FADE5_MYCS2
ID FADE5_MYCS2 Reviewed; 611 AA.
AC Q3L887; A0QPI1; I7FWC0;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Broad-specificity linear acyl-CoA dehydrogenase FadE5 {ECO:0000305};
DE AltName: Full=Long-chain-acyl-CoA dehydrogenase {ECO:0000305};
DE EC=1.3.8.8 {ECO:0000269|PubMed:32601219};
DE AltName: Full=Medium-chain-acyl-CoA dehydrogenase {ECO:0000305};
DE EC=1.3.8.7 {ECO:0000269|PubMed:32601219};
DE AltName: Full=Short-chain-acyl-CoA dehydrogenase {ECO:0000305};
DE EC=1.3.8.1 {ECO:0000269|PubMed:32601219};
GN Name=fadE5 {ECO:0000303|PubMed:32601219};
GN OrderedLocusNames=MSMEG_0406 {ECO:0000312|EMBL:ABK75628.1},
GN MSMEI_0396 {ECO:0000312|EMBL:AFP36877.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=16194230; DOI=10.1111/j.1365-2958.2005.04847.x;
RA Sonden B., Kocincova D., Deshayes C., Euphrasie D., Rhayat L., Laval F.,
RA Frehel C., Daffe M., Etienne G., Reyrat J.M.;
RT "Gap, a mycobacterial specific integral membrane protein, is required for
RT glycolipid transport to the cell surface.";
RL Mol. Microbiol. 58:426-440(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5] {ECO:0007744|PDB:6KPT, ECO:0007744|PDB:6KRI, ECO:0007744|PDB:6KS9, ECO:0007744|PDB:6KSA, ECO:0007744|PDB:6KSB, ECO:0007744|PDB:6LPY, ECO:0007744|PDB:6LQ0, ECO:0007744|PDB:6LQ1, ECO:0007744|PDB:6LQ2, ECO:0007744|PDB:6LQ3, ECO:0007744|PDB:6LQ4}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH FAD AND
RP MUTANT ALA-447 IN COMPLEXES WITH FAD AND LINEAR ACYL-COA SUBSTRATES,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, SUBUNIT, DISRUPTION PHENOTYPE, ACTIVE SITE, AND MUTAGENESIS OF
RP GLU-447.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=32601219; DOI=10.1073/pnas.2002835117;
RA Chen X., Chen J., Yan B., Zhang W., Guddat L.W., Liu X., Rao Z.;
RT "Structural basis for the broad substrate specificity of two acyl-CoA
RT dehydrogenases FadE5 from mycobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:16324-16332(2020).
CC -!- FUNCTION: Acyl-CoA dehydrogenase that exhibits broad specificity for
CC linear acyl-CoA substrates, with a preference for long-chain
CC substrates. {ECO:0000269|PubMed:32601219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:87487,
CC ChEBI:CHEBI:87488; EC=1.3.8.1;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:71412;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61526;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:32601219};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=285.9 uM for butanoyl-CoA {ECO:0000269|PubMed:32601219};
CC Note=kcat is 0.53 sec(-1) with butanoyl-CoA as substrate.
CC {ECO:0000269|PubMed:32601219};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:32601219}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:32601219}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene does not affect the growth
CC rate, but mutant shows decreased resistance to ethambutol and
CC streptomycin. {ECO:0000269|PubMed:32601219}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AY439015; AAU04876.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK75628.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36877.1; -; Genomic_DNA.
DR RefSeq; WP_011726920.1; NZ_SIJM01000040.1.
DR RefSeq; YP_884819.1; NC_008596.1.
DR PDB; 6KPT; X-ray; 1.96 A; A/B=1-611.
DR PDB; 6KRI; X-ray; 1.60 A; A/B=1-611.
DR PDB; 6KS9; X-ray; 2.00 A; A/B=1-611.
DR PDB; 6KSA; X-ray; 1.77 A; A/B=1-611.
DR PDB; 6KSB; X-ray; 1.97 A; A/B=1-611.
DR PDB; 6LPY; X-ray; 1.90 A; A/B=1-611.
DR PDB; 6LQ0; X-ray; 2.20 A; A/B=1-611.
DR PDB; 6LQ1; X-ray; 2.80 A; A/B=1-611.
DR PDB; 6LQ2; X-ray; 1.90 A; A/B=1-611.
DR PDB; 6LQ3; X-ray; 2.50 A; A/B=1-611.
DR PDB; 6LQ4; X-ray; 2.40 A; A/B=1-611.
DR PDB; 6LQ5; X-ray; 1.90 A; A/B=1-611.
DR PDB; 6LQ6; X-ray; 2.00 A; A/B=1-611.
DR PDB; 6LQ7; X-ray; 1.90 A; A/B=1-611.
DR PDB; 6LQ8; X-ray; 1.85 A; A/B=1-611.
DR PDBsum; 6KPT; -.
DR PDBsum; 6KRI; -.
DR PDBsum; 6KS9; -.
DR PDBsum; 6KSA; -.
DR PDBsum; 6KSB; -.
DR PDBsum; 6LPY; -.
DR PDBsum; 6LQ0; -.
DR PDBsum; 6LQ1; -.
DR PDBsum; 6LQ2; -.
DR PDBsum; 6LQ3; -.
DR PDBsum; 6LQ4; -.
DR PDBsum; 6LQ5; -.
DR PDBsum; 6LQ6; -.
DR PDBsum; 6LQ7; -.
DR PDBsum; 6LQ8; -.
DR AlphaFoldDB; Q3L887; -.
DR SMR; Q3L887; -.
DR STRING; 246196.MSMEI_0396; -.
DR PRIDE; Q3L887; -.
DR EnsemblBacteria; ABK75628; ABK75628; MSMEG_0406.
DR EnsemblBacteria; AFP36877; AFP36877; MSMEI_0396.
DR GeneID; 66738592; -.
DR KEGG; msg:MSMEI_0396; -.
DR KEGG; msm:MSMEG_0406; -.
DR PATRIC; fig|246196.19.peg.402; -.
DR eggNOG; COG1960; Bacteria.
DR OMA; MWAKMAK; -.
DR OrthoDB; 357522at2; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF12418; AcylCoA_DH_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..611
FT /note="Broad-specificity linear acyl-CoA dehydrogenase
FT FadE5"
FT /id="PRO_0000452497"
FT ACT_SITE 447
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:32601219"
FT BINDING 162..165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 171
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 198
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 224..225
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 301
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 338
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 420..424
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 447
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 449
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 456
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 460..461
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT MUTAGEN 447
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:32601219"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 35..50
FT /evidence="ECO:0007829|PDB:6KRI"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6KRI"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6LQ0"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6LQ0"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:6KRI"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 289..325
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:6KRI"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 349..373
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 389..421
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 433..441
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:6KRI"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 450..459
FT /evidence="ECO:0007829|PDB:6KRI"
FT TURN 460..467
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 468..481
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:6KPT"
FT HELIX 491..517
FT /evidence="ECO:0007829|PDB:6KRI"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 525..560
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 565..584
FT /evidence="ECO:0007829|PDB:6KRI"
FT TURN 585..587
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 588..597
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:6KRI"
FT HELIX 608..610
FT /evidence="ECO:0007829|PDB:6KRI"
SQ SEQUENCE 611 AA; 66532 MW; 41D1ABFE887E0206 CRC64;
MSHYKSNVRD QVFNLFEVFG VDKVLGADKF SDLDADTARE MLTEIARLAE GPIAESFVEG
DRNPPVFDPE THTVTLPEGF KKSMRALFDG GWDKVGLAEH LGGIPMPRAL QWALIEHILG
ANPAAYMYAM GPGMSEIFYN NGTDEQKKWA TIAAERGWGA TMVLTEPDAG SDVGAGRTKA
VQQPDGTWHI EGVKRFITSA DSDDLFENIM HLVLARPEGA GPGTKGLSLF FVPKFHFDHE
TGEIGERNGV FVTNVEHKMG LKVSATCELS LGQHGIPAVG WLVGEVHNGI AQMFDVIEQA
RMMVGTKAIA TLSTGYLNAL EYAKERVQGA DMTQMTDKTA PRVTITHHPD VRRSLMTQKA
YAEGLRAIYL YTATFQDAEV AQAVHGVDGD LAARVNDLLL PIVKGFGSET AYAKLTESLQ
TLGGSGFLQD YPIEQYIRDS KIDSLYEGTT AIQAQDFFFR KIIRDKGQAL AYVAGEIEQF
IKNENGNGRL KTERELLATA LADVQGMAAS LTGYLMAAQE DAASIYKVGL GSVRFLMAVG
DLLSGWLLAR QAAVAIEKLD AGATGADKSF YEGKIAAASF FAKNMLPLLT STRQIIENLD
NDVMELDEAA F
