BIOA_ECOLI
ID BIOA_ECOLI Reviewed; 429 AA.
AC P12995; Q2MBJ5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase;
DE EC=2.6.1.62 {ECO:0000269|PubMed:1092681, ECO:0000269|PubMed:1092682};
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000303|PubMed:1092681};
DE Short=DAPA AT;
DE Short=DAPA aminotransferase {ECO:0000303|PubMed:1092682};
DE AltName: Full=7,8-diaminononanoate synthase;
DE Short=DANS;
DE AltName: Full=Diaminopelargonic acid synthase;
GN Name=bioA; OrderedLocusNames=b0774, JW0757;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3058702; DOI=10.1016/s0021-9258(19)77675-3;
RA Otsuka A.J., Buoncristiani M.R., Howard P.K., Flamm J., Johnson O.,
RA Yamamoto R., Uchida K., Cook C., Ruppert J., Matsuzaki J.;
RT "The Escherichia coli biotin biosynthetic enzyme sequences predicted from
RT the nucleotide sequence of the bio operon.";
RL J. Biol. Chem. 263:19577-19585(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pearson B.M., McKee R.A.;
RT "Genetic material for expression of biotin synthetase enzymes.";
RL Patent number GB2216530, 11-OCT-1989.
RN [3]
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 [4]
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 [5]
RP FUNCTION, SUBUNIT, SUBSTRATE SPECIFICITY, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=1092681; DOI=10.1016/s0021-9258(19)41381-1;
RA Stoner G.L., Eisenberg M.A.;
RT "Purification and properties of 7, 8-diaminopelargonic acid
RT aminotransferase. An enzyme in the biotin biosynthetic pathway.";
RL J. Biol. Chem. 250:4029-4036(1975).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=1092682; DOI=10.1016/s0021-9258(19)41382-3;
RA Stoner G.L., Eisenberg M.A.;
RT "Biosynthesis of 7, 8-diaminopelargonic acid from 7-keto-8-aminopelargonic
RT acid and S-adenosyl-L-methionine. The kinetics of the reaction.";
RL J. Biol. Chem. 250:4037-4043(1975).
RN [7]
RP INDUCTION.
RX PubMed=6456358; DOI=10.1016/0022-2836(81)90043-7;
RA Barker D.F., Campbell A.M.;
RT "Genetic and biochemical characterization of the birA gene and its product:
RT evidence for a direct role of biotin holoenzyme synthetase in repression of
RT the biotin operon in Escherichia coli.";
RL J. Mol. Biol. 146:469-492(1981).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=16042602; DOI=10.1042/bst0330802;
RA Mann S., Marquet A., Ploux O.;
RT "Inhibition of 7,8-diaminopelargonic acid aminotransferase by amiclenomycin
RT and analogues.";
RL Biochem. Soc. Trans. 33:802-805(2005).
RN [9]
RP SUBSTRATE SPECIFICITY.
RX PubMed=20693992; DOI=10.1038/nchembio.420;
RA Lin S., Hanson R.E., Cronan J.E.;
RT "Biotin synthesis begins by hijacking the fatty acid synthetic pathway.";
RL Nat. Chem. Biol. 6:682-688(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=32042199; DOI=10.1038/s41589-019-0461-9;
RA Sakaki K., Ohishi K., Shimizu T., Kobayashi I., Mori N., Matsuda K.,
RA Tomita T., Watanabe H., Tanaka K., Kuzuyama T., Nishiyama M.;
RT "A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in
RT cyanobacteria.";
RL Nat. Chem. Biol. 16:415-422(2020).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP PYRIDOXAL PHOSPHATE.
RC STRAIN=B / BL21-DE3;
RX PubMed=10452893; DOI=10.1006/jmbi.1999.2997;
RA Kaeck H., Sandmark J., Gibson K., Schneider G., Lindqvist Y.;
RT "Crystal structure of diaminopelargonic acid synthase: evolutionary
RT relationships between pyridoxal-5'-phosphate-dependent enzymes.";
RL J. Mol. Biol. 291:857-876(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND MUTANTS ALA-391, MUTAGENESIS OF ARG-391, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12379100; DOI=10.1021/bi026339a;
RA Eliot A.C., Sandmark J., Schneider G., Kirsch J.F.;
RT "The dual-specific active site of 7,8-diaminopelargonic acid synthase and
RT the effect of the R391A mutation.";
RL Biochemistry 41:12582-12589(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP AND ACTIVITY REGULATION.
RX PubMed=12218056; DOI=10.1074/jbc.m207239200;
RA Sandmark J., Mann S., Marquet A., Schneider G.;
RT "Structural basis for the inhibition of the biosynthesis of biotin by the
RT antibiotic amiclenomycin.";
RL J. Biol. Chem. 277:43352-43358(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS PHE-17; PHE-144; ASN-147;
RP ALA-253 AND LYS-253 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, AND MUTAGENESIS OF
RP TYR-17; TYR-144; ASP-147 AND ARG-253.
RX PubMed=14756557; DOI=10.1021/bi0358059;
RA Sandmark J., Eliot A.C., Famm K., Schneider G., Kirsch J.F.;
RT "Conserved and nonconserved residues in the substrate binding site of 7,8-
RT diaminopelargonic acid synthase from Escherichia coli are essential for
RT catalysis.";
RL Biochemistry 43:1213-1222(2004).
CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
CC adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to
CC form 7,8-diaminopelargonic acid (DAPA) (PubMed:1092681,
CC PubMed:1092682). It is the only animotransferase known to utilize SAM
CC as an amino donor (PubMed:1092681, PubMed:1092682). Complements a bioU
CC deletion in Synechocystis PCC 6803 (PubMed:32042199).
CC {ECO:0000269|PubMed:1092681, ECO:0000269|PubMed:1092682,
CC ECO:0000269|PubMed:32042199}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine =
CC (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-
CC oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469;
CC EC=2.6.1.62; Evidence={ECO:0000269|PubMed:1092681,
CC ECO:0000269|PubMed:1092682};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:1092681};
CC -!- ACTIVITY REGULATION: Inhibited by amiclenomycin. S-adenosyl-L-(2-
CC hydroxy-4-methylthio)butyric acid and adenosine are competitive
CC inhibitors with SAM and uncompetitive inhibitors with KAPA as
CC substrates (PubMed:1092682). S-adenosyl-L-ethionine, adenine and 8-
CC keto-7-aminopelargonic acid are non-competitive inhibitors with both
CC substrates (PubMed:1092682). {ECO:0000269|PubMed:1092682,
CC ECO:0000269|PubMed:12218056, ECO:0000269|PubMed:16042602}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for KAPA {ECO:0000269|PubMed:1092682,
CC ECO:0000269|PubMed:12379100};
CC KM=150 uM for SAM {ECO:0000269|PubMed:1092682,
CC ECO:0000269|PubMed:12379100};
CC KM=21 uM for pyridoxamine phosphate (PMP)
CC {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100};
CC KM=32 uM for pyridoxal phosphate (PLP) {ECO:0000269|PubMed:1092682,
CC ECO:0000269|PubMed:12379100};
CC KM=1000 uM for 8-keto-7-aminopelargonic acid
CC {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100};
CC Vmax=0.16 umol/min/mg enzyme with KAPA as substrate
CC {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100};
CC Vmax=0.027 umol/min/mg enzyme with 8-keto-7-aminopelargonic acid as
CC substrate {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10452893,
CC ECO:0000269|PubMed:1092681, ECO:0000269|PubMed:12218056,
CC ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Repressed by BirA. {ECO:0000269|PubMed:6456358}.
CC -!- DISRUPTION PHENOTYPE: Loss of biotin synthesis.
CC {ECO:0000269|PubMed:32042199}.
CC -!- MISCELLANEOUS: Catalysis proceeds by a classical ping-pong bi-bi
CC reaction mechanism.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily. {ECO:0000305}.
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DR EMBL; J04423; AAA23514.1; -; Genomic_DNA.
DR EMBL; A11524; CAA00964.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC73861.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76361.1; -; Genomic_DNA.
DR PIR; F64813; XNECDP.
DR RefSeq; NP_415295.1; NC_000913.3.
DR RefSeq; WP_001295303.1; NZ_SSZK01000002.1.
DR PDB; 1DTY; X-ray; 2.14 A; A/B=1-429.
DR PDB; 1MGV; X-ray; 2.10 A; A/B=1-429.
DR PDB; 1MLY; X-ray; 1.81 A; A/B=1-429.
DR PDB; 1MLZ; X-ray; 2.15 A; A/B=1-429.
DR PDB; 1QJ3; X-ray; 2.70 A; A/B=1-429.
DR PDB; 1QJ5; X-ray; 1.80 A; A/B=1-429.
DR PDB; 1S06; X-ray; 2.20 A; A/B=1-429.
DR PDB; 1S07; X-ray; 2.42 A; A/B=1-429.
DR PDB; 1S08; X-ray; 2.10 A; A/B=1-429.
DR PDB; 1S09; X-ray; 1.83 A; A/B=1-429.
DR PDB; 1S0A; X-ray; 1.71 A; A/B=1-429.
DR PDB; 6ED7; X-ray; 2.43 A; A/B/C/D/E/F/G/H=2-429.
DR PDBsum; 1DTY; -.
DR PDBsum; 1MGV; -.
DR PDBsum; 1MLY; -.
DR PDBsum; 1MLZ; -.
DR PDBsum; 1QJ3; -.
DR PDBsum; 1QJ5; -.
DR PDBsum; 1S06; -.
DR PDBsum; 1S07; -.
DR PDBsum; 1S08; -.
DR PDBsum; 1S09; -.
DR PDBsum; 1S0A; -.
DR PDBsum; 6ED7; -.
DR AlphaFoldDB; P12995; -.
DR SMR; P12995; -.
DR BioGRID; 4261841; 13.
DR DIP; DIP-9219N; -.
DR IntAct; P12995; 5.
DR STRING; 511145.b0774; -.
DR DrugBank; DB02725; 2-Amino-4-(4-Amino-Cyclohexa-2,5-Dienyl)-Butyric Acid.
DR DrugBank; DB02274; 7-Keto-8-Aminopelargonic Acid.
DR DrugBank; DB04083; N(6)-(pyridoxal phosphate)-L-lysine.
DR PaxDb; P12995; -.
DR PRIDE; P12995; -.
DR EnsemblBacteria; AAC73861; AAC73861; b0774.
DR EnsemblBacteria; BAE76361; BAE76361; BAE76361.
DR GeneID; 945376; -.
DR KEGG; ecj:JW0757; -.
DR KEGG; eco:b0774; -.
DR PATRIC; fig|511145.12.peg.800; -.
DR EchoBASE; EB0115; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_6; -.
DR InParanoid; P12995; -.
DR OMA; VAVKMCL; -.
DR PhylomeDB; P12995; -.
DR BioCyc; EcoCyc:DAPASYN-MON; -.
DR BioCyc; MetaCyc:DAPASYN-MON; -.
DR BRENDA; 2.6.1.62; 2026.
DR SABIO-RK; P12995; -.
DR UniPathway; UPA00078; UER00160.
DR EvolutionaryTrace; P12995; -.
DR PRO; PR:P12995; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00834; BioA; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR005815; BioA.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00508; bioA; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Biotin biosynthesis; Cytoplasm;
KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..429
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000120366"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10452893,
FT ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY,
FT ECO:0007744|PDB:1QJ3"
FT BINDING 112..113
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:10452893,
FT ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557,
FT ECO:0007744|PDB:1DTY, ECO:0007744|PDB:1MGV,
FT ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5,
FT ECO:0007744|PDB:1S07"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:10452893"
FT BINDING 245
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:10452893,
FT ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557,
FT ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3,
FT ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S07"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10452893,
FT ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY,
FT ECO:0007744|PDB:1QJ3"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10452893,
FT ECO:0007744|PDB:1QJ3"
FT BINDING 308..309
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:10452893,
FT ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557,
FT ECO:0007744|PDB:1DTY, ECO:0007744|PDB:1MGV,
FT ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5,
FT ECO:0007744|PDB:1S07"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10452893,
FT ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY,
FT ECO:0007744|PDB:1MLZ, ECO:0007744|PDB:1QJ3"
FT SITE 17
FT /note="Participates in the substrate recognition with KAPA
FT and in a stacking interaction with the adenine ring of SAM"
FT /evidence="ECO:0000305"
FT MOD_RES 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:12379100,
FT ECO:0000269|PubMed:14756557, ECO:0007744|PDB:1DTY,
FT ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3,
FT ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S06,
FT ECO:0007744|PDB:1S08, ECO:0007744|PDB:1S09,
FT ECO:0007744|PDB:1S0A"
FT MUTAGEN 17
FT /note="Y->F: Severely reduces the aminotransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:14756557"
FT MUTAGEN 144
FT /note="Y->F: Severely reduces the aminotransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:14756557"
FT MUTAGEN 147
FT /note="D->N: Loss of aminotransferase activity."
FT /evidence="ECO:0000269|PubMed:14756557"
FT MUTAGEN 253
FT /note="R->A: Has only a small effect on the rate of
FT reaction with DAPA."
FT /evidence="ECO:0000269|PubMed:14756557"
FT MUTAGEN 253
FT /note="R->K: Increases aminotransferase activity toward
FT SAM."
FT /evidence="ECO:0000269|PubMed:14756557"
FT MUTAGEN 253
FT /note="R->M: Loss of aminotransferase activity."
FT /evidence="ECO:0000269|PubMed:14756557"
FT MUTAGEN 253
FT /note="R->Q: Increases aminotransferase activity toward
FT SAM."
FT /evidence="ECO:0000269|PubMed:14756557"
FT MUTAGEN 391
FT /note="R->A: Reduces aminotransferase activity."
FT /evidence="ECO:0000269|PubMed:12379100"
FT CONFLICT 11
FT /note="R -> P (in Ref. 2; CAA00964)"
FT /evidence="ECO:0000305"
FT CONFLICT 99..102
FT /note="TPQP -> SGRNA (in Ref. 1; AAA23514)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1S0A"
FT TURN 50..54
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1S0A"
FT TURN 157..161
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1S0A"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1DTY"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:1S0A"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1S0A"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1S0A"
FT TURN 247..254
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:1QJ5"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1MGV"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 332..347
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 376..385
FT /evidence="ECO:0007829|PDB:1S0A"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 407..420
FT /evidence="ECO:0007829|PDB:1S0A"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1S0A"
SQ SEQUENCE 429 AA; 47336 MW; 84D2D1AE3A1280FF CRC64;
MTTDDLAFDQ RHIWHPYTSM TSPLPVYPVV SAEGCELILS DGRRLVDGMS SWWAAIHGYN
HPQLNAAMKS QIDAMSHVMF GGITHAPAIE LCRKLVAMTP QPLECVFLAD SGSVAVEVAM
KMALQYWQAK GEARQRFLTF RNGYHGDTFG AMSVCDPDNS MHSLWKGYLP ENLFAPAPQS
RMDGEWDERD MVGFARLMAA HRHEIAAVII EPIVQGAGGM RMYHPEWLKR IRKICDREGI
LLIADEIATG FGRTGKLFAC EHAEIAPDIL CLGKALTGGT MTLSATLTTR EVAETISNGE
AGCFMHGPTF MGNPLACAAA NASLAILESG DWQQQVADIE VQLREQLAPA RDAEMVADVR
VLGAIGVVET THPVNMAALQ KFFVEQGVWI RPFGKLIYLM PPYIILPQQL QRLTAAVNRA
VQDETFFCQ
