GPDQ_KLEAE
ID GPDQ_KLEAE Reviewed; 274 AA.
AC Q6XBH1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Glycerophosphodiester phosphodiesterase GpdQ {ECO:0000303|PubMed:14711669};
DE Short=GDPD {ECO:0000303|PubMed:16820687};
DE Short=Glycerophosphoryl diester phosphodiesterase {ECO:0000305};
DE EC=3.1.4.46 {ECO:0000269|PubMed:14711669};
DE AltName: Full=Glycerophosphodiesterase {ECO:0000303|PubMed:16820687};
DE AltName: Full=Glycerophosphorylethanolamine phosphodiesterase {ECO:0000305};
DE Short=GPE phosphodiesterase {ECO:0000305};
GN Name=gpdQ {ECO:0000303|PubMed:14711669};
GN Synonyms=ph {ECO:0000312|EMBL:AAO83402.1};
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=251;
RX PubMed=14711669; DOI=10.1128/aem.70.1.404-412.2004;
RA Yu McLoughlin S., Jackson C., Liu J.W., Ollis D.L.;
RT "Growth of Escherichia coli coexpressing phosphotriesterase and
RT glycerophosphodiester phosphodiesterase, using paraoxon as the sole
RT phosphorus source.";
RL Appl. Environ. Microbiol. 70:404-412(2004).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 13048;
RX PubMed=168197; DOI=10.1016/s0021-9258(19)41277-5;
RA Gerlt J.A., Whitman G.J.;
RT "Purification and properties of a phosphohydrolase from Enterobacter
RT aerogenes.";
RL J. Biol. Chem. 250:5053-5058(1975).
RN [3]
RP SUBUNIT, AND CRYSTALLIZATION.
RX PubMed=16820687; DOI=10.1107/s1744309106020021;
RA Jackson C.J., Carr P.D., Kim H.K., Liu J.W., Ollis D.L.;
RT "The purification, crystallization and preliminary diffraction of a
RT glycerophosphodiesterase from Enterobacter aerogenes.";
RL Acta Crystallogr. F 62:659-661(2006).
RN [4]
RP FUNCTION, COFACTOR, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 13048;
RX PubMed=17630782; DOI=10.1021/bi700561k;
RA Ghanem E., Li Y., Xu C., Raushel F.M.;
RT "Characterization of a phosphodiesterase capable of hydrolyzing EA 2192,
RT the most toxic degradation product of the nerve agent VX.";
RL Biochemistry 46:9032-9040(2007).
RN [5]
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RX PubMed=18535849; DOI=10.1007/s00775-008-0392-5;
RA Mirams R.E., Smith S.J., Hadler K.S., Ollis D.L., Schenk G., Gahan L.R.;
RT "Cadmium(II) complexes of the glycerophosphodiester-degrading enzyme GpdQ
RT and a biomimetic N,O ligand.";
RL J. Biol. Inorg. Chem. 13:1065-1072(2008).
RN [6]
RP REACTION MECHANISM.
RX PubMed=19923005; DOI=10.1016/j.jinorgbio.2009.10.012;
RA Hadler K.S., Gahan L.R., Ollis D.L., Schenk G.;
RT "The bioremediator glycerophosphodiesterase employs a non-processive
RT mechanism for hydrolysis.";
RL J. Inorg. Biochem. 104:211-213(2010).
RN [7]
RP REACTION MECHANISM, AND ELECTRONIC STRUCTURE ANALYSIS OF MUTANT ASP-80.
RX PubMed=20163105; DOI=10.1021/ic901950c;
RA Hadler K.S., Mitic N., Yip S.H., Gahan L.R., Ollis D.L., Schenk G.,
RA Larrabee J.A.;
RT "Electronic structure analysis of the dinuclear metal center in the
RT bioremediator glycerophosphodiesterase (GpdQ) from Enterobacter
RT aerogenes.";
RL Inorg. Chem. 49:2727-2734(2010).
RN [8]
RP BIOTECHNOLOGY, AND MUTAGENESIS OF SER-127.
RX PubMed=24239906; DOI=10.1016/j.jinorgbio.2013.10.007;
RA Daumann L.J., Larrabee J.A., Ollis D., Schenk G., Gahan L.R.;
RT "Immobilization of the enzyme GpdQ on magnetite nanoparticles for
RT organophosphate pesticide bioremediation.";
RL J. Inorg. Biochem. 131:1-7(2014).
RN [9] {ECO:0007744|PDB:2DXL, ECO:0007744|PDB:2DXN}
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) IN COMPLEXES WITH ZINC AND COBALT,
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP SUBUNIT.
RX PubMed=17306828; DOI=10.1016/j.jmb.2007.01.032;
RA Jackson C.J., Carr P.D., Liu J.W., Watt S.J., Beck J.L., Ollis D.L.;
RT "The structure and function of a novel glycerophosphodiesterase from
RT Enterobacter aerogenes.";
RL J. Mol. Biol. 367:1047-1062(2007).
RN [10] {ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON, FUNCTION,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=18678932; DOI=10.1107/s1744309108017600;
RA Jackson C.J., Hadler K.S., Carr P.D., Oakley A.J., Yip S., Schenk G.,
RA Ollis D.L.;
RT "Malonate-bound structure of the glycerophosphodiesterase from Enterobacter
RT aerogenes (GpdQ) and characterization of the native Fe2+ metal-ion
RT preference.";
RL Acta Crystallogr. F Struct. Biol. Commun. 64:681-685(2008).
RN [11] {ECO:0007744|PDB:3D03}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COBALT, FUNCTION,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF ASN-80.
RX PubMed=18831553; DOI=10.1021/ja803346w;
RA Hadler K.S., Tanifum E.A., Yip S.H., Mitic N., Guddat L.W., Jackson C.J.,
RA Gahan L.R., Nguyen K., Carr P.D., Ollis D.L., Hengge A.C., Larrabee J.A.,
RA Schenk G.;
RT "Substrate-promoted formation of a catalytically competent binuclear center
RT and regulation of reactivity in a glycerophosphodiesterase from
RT Enterobacter aerogenes.";
RL J. Am. Chem. Soc. 130:14129-14138(2008).
CC -!- FUNCTION: Catalyzes the hydrolysis of the 3'-5' phosphodiester bond of
CC glycerophosphodiesters such as glycerophosphorylethanolamine (GPE), a
CC typical phospholipid metabolite which is probably the natural substrate
CC of the enzyme (PubMed:14711669). In addition, exhibits a broad
CC substrate specificity and can catalyze the hydrolysis of various
CC phosphomonoesters, diesters, triesters and phosphothiolates
CC (PubMed:14711669, PubMed:168197, PubMed:17630782). Preferentially
CC hydrolyzes the phosphate diesters over the phosphonate monoesters
CC (PubMed:17630782). Can hydrolyze the model substrates p-nitrophenyl
CC phosphate (pNPP), bis-(p-nitrophenyl phosphate) (bis(pNPP)) and ethyl
CC p-nitrophenyl phosphate (EtpNPP) (PubMed:168197, PubMed:14711669,
CC PubMed:17306828, PubMed:17630782, PubMed:18678932, PubMed:18831553).
CC Also exhibits activity towards some organophosphate pesticides and is
CC capable of hydrolyzing a close analog of EA 2192, the most toxic and
CC persistent degradation product of the nerve agent VX (PubMed:14711669,
CC PubMed:17630782). {ECO:0000269|PubMed:14711669,
CC ECO:0000269|PubMed:168197, ECO:0000269|PubMed:17306828,
CC ECO:0000269|PubMed:17630782, ECO:0000269|PubMed:18678932,
CC ECO:0000269|PubMed:18831553}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:83408; EC=3.1.4.46;
CC Evidence={ECO:0000269|PubMed:14711669};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycero-3-phosphoethanolamine = ethanolamine + H(+) +
CC sn-glycerol 3-phosphate; Xref=Rhea:RHEA:29319, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57597, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:143890; Evidence={ECO:0000269|PubMed:14711669};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:18678932};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17306828, ECO:0000269|PubMed:17630782,
CC ECO:0000269|PubMed:18678932};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:17306828, ECO:0000269|PubMed:18831553};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC Evidence={ECO:0000269|PubMed:18535849};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17630782};
CC Note=Binds 2 Fe(2+) ions per subunit (PubMed:18678932). Active in the
CC presence of various divalent cations such as Fe(2+), Zn(2+), Cd(2+),
CC Co(2+) and Mn(2+) (PubMed:17306828, PubMed:17630782, PubMed:18535849,
CC PubMed:18678932, PubMed:18831553). Fe(2+) is probably the native metal
CC ion (PubMed:18678932). {ECO:0000269|PubMed:17306828,
CC ECO:0000269|PubMed:17630782, ECO:0000269|PubMed:18535849,
CC ECO:0000269|PubMed:18678932, ECO:0000269|PubMed:18831553};
CC -!- ACTIVITY REGULATION: The active site contains a binuclear metal center,
CC with a fully occupied alpha-metal ion site, and partially occupied
CC beta-metal ion site (PubMed:17306828, PubMed:18678932,
CC PubMed:18831553). The presence of substrate promotes the formation of a
CC catalytically competent binuclear center by significantly enhancing the
CC binding affinity of one of the metal ions in the active site
CC (PubMed:18831553). {ECO:0000269|PubMed:17306828,
CC ECO:0000269|PubMed:18678932, ECO:0000269|PubMed:18831553}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.0 mM for bis(pNPP) (in the presence of Fe(2+))
CC {ECO:0000269|PubMed:18678932};
CC KM=3.5 mM for bis(pNPP) (in the presence of Zn(2+))
CC {ECO:0000269|PubMed:18678932};
CC KM=2.9 mM for bis(pNPP) (in the presence of Zn(2+))
CC {ECO:0000269|PubMed:17306828};
CC KM=1.4 mM for bis(pNPP) (in the presence of Co(2+))
CC {ECO:0000269|PubMed:17306828};
CC KM=0.12 mM for bis(pNPP) (in the presence of Co(2+))
CC {ECO:0000269|PubMed:18831553};
CC Note=kcat is 2.78 sec(-1) with bis(pNPP) as substrate (in the
CC presence of Fe(2+)) (PubMed:18678932). kcat is 0.176 sec(-1) with
CC bis(pNPP) as substrate (in the presence of Zn(2+)) (PubMed:18678932).
CC kcat is 0.107 sec(-1) with bis(pNPP) as substrate (in the presence of
CC Zn(2+)) (PubMed:17306828). kcat is 1.62 sec(-1) with bis(pNPP) as
CC substrate (in the presence of Co(2+)) (PubMed:17306828). kcat is 1.89
CC sec(-1) with bis(pNPP) as substrate (in the presence of Co(2+))
CC (PubMed:18831553). kcat is 15 sec(-1) with bis(pNPP) as substrate (in
CC the presence of Cd(2+)) (PubMed:18535849).
CC {ECO:0000269|PubMed:17306828, ECO:0000269|PubMed:18535849,
CC ECO:0000269|PubMed:18678932, ECO:0000269|PubMed:18831553};
CC pH dependence:
CC Optimum pH is 5.0 for mono- and diesters hydrolysis.
CC {ECO:0000269|PubMed:168197};
CC -!- SUBUNIT: Homohexamer (PubMed:168197, PubMed:17306828, PubMed:18831553).
CC Trimer of dimers (PubMed:17306828). Tends to form a dimer under
CC crystallization conditions (PubMed:16820687).
CC {ECO:0000269|PubMed:168197, ECO:0000269|PubMed:16820687,
CC ECO:0000269|PubMed:17306828, ECO:0000269|PubMed:18831553}.
CC -!- INDUCTION: Induced under phosphate-limiting conditions.
CC {ECO:0000269|PubMed:14711669}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to grow by using
CC dimethyl phosphate (DMP) or the phosphotriesters as phosphorus sources.
CC {ECO:0000269|PubMed:14711669}.
CC -!- BIOTECHNOLOGY: Is of interest for its potential application as a
CC bioremediator in the destruction of organophosphate pesticides and in
CC the detoxification of nerve agents (PubMed:17630782, PubMed:18535849).
CC The Ser127Ala mutant, which possesses improved metal binding abilities,
CC has been immobilized on magnetite nanoparticles and shown to be active
CC for multiple cycles, and could be stored over a prolonged time in the
CC immobilized form without loss of activity. This system has the
CC potential to be of potential use in the bioremediation of
CC organophosphate contaminated waterways (PubMed:24239906).
CC {ECO:0000269|PubMed:17630782, ECO:0000269|PubMed:18535849,
CC ECO:0000269|PubMed:24239906}.
CC -!- MISCELLANEOUS: Diester bonds are cleaved in two separate (non-
CC processive) reactions, indicating that GpdQ may regenerate its active
CC site after the first hydrolysis (PubMed:19923005). The metal ion-
CC bridging hydroxide molecule activates a terminally bound hydroxide
CC nucleophile (PubMed:20163105). {ECO:0000269|PubMed:19923005,
CC ECO:0000269|PubMed:20163105}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC III family. {ECO:0000305}.
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DR EMBL; AY243367; AAO83402.1; -; Genomic_DNA.
DR RefSeq; WP_048229681.1; NZ_PXKX01000007.1.
DR PDB; 2DXL; X-ray; 3.00 A; A/B=1-274.
DR PDB; 2DXN; X-ray; 2.92 A; A/B=1-274.
DR PDB; 2ZO9; X-ray; 2.20 A; B/C=1-274.
DR PDB; 2ZOA; X-ray; 2.40 A; A/B=1-274.
DR PDB; 3D03; X-ray; 1.90 A; A/B/C/D/E/F=1-274.
DR PDBsum; 2DXL; -.
DR PDBsum; 2DXN; -.
DR PDBsum; 2ZO9; -.
DR PDBsum; 2ZOA; -.
DR PDBsum; 3D03; -.
DR SMR; Q6XBH1; -.
DR PATRIC; fig|548.100.peg.3426; -.
DR EvolutionaryTrace; Q6XBH1; -.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07402; MPP_GpdQ; 1.
DR Gene3D; 3.30.750.180; -; 1.
DR Gene3D; 3.60.21.40; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR026575; GpdQ/CpdA-like.
DR InterPro; IPR042281; GpdQ_beta-strand.
DR InterPro; IPR042283; GpdQ_catalytic.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycerol metabolism; Hydrolase; Iron; Metal-binding.
FT CHAIN 1..274
FT /note="Glycerophosphodiester phosphodiesterase GpdQ"
FT /id="PRO_0000453792"
FT BINDING 8
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18678932,
FT ECO:0000305|PubMed:17306828, ECO:0000305|PubMed:18831553,
FT ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA"
FT BINDING 10
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18678932,
FT ECO:0000305|PubMed:17306828, ECO:0000305|PubMed:18831553,
FT ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA"
FT BINDING 50
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18678932,
FT ECO:0000305|PubMed:17306828, ECO:0000305|PubMed:18831553,
FT ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA"
FT BINDING 50
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18678932,
FT ECO:0000305|PubMed:17306828, ECO:0000305|PubMed:18831553,
FT ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA"
FT BINDING 80
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18678932,
FT ECO:0000305|PubMed:17306828, ECO:0000305|PubMed:18831553,
FT ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18678932,
FT ECO:0000305|PubMed:17306828, ECO:0000305|PubMed:18831553,
FT ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA"
FT BINDING 195
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18678932,
FT ECO:0000305|PubMed:17306828, ECO:0000305|PubMed:18831553,
FT ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18678932,
FT ECO:0000305|PubMed:17306828, ECO:0000305|PubMed:18831553,
FT ECO:0007744|PDB:2ZO9, ECO:0007744|PDB:2ZOA"
FT MUTAGEN 80
FT /note="N->A: Strong decrease in affinity for the substrate
FT but 4-fold increase of the kcat. Displays greatly
FT diminished metal ion binding affinity in the beta site."
FT /evidence="ECO:0000269|PubMed:18831553"
FT MUTAGEN 80
FT /note="N->D: Strong decrease in affinity for the substrate
FT and of the kcat. Increases metal ion binding affinity in
FT the beta site."
FT /evidence="ECO:0000269|PubMed:18831553"
FT MUTAGEN 127
FT /note="S->A: Increases the formation of a catalytically
FT active binuclear metal center."
FT /evidence="ECO:0000269|PubMed:24239906"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3D03"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2DXL"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3D03"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3D03"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:3D03"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:3D03"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:3D03"
SQ SEQUENCE 274 AA; 30840 MW; CDAC38387211DE90 CRC64;
MLLAHISDTH FRSRGEKLYG FIDVNAANAD VVSQLNALRE RPDAVVVSGD IVNCGRPEEY
QVARQILGSL NYPLYLIPGN HDDKALFLEY LQPLCPQLGS DANNMRCAVD DFATRLLFID
SSRAGTSKGW LTDETISWLE AQLFEGGDKP ATIFMHHPPL PLGNAQMDPI ACENGHRLLA
LVERFPSLTR IFCGHNHSLT MTQYRQALIS TLPGTVHQVP YCHEDTRPYY DLSPASCLMH
RQVGEQWVSY QHSLAHYAGP WLYDENISCP TEER
