LINB_SPHJU
ID LINB_SPHJU Reviewed; 296 AA.
AC D4Z2G1; P51698;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Haloalkane dehalogenase {ECO:0000255|HAMAP-Rule:MF_01231, ECO:0000303|PubMed:9293022};
DE EC=3.8.1.5 {ECO:0000255|HAMAP-Rule:MF_01231, ECO:0000269|PubMed:9293022};
DE AltName: Full=1,3,4,6-tetrachloro-1,4-cyclohexadiene halidohydrolase {ECO:0000303|PubMed:9293022};
DE Short=1,4-TCDN halidohydrolase {ECO:0000303|PubMed:9293022};
GN Name=linB {ECO:0000303|PubMed:7691794, ECO:0000303|PubMed:9293022};
GN OrderedLocusNames=SJA_C1-19590 {ECO:0000312|EMBL:BAI96793.1};
OS Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26 /
OS NBRC 101211 / UT26S).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=452662;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, FUNCTION,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=7691794; DOI=10.1128/jb.175.20.6403-6410.1993;
RA Nagata Y., Nariya T., Ohtomo R., Fukuda M., Yano K., Takagi M.;
RT "Cloning and sequencing of a dehalogenase gene encoding an enzyme with
RT hydrolase activity involved in the degradation of gamma-
RT hexachlorocyclohexane in Pseudomonas paucimobilis.";
RL J. Bacteriol. 175:6403-6410(1993).
RN [2]
RP SEQUENCE REVISION.
RA Nagata Y., Nariya T., Ohtomo R., Fukuda M., Yano K., Takagi M.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=20817768; DOI=10.1128/jb.00961-10;
RA Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A., Fukui S.,
RA Fujita N., Tsuda M.;
RT "Complete genome sequence of the representative gamma-
RT hexachlorocyclohexane-degrading bacterium Sphingobium japonicum UT26.";
RL J. Bacteriol. 192:5852-5853(2010).
RN [4]
RP PROTEIN SEQUENCE OF 2-10, AND SUBCELLULAR LOCATION.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=10464214; DOI=10.1128/jb.181.17.5409-5413.1999;
RA Nagata Y., Futamura A., Miyauchi K., Takagi M.;
RT "Two different types of dehalogenases, LinA and LinB, involved in gamma-
RT hexachlorocyclohexane degradation in Sphingomonas paucimobilis UT26 are
RT localized in the periplasmic space without molecular processing.";
RL J. Bacteriol. 181:5409-5413(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=9293022; DOI=10.1128/aem.63.9.3707-3710.1997;
RA Nagata Y., Miyauchi K., Damborsky J., Manova K., Ansorgova A., Takagi M.;
RT "Purification and characterization of a haloalkane dehalogenase of a new
RT substrate class from a gamma-hexachlorocyclohexane-degrading bacterium,
RT Sphingomonas paucimobilis UT26.";
RL Appl. Environ. Microbiol. 63:3707-3710(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP ASP-108; GLU-132; GLU-244 AND HIS-272, AND ACTIVE SITE.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=10100638; DOI=10.1016/s0014-5793(99)00199-4;
RA Hynkova K., Nagata Y., Takagi M., Damborsky J.;
RT "Identification of the catalytic triad in the haloalkane dehalogenase from
RT Sphingomonas paucimobilis UT26.";
RL FEBS Lett. 446:177-181(1999).
RN [7]
RP QUANTUM MECHANIC STUDIES, AND MUTAGENESIS OF ASN-38; TRP-109; PHE-151 AND
RP PHE-169.
RX PubMed=12450392; DOI=10.1021/bi026427v;
RA Bohac M., Nagata Y., Prokop Z., Prokop M., Monincova M., Tsuda M., Koca J.,
RA Damborsky J.;
RT "Halide-stabilizing residues of haloalkane dehalogenases studied by quantum
RT mechanic calculations and site-directed mutagenesis.";
RL Biochemistry 41:14272-14280(2002).
RN [8]
RP CRYSTALLIZATION.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=10329794; DOI=10.1107/s090744499900459x;
RA Smatanova I.K., Nagata Y., Svensson L.A., Takagi M., Marek J.;
RT "Crystallization and preliminary X-ray diffraction analysis of haloalkane
RT dehalogenase LinB from Sphingomonas paucimobilis UT26.";
RL Acta Crystallogr. D 55:1231-1233(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH
RP 1,3-PROPANEDIOL.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=11087355; DOI=10.1021/bi001539c;
RA Marek J., Vevodova J., Smatanova I.K., Nagata Y., Svensson L.A., Newman J.,
RA Takagi M., Damborsky J.;
RT "Crystal structure of the haloalkane dehalogenase from Sphingomonas
RT paucimobilis UT26.";
RL Biochemistry 39:14082-14086(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF COMPLEXES WITH 1,2-DICHLOROETHANE;
RP 1,2-DICHLOROPROPANE AND BUTAN-1-OL.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=11939779; DOI=10.1021/bi015734i;
RA Oakley A.J., Prokop Z., Bohac M., Kmunicek J., Jedlicka T., Monincova M.,
RA Kuta-Smatanova I., Nagata Y., Damborsky J., Wilce M.C.J.;
RT "Exploring the structure and activity of haloalkane dehalogenase from
RT Sphingomonas paucimobilis UT26: evidence for product- and water-mediated
RT inhibition.";
RL Biochemistry 41:4847-4855(2002).
RN [11] {ECO:0007744|PDB:1IZ7, ECO:0007744|PDB:1IZ8, ECO:0007744|PDB:1K5P, ECO:0007744|PDB:1K63, ECO:0007744|PDB:1K6E}
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH
RP 1,2-PROPANEDIOL; 1-BROMOPROPAN-2-OL AND 2-BROMO-2-PROPEN-1-OL, AND ACTIVE
RP SITE.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=12939138; DOI=10.1021/bi027280a;
RA Streltsov V.A., Prokop Z., Damborsky J., Nagata Y., Oakley A., Wilce M.C.;
RT "Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray
RT crystallographic studies of dehalogenation of brominated substrates.";
RL Biochemistry 42:10104-10112(2003).
RN [12] {ECO:0007744|PDB:1MJ5}
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) IN COMPLEX WITH CHLORIDE, AND ACTIVE
RP SITE.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=14744129; DOI=10.1021/bi034748g;
RA Oakley A.J., Klvana M., Otyepka M., Nagata Y., Wilce M.C., Damborsky J.;
RT "Crystal structure of haloalkane dehalogenase LinB from Sphingomonas
RT paucimobilis UT26 at 0.95 A resolution: dynamics of catalytic residues.";
RL Biochemistry 43:870-878(2004).
RN [13] {ECO:0007744|PDB:2BFN}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH
RP 2,3-DICHLOROPROPAN-1-OL AND CHLORIDE.
RX PubMed=17259360; DOI=10.1128/aem.02416-06;
RA Monincova M., Prokop Z., Vevodova J., Nagata Y., Damborsky J.;
RT "Weak activity of haloalkane dehalogenase LinB with 1,2,3-trichloropropane
RT revealed by X-Ray crystallography and microcalorimetry.";
RL Appl. Environ. Microbiol. 73:2005-2008(2007).
RN [14] {ECO:0007744|PDB:4WDQ, ECO:0007744|PDB:4WDR, ECO:0007744|PDB:5LKA}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF WILD-TYPE AND MUTANTS TRP-177 AND
RP ALA-140/LEU-143/TRP-177/LEU-211, AND MUTAGENESIS STUDIES.
RX DOI=10.1021/acscatal.6b02081;
RA Brezovsky J., Babkova P., Degtjarik O., Fortova A., Gora A., Iermak I.,
RA Rezacova P., Dvorak P., Kuta Smatanova I., Prokop Z., Chaloupkova R.,
RA Damborsky J.;
RT "Engineering a de novo transport tunnel.";
RL ACS Catal. 6:7597-7610(2016).
CC -!- FUNCTION: Catalyzes hydrolytic cleavage of carbon-halogen bonds in
CC halogenated aliphatic compounds, leading to the formation of the
CC corresponding primary alcohols, halide ions and protons. Has a broad
CC substrate specificity since not only monochloroalkanes (C3 to C10) but
CC also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic
CC alcohols are good substrates (PubMed:9293022, PubMed:10100638). Shows
CC almost no activity with 1,2-dichloroethane, but very high activity with
CC the brominated analog (PubMed:9293022). Is involved in the degradation
CC of the important environmental pollutant gamma-hexachlorocyclohexane
CC (gamma-HCH or lindane) as it also catalyzes conversion of 1,3,4,6-
CC tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-
CC cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-
CC trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL) (PubMed:7691794). This
CC degradation pathway allows S.japonicum UT26 to grow on gamma-HCH as the
CC sole source of carbon and energy. {ECO:0000269|PubMed:10100638,
CC ECO:0000269|PubMed:7691794, ECO:0000269|PubMed:9293022}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-haloalkane + H2O = a halide anion + a primary alcohol +
CC H(+); Xref=Rhea:RHEA:19081, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15734, ChEBI:CHEBI:16042, ChEBI:CHEBI:18060; EC=3.8.1.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01231,
CC ECO:0000269|PubMed:10100638, ECO:0000269|PubMed:9293022};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R,6R)-1,3,4,6-tetrachlorocyclohexa-1,4-diene + 2 H2O = 2,5-
CC dichlorocyclohexa-2,5-dien-1,4-diol + 2 chloride + 2 H(+);
CC Xref=Rhea:RHEA:11944, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:18904, ChEBI:CHEBI:28975;
CC Evidence={ECO:0000269|PubMed:7691794};
CC -!- ACTIVITY REGULATION: Competitively inhibited by the key pollutants 1,2-
CC dichloroethane (1,2-DCE) and 1,2-dichloropropane (1,2-DCP).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 mM for 1,2-dibromoethane {ECO:0000269|PubMed:9293022};
CC KM=3.9 mM for 1-chloro-2-bromoethane {ECO:0000269|PubMed:9293022};
CC KM=0.9 mM for 1,2-dibromopropane {ECO:0000269|PubMed:9293022};
CC KM=0.05 mM for 1-bromo-2-methylpropane {ECO:0000269|PubMed:9293022};
CC KM=0.7 mM for 2,3-dichloropropene {ECO:0000269|PubMed:9293022};
CC KM=0.14 mM for 1-chlorobutane {ECO:0000269|PubMed:10100638};
CC Note=kcat is 0.98 sec(-1) with 1-chlorobutane as substrate.
CC {ECO:0000269|PubMed:10100638};
CC pH dependence:
CC Optimum pH is 8.2. {ECO:0000269|PubMed:9293022};
CC -!- PATHWAY: Xenobiotic degradation; gamma-hexachlorocyclohexane
CC degradation. {ECO:0000305|PubMed:7691794}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9293022}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10464214}.
CC -!- INDUCTION: Constitutively expressed.
CC -!- MISCELLANEOUS: Is not N-terminally processed during export, so it may
CC be secreted into the periplasmic space via a hitherto unknown
CC mechanism. {ECO:0000305|PubMed:10464214}.
CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01231}.
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DR EMBL; D14594; BAA03443.2; -; Genomic_DNA.
DR EMBL; AP010803; BAI96793.1; -; Genomic_DNA.
DR PIR; A49896; A49896.
DR RefSeq; WP_013040256.1; NC_014006.1.
DR PDB; 1CV2; X-ray; 1.58 A; A=1-296.
DR PDB; 1D07; X-ray; 2.00 A; A=1-296.
DR PDB; 1G42; X-ray; 1.80 A; A=1-296.
DR PDB; 1G4H; X-ray; 1.80 A; A=1-296.
DR PDB; 1G5F; X-ray; 1.80 A; A=1-296.
DR PDB; 1IZ7; X-ray; 1.58 A; A=2-296.
DR PDB; 1IZ8; X-ray; 2.00 A; A=2-296.
DR PDB; 1K5P; X-ray; 1.80 A; A=2-296.
DR PDB; 1K63; X-ray; 1.80 A; A=2-296.
DR PDB; 1K6E; X-ray; 1.85 A; A=2-296.
DR PDB; 1MJ5; X-ray; 0.95 A; A=1-296.
DR PDB; 2BFN; X-ray; 1.60 A; A=1-296.
DR PDB; 4WDQ; X-ray; 1.58 A; A=2-296.
DR PDB; 4WDR; X-ray; 2.50 A; A/B=4-296.
DR PDB; 5LKA; X-ray; 1.30 A; A=2-296.
DR PDB; 6S06; X-ray; 1.15 A; A=1-296.
DR PDB; 7NFZ; X-ray; 1.55 A; A=1-296.
DR PDBsum; 1CV2; -.
DR PDBsum; 1D07; -.
DR PDBsum; 1G42; -.
DR PDBsum; 1G4H; -.
DR PDBsum; 1G5F; -.
DR PDBsum; 1IZ7; -.
DR PDBsum; 1IZ8; -.
DR PDBsum; 1K5P; -.
DR PDBsum; 1K63; -.
DR PDBsum; 1K6E; -.
DR PDBsum; 1MJ5; -.
DR PDBsum; 2BFN; -.
DR PDBsum; 4WDQ; -.
DR PDBsum; 4WDR; -.
DR PDBsum; 5LKA; -.
DR PDBsum; 6S06; -.
DR PDBsum; 7NFZ; -.
DR AlphaFoldDB; D4Z2G1; -.
DR SMR; D4Z2G1; -.
DR STRING; 452662.SJA_C1-19590; -.
DR ESTHER; sphpi-linb; Haloalkane_dehalogenase-HLD2.
DR EnsemblBacteria; BAI96793; BAI96793; SJA_C1-19590.
DR KEGG; sjp:SJA_C1-19590; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_13_3_5; -.
DR OMA; TLFCQDW; -.
DR BRENDA; 3.8.1.5; 10293.
DR UniPathway; UPA00689; -.
DR Proteomes; UP000007753; Chromosome 1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_01231; Haloalk_dehal_type2; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR023594; Haloalkane_dehalogenase_2.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Detoxification; Direct protein sequencing; Hydrolase;
KW Periplasm; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10464214,
FT ECO:0000269|PubMed:7691794"
FT CHAIN 2..296
FT /note="Haloalkane dehalogenase"
FT /id="PRO_0000216778"
FT DOMAIN 31..155
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:10100638,
FT ECO:0000305|PubMed:12939138, ECO:0000305|PubMed:14744129"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:10100638,
FT ECO:0000305|PubMed:12939138, ECO:0000305|PubMed:14744129"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:10100638,
FT ECO:0000305|PubMed:12939138, ECO:0000305|PubMed:14744129"
FT BINDING 38
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:14744129"
FT BINDING 109
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:14744129,
FT ECO:0000269|PubMed:17259360, ECO:0007744|PDB:1MJ5,
FT ECO:0007744|PDB:2BFN"
FT MUTAGEN 38
FT /note="N->D,E,F,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12450392"
FT MUTAGEN 108
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10100638"
FT MUTAGEN 108
FT /note="D->N: 58% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10100638"
FT MUTAGEN 109
FT /note="W->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12450392"
FT MUTAGEN 132
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10100638"
FT MUTAGEN 151
FT /note="F->L,W,Y: Increase in activity."
FT /evidence="ECO:0000269|PubMed:12450392"
FT MUTAGEN 169
FT /note="F->L: 31% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:12450392"
FT MUTAGEN 244
FT /note="E->Q: 38% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10100638"
FT MUTAGEN 272
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10100638"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:1MJ5"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1MJ5"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:6S06"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:1MJ5"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:1MJ5"
FT STRAND 261..272
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1MJ5"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:1MJ5"
SQ SEQUENCE 296 AA; 33108 MW; 6EEE011B157DBAE1 CRC64;
MSLGAKPFGE KKFIEIKGRR MAYIDEGTGD PILFQHGNPT SSYLWRNIMP HCAGLGRLIA
CDLIGMGDSD KLDPSGPERY AYAEHRDYLD ALWEALDLGD RVVLVVHDWG SALGFDWARR
HRERVQGIAY MEAIAMPIEW ADFPEQDRDL FQAFRSQAGE ELVLQDNVFV EQVLPGLILR
PLSEAEMAAY REPFLAAGEA RRPTLSWPRQ IPIAGTPADV VAIARDYAGW LSESPIPKLF
INAEPGALTT GRMRDFCRTW PNQTEITVAG AHFIQEDSPD EIGAAIAAFV RRLRPA
