ID ACNB_ECOLI Reviewed; 865 AA. AC P36683; P36648; P75652; Q59382; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 3. DT 02-SEP-2026, entry version 207. DE RecName: Full=Aconitate hydratase B {ECO:0000303|PubMed:8000525}; DE Short=ACN {ECO:0000303|PubMed:8000525}; DE Short=Aconitase {ECO:0000303|PubMed:8000525}; DE EC=4.2.1.3 {ECO:0000269|PubMed:10585860}; DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000305|PubMed:12473114}; DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000305|PubMed:12473114}; DE AltName: Full=2-methyl-cis-aconitate hydratase {ECO:0000303|PubMed:12473114}; DE EC=4.2.1.99 {ECO:0000269|PubMed:12473114}; DE AltName: Full=Iron-responsive protein-like {ECO:0000305|PubMed:10589714}; DE Short=IRP-like {ECO:0000305|PubMed:10589714}; DE AltName: Full=RNA-binding protein {ECO:0000303|PubMed:10589714}; GN Name=acnB {ECO:0000303|PubMed:8000525}; Synonyms=yacI, yacJ; GN OrderedLocusNames=b0118, JW0114; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8202364; DOI=10.1093/nar/22.9.1637; RA Fujita N., Mori H., Yura T., Ishihama A.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4- RT 4.1 min (110,917-193,643 bp) region."; RL Nucleic Acids Res. 22:1637-1639(1994). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION. 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131, PROTEIN SEQUENCE OF 1-11, RP FUNCTION, AND SUBUNIT. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8932712; DOI=10.1099/13500872-142-2-389; RA Bradbury A.J., Gruer M.J., Rudd K.E., Guest J.R.; RT "The second aconitase (AcnB) of Escherichia coli."; RL Microbiology 142:389-400(1996). RN [5] RP PROTEIN SEQUENCE OF 1-12. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [6] RP PROTEIN SEQUENCE OF 1-15, FUNCTION AS A 2-METHYL-ACONITATE HYDRATASE, RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=12473114; DOI=10.1046/j.1432-1033.2002.03336.x; RA Brock M., Maerker C., Schuetz A., Voelker U., Buckel W.; RT "Oxidation of propionate to pyruvate in Escherichia coli. Involvement of RT methylcitrate dehydratase and aconitase."; RL Eur. J. Biochem. 269:6184-6194(2002). RN [7] RP PROTEIN SEQUENCE OF 568-663, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, MAGNETIC CIRCULAR DICHROISM, AND EPR RP SPECTROSCOPY. RX PubMed=10585860; DOI=10.1042/bj3440739; RA Jordan P.A., Tang Y., Bradbury A.J., Thomson A.J., Guest J.R.; RT "Biochemical and spectroscopic characterization of Escherichia coli RT aconitases (AcnA and AcnB)."; RL Biochem. J. 344:739-746(1999). RN [8] RP FUNCTION. RX PubMed=8000525; DOI=10.1099/00221287-140-10-2531; RA Gruer M.J., Guest J.R.; RT "Two genetically-distinct and differentially-regulated aconitases (AcnA and RT AcnB) in Escherichia coli."; RL Microbiology 140:2531-2541(1994). RN [9] RP DISRUPTION PHENOTYPE. RX PubMed=9202458; DOI=10.1099/00221287-143-6-1837; RA Gruer M.J., Bradbury A.J., Guest J.R.; RT "Construction and properties of aconitase mutants of Escherichia coli."; RL Microbiology 143:1837-1846(1997). RN [10] RP FUNCTION AS A RNA-BINDING PROTEIN. RX PubMed=10589714; DOI=10.1099/00221287-145-11-3069; RA Tang Y., Guest J.R.; RT "Direct evidence for mRNA binding and post-transcriptional regulation by RT Escherichia coli aconitases."; RL Microbiology 145:3069-3079(1999). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=11932448; DOI=10.1099/00221287-148-4-1027; RA Tang Y., Quail M.A., Artymiuk P.J., Guest J.R., Green J.; RT "Escherichia coli aconitases and oxidative stress: post-transcriptional RT regulation of sodA expression."; RL Microbiology 148:1027-1037(2002). RN [12] RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-769, AND SUBUNIT. RX PubMed=15882410; DOI=10.1111/j.1365-2958.2005.04610.x; RA Tang Y., Guest J.R., Artymiuk P.J., Green J.; RT "Switching aconitase B between catalytic and regulatory modes involves RT iron-dependent dimer formation."; RL Mol. Microbiol. 56:1149-1158(2005). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR AND THE RP SUBSTRATE ANALOGS, COFACTOR, AND SUBUNIT. RX PubMed=11992126; DOI=10.1038/nsb801; RA Williams C.H. Jr., Stillman T.J., Barynin V.V., Sedelnikova S.E., Tang Y., RA Green J., Guest J.R., Artymiuk P.J.; RT "E. coli aconitase B structure reveals a HEAT-like domain with implications RT for protein-protein recognition."; RL Nat. Struct. Biol. 9:447-452(2002). CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) CC via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2- CC methylcitrate cycle I (propionate degradation route). Catalyzes the CC reversible isomerization of citrate to isocitrate via cis-aconitate. CC Also catalyzes the hydration of 2-methyl-cis-aconitate to yield CC (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA- CC binding regulatory protein. During oxidative stress inactive AcnB apo- CC enzyme without iron sulfur clusters binds the acnB mRNA 3' UTRs CC (untranslated regions), stabilizes acnB mRNA and increases AcnB CC synthesis, thus mediating a post-transcriptional positive CC autoregulatory switch. AcnB also decreases the stability of the sodA CC transcript. {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:10589714, CC ECO:0000269|PubMed:11932448, ECO:0000269|PubMed:12473114, CC ECO:0000269|PubMed:15882410, ECO:0000269|PubMed:8000525, CC ECO:0000269|PubMed:8932712}. CC -!- CATALYTIC ACTIVITY: CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; CC Evidence={ECO:0000269|PubMed:10585860}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis- CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99; CC Evidence={ECO:0000269|PubMed:12473114}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:11992126}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000269|PubMed:11992126}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=11 mM for citrate {ECO:0000269|PubMed:10585860, CC ECO:0000269|PubMed:12473114}; CC KM=0.016 mM for cis-aconitate {ECO:0000269|PubMed:10585860, CC ECO:0000269|PubMed:12473114}; CC KM=0.051 mM for isocitrate (using 0.01-0.8 mM substrate) CC {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:12473114}; CC KM=19.7 mM for isocitrate (using 0.8-40 mM substrate) CC {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:12473114}; CC KM=0.21 mM for (2R,3S)-2-methylisocitrate CC {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:12473114}; CC Vmax=23.8 umol/min/mg enzyme with citrate as substrate CC {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:12473114}; CC Vmax=39.1 umol/min/mg enzyme with cis-aconitate as substrate CC {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:12473114}; CC Vmax=5.92 umol/min/mg enzyme using 0.01-0.8 mM isocitrate as CC substrate {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:12473114}; CC Vmax=57.8 umol/min/mg enzyme using 0.8-40 mM isocitrate as substrate CC {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:12473114}; CC pH dependence: CC Optimum pH is 7.4. {ECO:0000269|PubMed:10585860, CC ECO:0000269|PubMed:12473114}; CC -!- PATHWAY: Organic acid metabolism; propanoate degradation. CC {ECO:0000305|PubMed:12473114}. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate CC from oxaloacetate: step 2/2. {ECO:0000305|PubMed:12473114}. CC -!- SUBUNIT: Monomer. AcnB can also form a homodimer. The monomer-homodimer CC transition is dependent on iron availability and the carboxymethylation CC of C-273 inhibits the dimer formation. {ECO:0000269|PubMed:11992126, CC ECO:0000269|PubMed:15882410, ECO:0000269|PubMed:8932712}. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are more sensitive to CC peroxide stress. The acnAB double mutant does not grow on CC unsupplemented glucose minimal medium and does not respond under CC aerobic conditions to glutamate. The acnAB double mutant retains a low CC but significant aconitase activity. {ECO:0000269|PubMed:11932448, CC ECO:0000269|PubMed:15882410, ECO:0000269|PubMed:9202458}. CC -!- MISCELLANEOUS: AcnB is sensitive to oxidation in vivo. CC {ECO:0000269|PubMed:10585860}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase 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; U00096; AAC73229.1; -; Genomic_DNA. DR EMBL; AP009048; BAB96692.2; -; Genomic_DNA. DR EMBL; U41560; AAC43710.1; -; Genomic_DNA. DR PIR; F64734; F64734. DR RefSeq; NP_414660.1; NC_000913.3. DR RefSeq; WP_001307570.1; NZ_CP009789.1. DR PDB; 1L5J; X-ray; 2.40 A; A/B=1-865. DR AlphaFoldDB; P36683; -. DR SMR; P36683; -. DR BioGRID; 4261902; 121. DR BioGRID; 849264; 1. DR DIP; DIP-9044N; -. DR FunCoup; P36683; 419. DR IntAct; P36683; 15. DR STRING; 511145.b0118; -. DR DrugBank; DB04351; Aconitate Ion. DR CarbonylDB; P36683; -. DR jPOST; P36683; -. DR PaxDb; 511145-b0118; -. DR EnsemblBacteria; AAC73229; AAC73229; b0118. DR GeneID; 93777318; -. DR GeneID; 944864; -. DR KEGG; ecj:JW0114; -. DR KEGG; eco:b0118; -. DR KEGG; ecoc:C3026_00495; -. DR PATRIC; fig|1411691.4.peg.2164; -. DR EchoBASE; EB2222; -. DR eggNOG; COG1049; Bacteria. DR HOGENOM; CLU_016536_0_0_6; -. DR InParanoid; P36683; -. DR OMA; PLHAKAM; -. DR OrthoDB; 9758061at2; -. DR PhylomeDB; P36683; -. DR BioCyc; EcoCyc:ACONITATEDEHYDRB-MONOMER; -. DR BioCyc; MetaCyc:ACONITATEDEHYDRB-MONOMER; -. DR BRENDA; 4.2.1.3; 2026. DR SABIO-RK; P36683; -. DR UniPathway; UPA00223; UER00718. DR UniPathway; UPA00946; -. DR EvolutionaryTrace; P36683; -. DR PRO; PR:P36683; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P36683; -. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IDA:EcoCyc. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc. DR GO; GO:0003994; F:aconitate hydratase activity; IDA:EcoCyc. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:EcoCyc. DR GO; GO:0003729; F:mRNA binding; IDA:EcoliWiki. DR GO; GO:0006097; P:glyoxylate cycle; NAS:EcoliWiki. DR GO; GO:0006417; P:regulation of translation; IDA:EcoCyc. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR CDD; cd01581; AcnB; 1. DR CDD; cd01576; AcnB_Swivel; 1. DR FunFam; 1.25.40.310:FF:000001; Aconitate hydratase B; 1. DR FunFam; 3.20.19.10:FF:000004; Aconitate hydratase B; 1. DR FunFam; 3.30.499.10:FF:000001; Aconitate hydratase B; 1. DR FunFam; 3.30.499.10:FF:000008; Aconitate hydratase B; 1. DR FunFam; 3.40.1060.10:FF:000002; Aconitate hydratase B; 1. DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1. DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2. DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1. DR Gene3D; 1.25.40.310; Aconitate B, HEAT-like domain; 1. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR050926; Aconitase/IPM_isomerase. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR InterPro; IPR036008; Aconitase_4Fe-4S_dom. DR InterPro; IPR004406; Aconitase_B. DR InterPro; IPR015933; Aconitase_B_HEAT-like_dom. DR InterPro; IPR036288; Aconitase_B_HEAT-like_dom_sf. DR InterPro; IPR015929; Aconitase_B_swivel. DR InterPro; IPR015932; Aconitase_dom2. DR NCBIfam; TIGR00117; acnB; 1. DR NCBIfam; NF006690; PRK09238.1; 1. DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1. DR PANTHER; PTHR43160:SF4; ACONITATE HYDRATASE B; 1. DR Pfam; PF00330; Aconitase; 1. DR Pfam; PF06434; Aconitase_2_N; 1. DR Pfam; PF11791; Aconitase_B_N; 1. DR PIRSF; PIRSF036687; AcnB; 1. DR SUPFAM; SSF74778; Aconitase B, N-terminal domain; 1. DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1. DR SUPFAM; SSF52016; LeuD/IlvD-like; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. DR PDBsum; 1L5J; -. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Lyase; KW Metal-binding; Reference proteome; RNA-binding; Tricarboxylic acid cycle. FT CHAIN 1..865 FT /note="Aconitate hydratase B" FT /id="PRO_0000076675" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11992126" FT BINDING 244..246 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11992126" FT BINDING 414..416 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11992126" FT BINDING 498 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11992126" FT BINDING 710 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:11992126" FT BINDING 769 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:11992126" FT BINDING 772 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:11992126" FT BINDING 791 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11992126" FT BINDING 796 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11992126" FT MUTAGEN 769 FT /note="C->S: Inhibits the dimer formation." FT /evidence="ECO:0000269|PubMed:15882410" FT HELIX 2..14 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 18..22 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 24..35 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 42..51 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 59..72 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 83..90 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 99..104 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 112..120 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 124..127 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 141..151 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 154..157 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 160..163 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 166..178 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 179..182 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 185..190 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 194..197 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 220..227 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 233..243 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 248..257 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 264..269 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 272..278 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 280..288 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 306..310 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 311..314 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 315..318 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 319..321 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 324..327 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 334..341 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 344..360 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 370..375 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 384..391 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 409..413 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 415..417 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 418..427 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 444..448 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 451..465 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 466..468 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 479..483 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 484..486 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 492..497 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 503..507 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 512..521 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 531..538 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 546..559 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 573..576 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 577..583 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 589..597 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 598..600 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 601..603 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 605..609 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 613..632 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 638..653 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 667..673 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 674..676 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 681..683 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 691..693 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 694..696 FT /evidence="ECO:0007829|PDB:1L5J" FT TURN 697..699 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 704..707 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 714..726 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 732..737 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 742..750 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 753..760 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 770..772 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 775..777 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 784..790 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 796..798 FT /evidence="ECO:0007829|PDB:1L5J" FT STRAND 802..805 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 808..817 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 820..822 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 823..834 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 837..840 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 842..844 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 846..848 FT /evidence="ECO:0007829|PDB:1L5J" FT HELIX 850..857 FT /evidence="ECO:0007829|PDB:1L5J" SQ SEQUENCE 865 AA; 93498 MW; FEC8AA5D2A9DD2BD CRC64; MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT NRVPPGVDEA AYVKAGFLAA IAKGEAKSPL LTPEKAIELL GTMQGGYNIH PLIDALDDAK LAPIAAKALS HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW ADAEWFLNRP ALAEKLTVTV FKVTGETNTD DLSPAPDAWS RPDIPLHALA MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV GTGSSRKSAT NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG RGLTTKAREA LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP GAYCEPKMTS VGSQDTTGPM TRDELKDLAC LGFSADLVMQ SFCHTAAYPK PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM QPGITLRDLV HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK WLANPELLEA DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARPLSAVQGE KIDEVFIGSC MTNIGHFRAA GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT YRYLNFNQLS QYTEKADGVI FQTAV //