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 22-FEB-2023, entry version 117. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; 9807883at2; -. 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:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.40.110.20; -; 1. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1. 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 PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1. DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1. 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; Acyl-CoA dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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 //