ID FADB_ECOLI Reviewed; 729 AA. AC P21177; Q2M8E9; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 2. DT 10-JUN-2026, entry version 203. DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01621}; DE Includes: DE RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=5.3.3.8 {ECO:0000255|HAMAP-Rule:MF_01621}; DE Includes: DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01621}; GN Name=fadB {ECO:0000255|HAMAP-Rule:MF_01621}; Synonyms=oldB; GN OrderedLocusNames=b3846, JW3822; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1699931; DOI=10.1128/jb.172.11.6459-6468.1990; RA Dirusso C.C.; RT "Primary sequence of the Escherichia coli fadBA operon, encoding the fatty RT acid-oxidizing multienzyme complex, indicates a high degree of homology to RT eucaryotic enzymes."; RL J. Bacteriol. 172:6459-6468(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10. RC STRAIN=K12; RX PubMed=2191949; DOI=10.1016/s0021-9258(18)86963-0; RA Yang S.-Y., Yang X.-Y.H., Healy-Louie G., Schulz H., Elzinga M.; RT "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl- RT coenzyme A thiolase from Escherichia coli and the structural organization RT of the fadAB operon."; RL J. Biol. Chem. 265:10424-10429(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=2204034; DOI=10.1093/nar/18.16.4937; RA Nakahigashi K., Inokuchi H.; RT "Nucleotide sequence of the fadA and fadB genes from Escherichia coli."; RL Nucleic Acids Res. 18:4937-4937(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1712230; DOI=10.1021/bi00241a023; RA Yang X.Y.H., Schulz H., Elzinga M., Yang S.Y.; RT "Nucleotide sequence of the promoter and fadB gene of the fadBA operon and RT primary structure of the multifunctional fatty acid oxidation protein from RT Escherichia coli."; RL Biochemistry 30:6788-6795(1991). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=1379743; DOI=10.1126/science.1379743; RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.; RT "Analysis of the Escherichia coli genome: DNA sequence of the region from RT 84.5 to 86.5 minutes."; RL Science 257:771-778(1992). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [8] RP FUNCTION, AND SUBUNIT. RX PubMed=368024; DOI=10.1128/jb.137.1.469-473.1979; RA Pramanik A., Pawar S., Antonian E., Schulz H.; RT "Five different enzymatic activities are associated with the multienzyme RT complex of fatty acid oxidation from Escherichia coli."; RL J. Bacteriol. 137:469-473(1979). RN [9] RP FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=1748662; DOI=10.1016/s0021-9258(18)54369-6; RA Smeland T.E., Cuebas D., Schulz H.; RT "Epimerization of 3-hydroxy-4-trans-decenoyl coenzyme A by a RT dehydration/hydration mechanism catalyzed by the multienzyme complex of RT fatty acid oxidation from Escherichia coli."; RL J. Biol. Chem. 266:23904-23908(1991). RN [10] RP FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, ACTIVE SITE, RP MUTAGENESIS OF GLY-116, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=8454629; DOI=10.1016/s0021-9258(18)53291-9; RA Yang S.Y., Elzinga M.; RT "Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme RT A epimerase with an active site in the amino-terminal domain of the RT multifunctional fatty acid oxidation protein from Escherichia coli."; RL J. Biol. Chem. 268:6588-6592(1993). RN [11] RP FUNCTION AS A DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, ACTIVE SITE, NAD-BINDING, AND MUTAGENESIS OF GLY-322 AND RP HIS-450. RX PubMed=8755745; DOI=10.1021/bi960374y; RA He X.Y., Yang S.Y.; RT "Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A RT dehydrogenase associated with the large alpha-subunit of the multienzyme RT complex of fatty acid oxidation from Escherichia coli."; RL Biochemistry 35:9625-9630(1996). RN [12] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [13] RP FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=12535077; DOI=10.1046/j.1365-2958.2003.03341.x; RA Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.; RT "A new Escherichia coli metabolic competency: growth on fatty acids by a RT novel anaerobic beta-oxidation pathway."; RL Mol. Microbiol. 47:793-805(2003). CC -!- FUNCTION: Involved in the aerobic and anaerobic degradation of long- CC chain fatty acids via beta-oxidation cycle. Catalyzes the formation of CC 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use CC D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. CC {ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000269|PubMed:12535077, CC ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:368024, CC ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + NADH + CC H(+); Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, CC ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, CC ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; CC Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; CC EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; CC Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; CC EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; CC EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=53 uM for crotonyl-CoA (for enoyl-CoA hydratase activity) CC {ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:8454629, CC ECO:0000269|PubMed:8755745}; CC KM=8.7 mM for L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA CC hydratase activity) {ECO:0000269|PubMed:1748662, CC ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745}; CC KM=38 mM for D-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA CC hydratase activity) {ECO:0000269|PubMed:1748662, CC ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745}; CC KM=5.8 uM for 3-cis-tetradecenoyl-CoA (for CC Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase activity) CC {ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:8454629, CC ECO:0000269|PubMed:8755745}; CC KM=69 uM for acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase CC activity) {ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:8454629, CC ECO:0000269|PubMed:8755745}; CC KM=2 uM for NADH (for 3-hydroxyacyl-CoA dehydrogenase activity) CC {ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:8454629, CC ECO:0000269|PubMed:8755745}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains CC (FadA). {ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000269|PubMed:368024}. CC -!- INDUCTION: Repressed by FadR in the absence of LCFAs (fatty acids of, CC at least, 12 carbon atoms). When LCFAs are present in the medium, they CC are converted to long-chain acyl-CoAs which bind to FadR resulting in CC its release from the DNA and thus derepression of the transcription. CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01621}. 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; M59368; AAA23750.1; -; Genomic_DNA. DR EMBL; X52837; CAB40809.1; -; Genomic_DNA. DR EMBL; M74164; AAA62777.1; -; Genomic_DNA. DR EMBL; M87049; AAA67643.1; -; Genomic_DNA. DR EMBL; U00096; AAC76849.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77457.1; -; Genomic_DNA. DR PIR; A39592; A39592. DR RefSeq; NP_418288.1; NC_000913.3. DR RefSeq; WP_000965936.1; NZ_CP009789.1. DR PDB; 6TNM; X-ray; 2.95 A; A=1-729. DR AlphaFoldDB; P21177; -. DR SASBDB; P21177; -. DR SMR; P21177; -. DR BioGRID; 4263448; 165. DR BioGRID; 852633; 1. DR ComplexPortal; CPX-3964; fadBA fatty acid oxidation complex, aerobic conditions. DR DIP; DIP-9560N; -. DR FunCoup; P21177; 282. DR IntAct; P21177; 7. DR STRING; 511145.b3846; -. DR jPOST; P21177; -. DR PaxDb; 511145-b3846; -. DR EnsemblBacteria; AAC76849; AAC76849; b3846. DR GeneID; 948336; -. DR KEGG; ecj:JW3822; -. DR KEGG; eco:b3846; -. DR KEGG; ecoc:C3026_20795; -. DR PATRIC; fig|511145.12.peg.3960; -. DR EchoBASE; EB0275; -. DR eggNOG; COG1024; Bacteria. DR eggNOG; COG1250; Bacteria. DR HOGENOM; CLU_009834_16_3_6; -. DR InParanoid; P21177; -. DR OMA; YNGAAMG; -. DR OrthoDB; 5389341at2; -. DR PhylomeDB; P21177; -. DR BioCyc; EcoCyc:FADB-MONOMER; -. DR BioCyc; MetaCyc:FADB-MONOMER; -. DR SABIO-RK; P21177; -. DR UniPathway; UPA00659; -. DR PRO; PR:P21177; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P21177; -. DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IDA:EcoCyc. DR GO; GO:0003857; F:(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity; IDA:UniProtKB. DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IEA:RHEA. DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IDA:UniProtKB. DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:UniProtKB. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB. DR GO; GO:0016509; F:long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity; IBA:GO_Central. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:ComplexPortal. DR CDD; cd06558; crotonase-like; 1. DR FunFam; 1.10.1040.50:FF:000001; Fatty acid oxidation complex subunit alpha; 1. DR FunFam; 3.90.226.10:FF:000018; Fatty acid oxidation complex subunit alpha; 1. DR FunFam; 3.40.50.720:FF:000009; Fatty oxidation complex, alpha subunit; 1. DR Gene3D; 1.10.1040.50; -; 1. DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_01621; FadB; 1. DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS. DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd. DR InterPro; IPR006108; 3HC_DH_C. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR InterPro; IPR001753; Enoyl-CoA_hydra/iso. DR InterPro; IPR050136; FA_oxidation_alpha_subunit. DR InterPro; IPR012799; FadB. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR02437; FadB; 1. DR NCBIfam; NF008727; PRK11730.1; 1. DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1. DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR Pfam; PF00725; 3HCDH; 2. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH_1; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. DR PDBsum; 6TNM; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Fatty acid metabolism; Isomerase; KW Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; KW Oxidoreductase; Reference proteome. FT CHAIN 1..729 FT /note="Fatty acid oxidation complex subunit alpha" FT /id="PRO_0000109268" FT REGION 1..189 FT /note="Enoyl-CoA hydratase/isomerase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT REGION 311..729 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT REGION 708..729 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 450 FT /note="For 3-hydroxyacyl-CoA dehydrogenase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621, FT ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745" FT BINDING 296 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 324 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000305" FT BINDING 343 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 400..402 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 407 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 429 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 453 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 500 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 660 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT SITE 119 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT SITE 139 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT MUTAGEN 116 FT /note="G->F: Absence of both enoyl-CoA hydratase and FT 3-hydroxyacyl-CoA epimerase activities. FT Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only FT slightly affected." FT /evidence="ECO:0000269|PubMed:8454629" FT MUTAGEN 322 FT /note="G->A: 10-fold increase in KM for NADH." FT /evidence="ECO:0000269|PubMed:8755745" FT MUTAGEN 450 FT /note="H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA FT dehydrogenase activity." FT /evidence="ECO:0000269|PubMed:8755745" FT CONFLICT 518 FT /note="A -> R (in Ref. 1; AAA23750)" FT /evidence="ECO:0000305" FT CONFLICT 664 FT /note="F -> L (in Ref. 3; CAB40809)" FT /evidence="ECO:0000305" FT CONFLICT 666 FT /note="P -> A (in Ref. 3; CAB40809)" FT /evidence="ECO:0000305" FT STRAND 6..13 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 14..16 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 17..22 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 33..46 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 54..65 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 73..76 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 81..99 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 105..109 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 116..123 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 150..158 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 160..169 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 175..181 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 190..205 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 211..215 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 226..241 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 249..260 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 266..282 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 284..306 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 307..309 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 314..319 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 323..333 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 334..336 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 346..365 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 371..378 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 381..386 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 394..398 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 404..416 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 423..426 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 433..436 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 437..439 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 443..445 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 446..450 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 455..457 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 460..465 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 471..483 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 487..492 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 495..498 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 499..515 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 520..529 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 537..544 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 546..559 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 561..563 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 571..577 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 583..586 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 587..593 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 596..598 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 601..603 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 607..615 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 624..644 FT /evidence="ECO:0007829|PDB:6TNM" FT STRAND 647..649 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 651..661 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 666..668 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 671..677 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 680..688 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 689..693 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 695..697 FT /evidence="ECO:0007829|PDB:6TNM" FT HELIX 701..706 FT /evidence="ECO:0007829|PDB:6TNM" FT TURN 707..710 FT /evidence="ECO:0007829|PDB:6TNM" SQ SEQUENCE 729 AA; 79594 MW; 6F1055E402F6B129 CRC64; MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS DLKGLLLRSN KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTIAAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK IGLVDGVVKA EKLVEGAKAV LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV AQTAGKHYPA PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT LGMTEAAKLL NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDIVVEAV VENPKVKKAV LAETEQKVRQ DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT PAEADMALVY GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA RPVGDLKTA //