BIOD_MYCTU
ID BIOD_MYCTU Reviewed; 226 AA.
AC P9WPQ5; L0T9U0; O06620;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Dethiobiotin synthetase BioD {ECO:0000305};
DE EC=6.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00336};
DE AltName: Full=DTB synthetase {ECO:0000255|HAMAP-Rule:MF_00336};
DE Short=DTBS {ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000303|PubMed:20565114};
DE AltName: Full=Dethiobiotin synthase {ECO:0000255|HAMAP-Rule:MF_00336};
GN Name=bioD {ECO:0000255|HAMAP-Rule:MF_00336}; OrderedLocusNames=Rv1570;
GN ORFNames=MTCY336.33c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3] {ECO:0007744|PDB:3FGN, ECO:0007744|PDB:3FMF, ECO:0007744|PDB:3FMI, ECO:0007744|PDB:3FPA}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP PHOSPHATE AND MAGNESIUM IONS, FUNCTION AS A DETHIOBIOTIN SYNTHETASE,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20565114; DOI=10.1021/bi902097j;
RA Dey S., Lane J.M., Lee R.E., Rubin E.J., Sacchettini J.C.;
RT "Structural characterization of the Mycobacterium tuberculosis biotin
RT biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin
RT synthetase.";
RL Biochemistry 49:6746-6760(2010).
RN [4] {ECO:0007744|PDB:4WOP}
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 2-226 IN COMPLEX WITH CTP,
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF
RP GLY-169.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=25801336; DOI=10.1016/j.tube.2015.02.046;
RA Salaemae W., Yap M.Y., Wegener K.L., Booker G.W., Wilce M.C., Polyak S.W.;
RT "Nucleotide triphosphate promiscuity in Mycobacterium tuberculosis
RT dethiobiotin synthetase.";
RL Tuberculosis 95:259-266(2015).
RN [5] {ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF, ECO:0007744|PDB:6CVU, ECO:0007744|PDB:6CVV, ECO:0007744|PDB:6CZB, ECO:0007744|PDB:6CZC, ECO:0007744|PDB:6CZE}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-226 IN COMPLEX WITH VARIOUS
RP NUCLEOTIDES AND MAGNESIUM, NUCLEOTIDE SUBSTRATE SPECIFICITY, COFACTOR,
RP SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 25618 / H37Rv;
RX DOI=10.1021/acscatal.8b03475;
RA Thompson A.P., Salaemae W., Pederick J.L., Abell A.D., Booker G.W.,
RA Bruning J.B., Polyak S.W.;
RT "Mycobacterium tuberculosis Dethiobiotin Synthetase Facilitates Nucleoside
RT Triphosphate Promiscuity through Alternate Binding Modes.";
RL ACS Catal. 8:10774-10783(2018).
RN [6] {ECO:0007744|PDB:6CZD, ECO:0007744|PDB:6E05, ECO:0007744|PDB:6E06}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-226 IN COMPLEX WITH ADP OR CTP
RP AND MAGNESIUM, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=30289406; DOI=10.1107/s2059798318010136;
RA Thompson A.P., Wegener K.L., Booker G.W., Polyak S.W., Bruning J.B.;
RT "Precipitant-ligand exchange technique reveals the ADP binding mode in
RT Mycobacterium tuberculosis dethiobiotin synthetase.";
RL Acta Crystallogr. D 74:965-972(2018).
CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-
CC diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to
CC form a ureido ring (PubMed:20565114). Can use a range of NTPs; has
CC highest affinity for CTP (KD is measured as 17.2 uM or 0.160 uM in 2
CC different papers) while KD for ATP is 331 uM or 75 uM in the same
CC papers. Gly-169 plays a role in NTP discrimination (PubMed:25801336,
CC Ref.5). {ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:25801336,
CC ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-
CC dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473,
CC ChEBI:CHEBI:456216; EC=6.3.3.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00336};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00336,
CC ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:30289406,
CC ECO:0000269|Ref.5};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000269|PubMed:20565114,
CC ECO:0000269|PubMed:30289406, ECO:0000269|Ref.5};
CC -!- ACTIVITY REGULATION: Inhibited by ADP. {ECO:0000269|PubMed:30289406}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for DAPA (at pH 8.5 and at 20 degrees Celsius)
CC {ECO:0000269|PubMed:20565114};
CC KM=29 uM for ATP (at pH 8.5 and at 20 degrees Celsius)
CC {ECO:0000269|PubMed:20565114};
CC KM=30.2 uM for DAPA (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=3.074 mM for NaHCO(3) (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=30.2 uM for ATP (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=25.2 uM for CTP (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=26.3 uM for GTP (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=17.7 uM for ITP (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=23.2 uM for TTP (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=26.1 uM for UTP (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC Vmax=3.5 umol/min/mg enzyme toward ATP (at pH 8.5 and at 20 degrees
CC Celsius) {ECO:0000269|PubMed:20565114};
CC Vmax=6 umol/min/mg enzyme toward DAPA (at pH 8.5 and at 20 degrees
CC Celsius) {ECO:0000269|PubMed:20565114};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00336,
CC ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:25801336,
CC ECO:0000269|PubMed:30289406, ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}.
CC -!- DOMAIN: While ADP, ATP, ITP, TTP and UTP can be crystallized in the
CC enzyme in approximately the same place as CTP, it is their phosphate
CC tails that anchor them to the enzyme, their nucleoside moieties do not
CC bind in the same way CTP does. {ECO:0000269|PubMed:30289406,
CC ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00336}.
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DR EMBL; AL123456; CCP44334.1; -; Genomic_DNA.
DR PIR; D70540; D70540.
DR RefSeq; NP_216086.1; NC_000962.3.
DR RefSeq; WP_009935471.1; NZ_NVQJ01000004.1.
DR PDB; 3FGN; X-ray; 1.85 A; A/B/C/D=1-226.
DR PDB; 3FMF; X-ray; 2.05 A; A/B/C/D=1-226.
DR PDB; 3FMI; X-ray; 2.18 A; A/B/C/D=1-226.
DR PDB; 3FPA; X-ray; 2.30 A; A/B/C/D=1-226.
DR PDB; 4WOP; X-ray; 2.39 A; A/B/C/D=2-225.
DR PDB; 6CVE; X-ray; 2.20 A; A/B/C/D=2-226.
DR PDB; 6CVF; X-ray; 2.30 A; A/B/C/D=2-226.
DR PDB; 6CVU; X-ray; 2.43 A; A/B/C/D=2-226.
DR PDB; 6CVV; X-ray; 2.41 A; A/B/C/D=2-226.
DR PDB; 6CZB; X-ray; 2.40 A; A/B/C/D=2-226.
DR PDB; 6CZC; X-ray; 2.30 A; A/B/C/D=2-226.
DR PDB; 6CZD; X-ray; 2.40 A; A/B/C/D=2-226.
DR PDB; 6CZE; X-ray; 2.30 A; A/B/C/D=2-226.
DR PDB; 6E05; X-ray; 2.50 A; A/B/C/D=2-226.
DR PDB; 6E06; X-ray; 2.50 A; A/B/C/D=2-226.
DR PDB; 6NKA; X-ray; 2.23 A; A/B/C/D=2-226.
DR PDB; 6NKB; X-ray; 2.00 A; A/B/C/D=2-226.
DR PDB; 6NL4; X-ray; 1.99 A; A/B/C/D=2-226.
DR PDB; 6NL5; X-ray; 2.31 A; A/B/C/D=2-226.
DR PDB; 6NLZ; X-ray; 1.90 A; A/B/C/D=2-226.
DR PDB; 6NMZ; X-ray; 2.40 A; A/B/C/D=2-226.
DR PDB; 6NN0; X-ray; 2.34 A; A/B/C/D=2-226.
DR PDB; 6NNZ; X-ray; 2.30 A; A/B/C/D=2-226.
DR PDB; 6NU6; X-ray; 2.44 A; A/B/C/D=2-226.
DR PDB; 6NVC; X-ray; 2.25 A; A/B/C/D=2-226.
DR PDB; 6NVD; X-ray; 2.44 A; A/B/C/D=2-226.
DR PDB; 6NVE; X-ray; 2.00 A; A/B/C/D=2-226.
DR PDB; 6NVF; X-ray; 1.99 A; A/B/C/D=2-226.
DR PDB; 6NWG; X-ray; 1.94 A; A/B/C/D=2-226.
DR PDB; 6NWN; X-ray; 2.00 A; A/B/C/D=2-226.
DR PDB; 7JT5; X-ray; 2.00 A; A/B/C/D=2-226.
DR PDB; 7JT6; X-ray; 2.00 A; A/B/C/D=2-226.
DR PDB; 7L1J; X-ray; 1.60 A; A/B/C/D=2-226.
DR PDBsum; 3FGN; -.
DR PDBsum; 3FMF; -.
DR PDBsum; 3FMI; -.
DR PDBsum; 3FPA; -.
DR PDBsum; 4WOP; -.
DR PDBsum; 6CVE; -.
DR PDBsum; 6CVF; -.
DR PDBsum; 6CVU; -.
DR PDBsum; 6CVV; -.
DR PDBsum; 6CZB; -.
DR PDBsum; 6CZC; -.
DR PDBsum; 6CZD; -.
DR PDBsum; 6CZE; -.
DR PDBsum; 6E05; -.
DR PDBsum; 6E06; -.
DR PDBsum; 6NKA; -.
DR PDBsum; 6NKB; -.
DR PDBsum; 6NL4; -.
DR PDBsum; 6NL5; -.
DR PDBsum; 6NLZ; -.
DR PDBsum; 6NMZ; -.
DR PDBsum; 6NN0; -.
DR PDBsum; 6NNZ; -.
DR PDBsum; 6NU6; -.
DR PDBsum; 6NVC; -.
DR PDBsum; 6NVD; -.
DR PDBsum; 6NVE; -.
DR PDBsum; 6NVF; -.
DR PDBsum; 6NWG; -.
DR PDBsum; 6NWN; -.
DR PDBsum; 7JT5; -.
DR PDBsum; 7JT6; -.
DR PDBsum; 7L1J; -.
DR AlphaFoldDB; P9WPQ5; -.
DR SMR; P9WPQ5; -.
DR STRING; 83332.Rv1570; -.
DR ChEMBL; CHEMBL4105930; -.
DR DrugBank; DB03775; Dethiobiotin.
DR PaxDb; P9WPQ5; -.
DR DNASU; 886338; -.
DR GeneID; 886338; -.
DR KEGG; mtu:Rv1570; -.
DR TubercuList; Rv1570; -.
DR eggNOG; COG0132; Bacteria.
DR OMA; SPHWAAE; -.
DR BRENDA; 6.3.3.3; 3445.
DR UniPathway; UPA00078; UER00161.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00336; BioD; 1.
DR InterPro; IPR004472; DTB_synth_BioD.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43210; PTHR43210; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00347; bioD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biotin biosynthesis; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..226
FT /note="Dethiobiotin synthetase BioD"
FT /id="PRO_0000187977"
FT ACT_SITE 37
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 11..17
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:25801336,
FT ECO:0000269|PubMed:30289406, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:4WOP, ECO:0007744|PDB:6CVE,
FT ECO:0007744|PDB:6CVF, ECO:0007744|PDB:6E05,
FT ECO:0007744|PDB:6E06"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:30289406,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:3FPA,
FT ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF,
FT ECO:0007744|PDB:6CVV, ECO:0007744|PDB:6CZB,
FT ECO:0007744|PDB:6CZC, ECO:0007744|PDB:6CZD,
FT ECO:0007744|PDB:6CZE, ECO:0007744|PDB:6E05,
FT ECO:0007744|PDB:6E06"
FT BINDING 37..41
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20565114, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:3FMF, ECO:0007744|PDB:3FMI,
FT ECO:0007744|PDB:6CVE"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 49
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:25801336,
FT ECO:0007744|PDB:4WOP, ECO:0007744|PDB:6CZC"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:30289406,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:3FPA,
FT ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF,
FT ECO:0007744|PDB:6CVV, ECO:0007744|PDB:6CZB,
FT ECO:0007744|PDB:6CZC, ECO:0007744|PDB:6CZD,
FT ECO:0007744|PDB:6CZE, ECO:0007744|PDB:6E05,
FT ECO:0007744|PDB:6E06"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:30289406,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:3FPA,
FT ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF,
FT ECO:0007744|PDB:6CVV, ECO:0007744|PDB:6CZB,
FT ECO:0007744|PDB:6CZC, ECO:0007744|PDB:6CZD,
FT ECO:0007744|PDB:6CZE, ECO:0007744|PDB:6E05,
FT ECO:0007744|PDB:6E06"
FT BINDING 144..147
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20565114, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:3FMF, ECO:0007744|PDB:3FMI,
FT ECO:0007744|PDB:3FPA, ECO:0007744|PDB:6CVE"
FT BINDING 169
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:30289406, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF,
FT ECO:0007744|PDB:6CVU, ECO:0007744|PDB:6E05,
FT ECO:0007744|PDB:6E06"
FT BINDING 197..201
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000269|PubMed:25801336,
FT ECO:0000269|PubMed:30289406, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:4WOP, ECO:0007744|PDB:6CVE,
FT ECO:0007744|PDB:6CVF, ECO:0007744|PDB:6E05,
FT ECO:0007744|PDB:6E06"
FT MUTAGEN 169
FT /note="G->N: Decreases affinity for NaHCO(3) 3-fold, for
FT CTP 1.8-fold and for GTP 3.8-fold."
FT /evidence="ECO:0000269|PubMed:25801336"
FT STRAND 2..14
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:7L1J"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:7L1J"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:7L1J"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:7L1J"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:7L1J"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7L1J"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7L1J"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:7L1J"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:7L1J"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:7L1J"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:7L1J"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:7L1J"
SQ SEQUENCE 226 AA; 22456 MW; 43581D072ED41AAE CRC64;
MTILVVTGTG TGVGKTVVCA ALASAARQAG IDVAVCKPVQ TGTARGDDDL AEVGRLAGVT
QLAGLARYPQ PMAPAAAAEH AGMALPARDQ IVRLIADLDR PGRLTLVEGA GGLLVELAEP
GVTLRDVAVD VAAAALVVVT ADLGTLNHTK LTLEALAAQQ VSCAGLVIGS WPDPPGLVAA
SNRSALARIA MVRAALPAGA ASLDAGDFAA MSAAAFDRNW VAGLVG
