ACNB_ECOLI
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 03-AUG-2022, entry version 190.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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}.
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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_STEB01000010.1.
DR PDB; 1L5J; X-ray; 2.40 A; A/B=1-865.
DR PDBsum; 1L5J; -.
DR AlphaFoldDB; P36683; -.
DR SMR; P36683; -.
DR BioGRID; 4261902; 105.
DR BioGRID; 849264; 1.
DR DIP; DIP-9044N; -.
DR IntAct; P36683; 15.
DR STRING; 511145.b0118; -.
DR DrugBank; DB04351; Aconitate Ion.
DR CarbonylDB; P36683; -.
DR SWISS-2DPAGE; P36683; -.
DR jPOST; P36683; -.
DR PaxDb; P36683; -.
DR PRIDE; P36683; -.
DR EnsemblBacteria; AAC73229; AAC73229; b0118.
DR EnsemblBacteria; BAB96692; BAB96692; BAB96692.
DR GeneID; 66671594; -.
DR GeneID; 944864; -.
DR KEGG; ecj:JW0114; -.
DR KEGG; eco:b0118; -.
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; QDTTGAM; -.
DR PhylomeDB; P36683; -.
DR BioCyc; EcoCyc:ACONITATEDEHYDRB-MON; -.
DR BioCyc; MetaCyc:ACONITATEDEHYDRB-MON; -.
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; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IDA:EcoCyc.
DR GO; GO:0006417; P:regulation of translation; IDA:EcoCyc.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd01576; AcnB_Swivel; 1.
DR Gene3D; 1.25.40.310; -; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 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; 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 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; SSF53732; SSF53732; 1.
DR SUPFAM; SSF74778; SSF74778; 1.
DR TIGRFAMs; TIGR00117; acnB; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
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 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 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 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 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 823..834
FT /evidence="ECO:0007829|PDB:1L5J"
FT HELIX 837..840
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
