ICMF_CUPMC
ID ICMF_CUPMC Reviewed; 1093 AA.
AC Q1LRY0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Fused isobutyryl-CoA mutase {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:22167181};
DE Includes:
DE RecName: Full=Isobutyryl-CoA mutase {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:22167181};
DE Short=ICM {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:22167181};
DE EC=5.4.99.13 {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000269|PubMed:22167181};
DE Includes:
DE RecName: Full=P-loop GTPase {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:22167181};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000269|PubMed:22167181};
DE AltName: Full=G-protein chaperone {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:22167181};
GN Name=icmF {ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000303|PubMed:22167181};
GN Synonyms=sbm {ECO:0000312|EMBL:ABF07096.1};
GN OrderedLocusNames=Rmet_0210 {ECO:0000312|EMBL:ABF07096.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22167181; DOI=10.1074/jbc.m111.320051;
RA Cracan V., Banerjee R.;
RT "Novel coenzyme B12-dependent interconversion of isovaleryl-CoA and
RT pivalyl-CoA.";
RL J. Biol. Chem. 287:3723-3732(2012).
RN [3]
RP MUTAGENESIS OF PHE-598.
RX PubMed=26134562; DOI=10.1074/jbc.m115.646299;
RA Kitanishi K., Cracan V., Banerjee R.;
RT "Engineered and native coenzyme B12-dependent isovaleryl-CoA/pivalyl-CoA
RT mutase.";
RL J. Biol. Chem. 290:20466-20476(2015).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=28130442; DOI=10.1074/jbc.m117.775957;
RA Li Z., Kitanishi K., Twahir U.T., Cracan V., Chapman D., Warncke K.,
RA Banerjee R.;
RT "Cofactor editing by the G-protein metallochaperone domain regulates the
RT radical B12 enzyme IcmF.";
RL J. Biol. Chem. 292:3977-3987(2017).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF APOENYZME AND IN COMPLEXES WITH
RP ADENOSYLCOBALAMIN; BUTYRYL-COA; GDP AND MAGNESIUM, FUNCTION, COFACTOR,
RP SUBUNIT, AND DOMAIN.
RX PubMed=25675500; DOI=10.1073/pnas.1419582112;
RA Jost M., Cracan V., Hubbard P.A., Banerjee R., Drennan C.L.;
RT "Visualization of a radical B12 enzyme with its G-protein chaperone.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:2419-2424(2015).
CC -!- FUNCTION: Catalyzes the reversible interconversion of isobutyryl-CoA
CC and n-butyryl-CoA, and to a much lesser extent, of pivalyl-CoA and
CC isovaleryl-CoA, using radical chemistry (PubMed:22167181). Also
CC exhibits GTPase activity, associated with its G-protein domain (MeaI)
CC that functions as a chaperone that assists cofactor delivery and proper
CC holo-enzyme assembly (PubMed:22167181, PubMed:25675500). The G-domain
CC of IcmF has also a role in its cofactor repair (PubMed:28130442). Does
CC not display ATPase activity. {ECO:0000269|PubMed:22167181,
CC ECO:0000269|PubMed:25675500, ECO:0000269|PubMed:28130442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA = butanoyl-CoA; Xref=Rhea:RHEA:13141,
CC ChEBI:CHEBI:57338, ChEBI:CHEBI:57371; EC=5.4.99.13;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02050,
CC ECO:0000269|PubMed:22167181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutanoyl-CoA = 2,2-dimethylpropanoyl-CoA;
CC Xref=Rhea:RHEA:52620, ChEBI:CHEBI:57345, ChEBI:CHEBI:136712;
CC Evidence={ECO:0000269|PubMed:22167181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02050, ECO:0000269|PubMed:22167181};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02050,
CC ECO:0000269|PubMed:25675500};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02050,
CC ECO:0000269|PubMed:25675500};
CC -!- ACTIVITY REGULATION: Is prone to inactivation during catalytic turnover
CC due to the occasional loss of the 5'-deoxyadenosine moiety and
CC formation of the inactive cob(II)alamin cofactor in its active site.
CC The GTPase activity of IcmF powers the ejection of the inactive
CC cofactor and requires the presence of an acceptor protein,
CC adenosyltransferase (ATR), for receiving it. ATR, in turn, catalyzes an
CC adenosylation reaction converting cob(II)alamin in the presence of ATP
CC and a reductant to the active AdoCbl cofactor. The repaired cofactor is
CC then reloaded onto IcmF in a GTPase-gated step, regenerating active
CC enzyme. The GTPase activity of IcmF is significantly decreased in the
CC presence of excess of AdoCbl or cob(II)alamin and is higher in the
CC apoenzyme state, indicating that the G-domain senses the presence and
CC identity of the cofactor in the mutase active site.
CC {ECO:0000269|PubMed:28130442}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for GTP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:22167181};
CC Vmax=0.015 umol/min/mg enzyme for isovaleryl-CoA isomerization (at 37
CC degrees Celsius) {ECO:0000269|PubMed:22167181};
CC Vmax=13.8 umol/min/mg enzyme for isobutyryl-CoA isomerization (at 37
CC degrees Celsius) {ECO:0000269|PubMed:22167181};
CC Vmax=33.0 umol/min/mg enzyme for n-butyryl-CoA isomerization (at 37
CC degrees Celsius) {ECO:0000269|PubMed:22167181};
CC Note=kcat is 18 min(-1) for GTPase activity (at 37 degrees Celsius).
CC {ECO:0000269|PubMed:22167181};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02050,
CC ECO:0000269|PubMed:25675500}.
CC -!- DOMAIN: Is composed of four functional domains: the N-terminal 5'-
CC deoxyadenosylcobalamin binding region that is homologous to the small
CC subunit of ICM (IcmB), a middle P-loop GTPase domain (MeaI) that acts
CC as a chaperone for ICM, a structured linker region involved in dimer
CC formation, and a C-terminal part that is homologous to the large
CC substrate-binding subunit of ICM (IcmA). {ECO:0000269|PubMed:25675500}.
CC -!- MISCELLANEOUS: In many AdoCbl-dependent isomerases, e.g. methylmalonyl-
CC CoA mutase (MCM), its G-protein chaperone is a separate protein.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IcmF family. {ECO:0000255|HAMAP-
CC Rule:MF_02050, 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; CP000352; ABF07096.1; -; Genomic_DNA.
DR RefSeq; WP_011515115.1; NC_007973.1.
DR PDB; 4XC6; X-ray; 3.35 A; A/B=1-1093.
DR PDB; 4XC7; X-ray; 3.45 A; A/B=1-1093.
DR PDB; 4XC8; X-ray; 3.25 A; A/B=1-1093.
DR PDB; 5CJT; X-ray; 3.40 A; A/B=1-1093.
DR PDB; 5CJU; X-ray; 3.50 A; A/B=1-1093.
DR PDB; 5CJV; X-ray; 3.45 A; A/B=1-1093.
DR PDB; 5CJW; X-ray; 3.40 A; A/B=1-1093.
DR PDBsum; 4XC6; -.
DR PDBsum; 4XC7; -.
DR PDBsum; 4XC8; -.
DR PDBsum; 5CJT; -.
DR PDBsum; 5CJU; -.
DR PDBsum; 5CJV; -.
DR PDBsum; 5CJW; -.
DR AlphaFoldDB; Q1LRY0; -.
DR SMR; Q1LRY0; -.
DR STRING; 266264.Rmet_0210; -.
DR PRIDE; Q1LRY0; -.
DR EnsemblBacteria; ABF07096; ABF07096; Rmet_0210.
DR KEGG; rme:Rmet_0210; -.
DR eggNOG; COG1703; Bacteria.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_2_0_4; -.
DR OMA; LAMFMNT; -.
DR OrthoDB; 154460at2; -.
DR BRENDA; 5.4.99.13; 5272.
DR SABIO-RK; Q1LRY0; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0047727; F:isobutyryl-CoA mutase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:InterPro.
DR GO; GO:0034784; F:pivalyl-CoA mutase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02050; IcmF; 1.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR033669; IcmF.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cobalamin; Cobalt; GTP-binding; Hydrolase;
KW Isomerase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1093
FT /note="Fused isobutyryl-CoA mutase"
FT /id="PRO_0000434125"
FT DOMAIN 26..156
FT /note="B12-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..417
FT /note="GTPase chaperone MeaI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT REGION 418..579
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT BINDING 39
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 219..224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 357..360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 587
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT BINDING 622
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT BINDING 728
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT BINDING 772
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT BINDING 821
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT BINDING 856
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT BINDING 861
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500"
FT BINDING 973
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT BINDING 1092
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02050,
FT ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6"
FT MUTAGEN 598
FT /note="F->A: Switches the substrate specificity and
FT enhances the catalytic efficiency of the isovaleryl-CoA
FT mutase over the native isobutyryl-CoA mutase activity about
FT 4000-fold. Is even more susceptible to inactivation than
FT wild-type during turnover."
FT /evidence="ECO:0000269|PubMed:26134562"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:4XC6"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 222..237
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 364..378
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 402..416
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 449..485
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 493..504
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 507..522
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:4XC6"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:4XC7"
FT STRAND 550..554
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 562..571
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 604..614
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:4XC6"
FT STRAND 619..627
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 629..632
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 641..644
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 645..650
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:4XC7"
FT HELIX 657..663
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 684..706
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 713..726
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 735..738
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 739..742
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 749..765
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 770..777
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 779..783
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 788..809
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 813..816
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 817..819
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 820..825
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 830..834
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 835..849
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 855..858
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 861..865
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 873..875
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 876..878
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 879..892
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 896..899
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 903..907
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 913..927
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 931..933
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 937..940
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 942..963
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 964..966
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 967..974
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 976..994
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 995..997
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 1000..1002
FT /evidence="ECO:0007829|PDB:4XC8"
FT STRAND 1003..1005
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 1024..1040
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 1041..1043
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 1044..1057
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 1062..1069
FT /evidence="ECO:0007829|PDB:4XC8"
FT TURN 1070..1072
FT /evidence="ECO:0007829|PDB:4XC8"
FT HELIX 1075..1086
FT /evidence="ECO:0007829|PDB:4XC8"
SQ SEQUENCE 1093 AA; 120612 MW; 42ABCE6FD4B22E82 CRC64;
MTDLSDVSRT AAAKPPAVPG RGPANKVRFV TAASLFDGHD ASINIMRRIL QSQGCEVIHL
GHNRSVQEVV TAALQEDVQG IAISSYQGGH VEYFKYMIDL LREHGGEHIQ VFGGGGGVIV
PDEIRELQAY GVARIYSPED GQRMGLAGMI TDMAQRCDID LTRYAPTTLD TVVAGDRRAL
AQLITALENG KADPELVSAL HAQAKAAAVP VLGITGTGGA GKSSLTDELI RRFRLDQDDA
LSIAVISIDP SRRKSGGALL GDRIRMNAIN HPNIFMRSLA TREAGSEISQ ALPDVIAACK
AARFDLVIVE TSGIGQGDAA IVPHVDLSLY VMTPEFGAAS QLEKIDMLDF ADFVAINKFD
RKGAQDAWRD VAKQVQRNRE QWHSRAEDMP VYGTQASRFN DDGVTMLYQG LVGALGARGM
SLKPGTLPNL EGRISTGQNV IVPPARSRYL AELADTVRAY HRRVVAQSKL ARERQQLRAA
HDMLQGAGHE SAALETLASE RDVSLGAVER KLLAMWPQMQ QAYSGDEYVV KIRDKEIRTG
LISTTLSGTK IRKVVLPRFE DEGEILKWLM RENVPGSFPY TAGVFAFKRE GEDPTRMFAG
EGDAFRTNRR FKLVSEGMEA KRLSTAFDSV TLYGEDPHER PDIYGKVGNS GVSIATLEDM
KVLYDGFDLT NPSTSVSMTI NGPAPTILAM FMNTAIDQQI DRFRADNGRD PTADEEAKIR
AWVLQNVRGT VQADILKEDQ GQNTCIFSTE FSLKVMGDIQ EYFVHHQVRN FYSVSISGYH
IAEAGANPIS QLAFTLANGF TYVEAYLARG MHIDDFAPNL SFFFSNGMDP EYSVLGRVAR
RIWAVTMRDK YGANDRSQKL KYHIQTSGRS LHAQEIDFND IRTTLQALIA IYDNCNSLHT
NAYDEAITTP TAESVRRALA IQLIINREWG VAKCENPNQG SFLIEELTDL VEEAVLQEFE
RIAERGGVLG AMETGYQRGK IQEESLYYEQ LKHDGTLPII GVNTFRNPNG DPTPQTLELA
RSSEDEKQSQ LHRLTEFHGA HQADAEAMLA RLRQAVIDNR NVFAVLMDAV RVCSLGQITH
ALFEVGGQYR RNM
