.
DR PaxDb; P9WPP3; -.
DR DNASU; 887763; -.
DR GeneID; 45426248; -.
DR GeneID; 887763; -.
DR KEGG; mtu:Rv2266; -.
DR TubercuList; Rv2266; -.
DR eggNOG; COG2124; Bacteria.
DR OMA; DKVTLWY; -.
DR PhylomeDB; P9WPP3; -.
DR BioCyc; MetaCyc:G185E-6483-MON; -.
DR BRENDA; 1.14.15.14; 3445.
DR UniPathway; UPA01022; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0031073; F:cholesterol 26-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0006707; P:cholesterol catabolic process; IBA:GO_Central.
DR GO; GO:0010430; P:fatty acid omega-oxidation; IDA:MTBBASE.
DR GO; GO:0097089; P:methyl-branched fatty acid metabolic process; IDA:MTBBASE.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 2.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid metabolism; Heme; Iron; Lipid metabolism;
KW Metal-binding; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..428
FT /note="Methyl-branched lipid omega-hydroxylase"
FT /id="PRO_0000052278"
FT BINDING 379
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:19933331,
FT ECO:0007744|PDB:2WM4, ECO:0007744|PDB:2WM5"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:6T0H"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 138..154
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:6T0H"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:6T0H"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 209..232
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:2WM4"
FT HELIX 254..269
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 297..312
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:6T0H"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6T0K"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6T0H"
FT HELIX 382..399
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6T0H"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:6T0H"
SQ SEQUENCE 428 AA; 47825 MW; 76B1F3C5AE348591 CRC64;
MGLNTAIATR VNGTPPPEVP IADIELGSLD FWALDDDVRD GAFATLRREA PISFWPTIEL
PGFVAGNGHW ALTKYDDVFY ASRHPDIFSS YPNITINDQT PELAEYFGSM IVLDDPRHQR
LRSIVSRAFT PKVVARIEAA VRDRAHRLVS SMIANNPDRQ ADLVSELAGP LPLQIICDMM
GIPKADHQRI FHWTNVILGF GDPDLATDFD EFMQVSADIG AYATALAEDR RVNHHDDLTS
SLVEAEVDGE RLSSREIASF FILLVVAGNE TTRNAITHGV LALSRYPEQR DRWWSDFDGL
APTAVEEIVR WASPVVYMRR TLTQDIELRG TKMAAGDKVS LWYCSANRDE SKFADPWTFD
LARNPNPHLG FGGGGAHFCL GANLARREIR VAFDELRRQM PDVVATEEPA RLLSQFIHGI
KTLPVTWS
