GAPN_THETE
ID GAPN_THETE Reviewed; 501 AA.
AC O57693;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE EC=1.2.1.90 {ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334};
DE AltName: Full=Glyceraldehyde phosphate dehydrogenase (NAD(P));
DE Short=GAPN;
GN Name=gapN;
OS Thermoproteus tenax.
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=2271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=KRA 1;
RX PubMed=9497334; DOI=10.1074/jbc.273.11.6149;
RA Brunner N.A., Brinkmann H., Siebers B., Hensel R.;
RT "NAD+-dependent GAPDH from Thermoproteus tenax - the first identified
RT archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic
RT enzyme with unusual regulatory properties.";
RL J. Biol. Chem. 273:6149-6156(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=KRA 1;
RX PubMed=3121324; DOI=10.1111/j.1432-1033.1987.tb13703.x;
RA Hensel R., Laumann S., Lang J., Heumann H., Lottspeich F.;
RT "Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from
RT the extremely thermophilic archaebacterium Thermoproteus tenax.";
RL Eur. J. Biochem. 170:325-333(1987).
RN [3] {ECO:0007744|PDB:1KY8}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
RX PubMed=11842090; DOI=10.1074/jbc.m112244200;
RA Pohl E., Brunner N., Wilmanns M., Hensel R.;
RT "The crystal structure of the allosteric non-phosphorylating
RT glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic
RT archaeum Thermoproteus tenax.";
RL J. Biol. Chem. 277:19938-19945(2002).
RN [4] {ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP, ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR, ECO:0007744|PDB:1UXT, ECO:0007744|PDB:1UXU, ECO:0007744|PDB:1UXV}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH
RP GLYCERALDEHYDE-3-PHOSPHATE; AMP; FRUCTOSE-6-PHOSPHATE; GLUCOSE-1-PHOSPHATE;
RP NADP AND NAD, ACTIVE SITE, ALLOSTERIC REGULATION, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RX PubMed=15288789; DOI=10.1016/j.jmb.2004.05.032;
RA Lorentzen E., Hensel R., Knura T., Ahmed H., Pohl E.;
RT "Structural basis of allosteric regulation and substrate specificity of the
RT non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from
RT Thermoproteus tenax.";
RL J. Mol. Biol. 341:815-828(2004).
CC -!- FUNCTION: Catalyzes the irreversible NAD(P)-dependent non-
CC phosphorylating oxidation of glyceraldehyde-3-phosphate (GAP) to 3-
CC phosphoglycerate (3PG). It is highly specific for D-GAP.
CC {ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H2O + NADP(+) = (2R)-3-
CC phosphoglycerate + 2 H(+) + NADPH; Xref=Rhea:RHEA:14669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58272, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.90;
CC Evidence={ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H2O + NAD(+) = (2R)-3-
CC phosphoglycerate + 2 H(+) + NADH; Xref=Rhea:RHEA:42760,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58272, ChEBI:CHEBI:59776; EC=1.2.1.90;
CC Evidence={ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334};
CC -!- ACTIVITY REGULATION: Allosterically activated by AMP, ADP, glucose 1-
CC phosphate (G1P), and fructose 6-phosphate (F6P).
CC {ECO:0000269|PubMed:9497334}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for NAD (with G1P as effector)
CC {ECO:0000269|PubMed:9497334};
CC KM=1.3 mM for NAD (with AMP as effector)
CC {ECO:0000269|PubMed:9497334};
CC KM=1.7 mM for NAD (with ADP as effector)
CC {ECO:0000269|PubMed:9497334};
CC KM=3.1 mM for NAD {ECO:0000269|PubMed:3121324};
CC Vmax=32.5 umol/min/mg enzyme with NAD as substrate (with AMP as
CC effector) {ECO:0000269|PubMed:9497334};
CC Vmax=35 umol/min/mg enzyme with NAD as substrate (with G1P as
CC effector) {ECO:0000269|PubMed:9497334};
CC Vmax=36 umol/min/mg enzyme with NAD as substrate (with ADP as
CC effector) {ECO:0000269|PubMed:9497334};
CC Vmax=36 umol/min/mg enzyme with NAD as substrate
CC {ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334};
CC Vmax=14 umol/min/mg enzyme with NADP as substrate
CC {ECO:0000269|PubMed:15288789, ECO:0000269|PubMed:3121324,
CC ECO:0000269|PubMed:9497334};
CC Vmax=31 umol/min/mg enzyme with NADP as substrate (with F6P as
CC effector) {ECO:0000269|PubMed:15288789};
CC Vmax=33 umol/min/mg enzyme with NADP as substrate (with ADP as
CC effector) {ECO:0000269|PubMed:15288789};
CC Vmax=39 umol/min/mg enzyme with NADP as substrate (with AMP as
CC effector) {ECO:0000269|PubMed:15288789};
CC Vmax=43 umol/min/mg enzyme with NADP as substrate (with G1P as
CC effector) {ECO:0000269|PubMed:15288789};
CC Note=Km applies to a data set exhibiting Michaelis-Menten kinetics.
CC When an enzyme does not exhibit Michaelis-Menten kinetics the binding
CC affinity is simply expressed as S0.5 which corresponds to the
CC observed substrate concentration for 0.5 x Vmax. S0.5 is 20 mM for
CC NADP alone, 0.1 mM for NADP with G1P as effector, 0.2 mM for NADP
CC with F6P as effector, 0.15 mM for NADP with AMP as effector and 0.2
CC mM for NADP with ADP as effector.;
CC Temperature dependence:
CC Optimum temperature is 96 degrees Celsius. High thermostability.
CC {ECO:0000269|PubMed:3121324, ECO:0000269|PubMed:9497334};
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000269|PubMed:11842090,
CC ECO:0000269|PubMed:15288789, ECO:0000269|PubMed:3121324}.
CC -!- MISCELLANEOUS: GapN is also able to utilize NADP as a cosubstrate but
CC with remarkably different kinetic properties. In contrast to the NAD-
CC dependent reaction, the NADP-dependent reaction does not follow
CC classical Michaelis-Menten kinetics. The saturation kinetics of the
CC NADP-dependent reaction shows an unexpectedly bumpy curve with several
CC more or less pronounced intermediate plateaus, which can be explained
CC by the assumption that the catalytic or binding constants first
CC decrease, then increase with saturation. The first saturation phase is
CC characterized by negative cooperativity. The later saturation phases
CC display sigmoidal shapes indicating positive cooperativity. The
CC negative cooperativity of the first saturation phase could also explain
CC the strong inhibition of NADP on the NAD-dependent reaction if it is
CC assumed that NADP excludes NAD more efficiently from the vacant
CC cosubstrate-binding site than NADP itself (PubMed:15288789).
CC {ECO:0000305|PubMed:15288789}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Y10625; CAA71651.1; -; Genomic_DNA.
DR PIR; T44939; T44939.
DR PDB; 1KY8; X-ray; 2.40 A; A=1-501.
DR PDB; 1UXN; X-ray; 2.30 A; A=1-501.
DR PDB; 1UXP; X-ray; 2.55 A; A=1-501.
DR PDB; 1UXQ; X-ray; 2.40 A; A=1-501.
DR PDB; 1UXR; X-ray; 2.30 A; A=1-501.
DR PDB; 1UXT; X-ray; 2.20 A; A=1-501.
DR PDB; 1UXU; X-ray; 2.25 A; A=1-501.
DR PDB; 1UXV; X-ray; 2.35 A; A=1-501.
DR PDBsum; 1KY8; -.
DR PDBsum; 1UXN; -.
DR PDBsum; 1UXP; -.
DR PDBsum; 1UXQ; -.
DR PDBsum; 1UXR; -.
DR PDBsum; 1UXT; -.
DR PDBsum; 1UXU; -.
DR PDBsum; 1UXV; -.
DR AlphaFoldDB; O57693; -.
DR SMR; O57693; -.
DR KEGG; ag:CAA71651; -.
DR BRENDA; 1.2.1.90; 6329.
DR SABIO-RK; O57693; -.
DR EvolutionaryTrace; O57693; -.
DR GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase.
FT CHAIN 1..501
FT /note="NAD(P)-dependent glyceraldehyde-3-phosphate
FT dehydrogenase"
FT /id="PRO_0000422654"
FT ACT_SITE 263
FT /evidence="ECO:0000305|PubMed:15288789"
FT ACT_SITE 297
FT /evidence="ECO:0000305|PubMed:15288789"
FT BINDING 72
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXT"
FT BINDING 72
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP,
FT ECO:0007744|PDB:1UXU, ECO:0007744|PDB:1UXV"
FT BINDING 72
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXR"
FT BINDING 79
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXT"
FT BINDING 79
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP,
FT ECO:0007744|PDB:1UXU, ECO:0007744|PDB:1UXV"
FT BINDING 79
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXR"
FT BINDING 134
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXU"
FT BINDING 154..155
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXT"
FT BINDING 154..155
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXU"
FT BINDING 165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXT"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11842090,
FT ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1KY8,
FT ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR,
FT ECO:0007744|PDB:1UXU, ECO:0007744|PDB:1UXV"
FT BINDING 168
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXU"
FT BINDING 184
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXR"
FT BINDING 191..194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11842090,
FT ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1KY8,
FT ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR,
FT ECO:0007744|PDB:1UXU, ECO:0007744|PDB:1UXV"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXT"
FT BINDING 224
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11842090,
FT ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1KY8,
FT ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR,
FT ECO:0007744|PDB:1UXU, ECO:0007744|PDB:1UXV"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXT"
FT BINDING 228
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11842090,
FT ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1KY8,
FT ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR,
FT ECO:0007744|PDB:1UXU, ECO:0007744|PDB:1UXV"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXT"
FT BINDING 244
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11842090,
FT ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1KY8,
FT ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR,
FT ECO:0007744|PDB:1UXU, ECO:0007744|PDB:1UXV"
FT BINDING 265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXT"
FT BINDING 265
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11842090,
FT ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1KY8,
FT ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR,
FT ECO:0007744|PDB:1UXV"
FT BINDING 296..298
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXU"
FT BINDING 395
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXT"
FT BINDING 395
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11842090,
FT ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1KY8,
FT ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP,
FT ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR,
FT ECO:0007744|PDB:1UXV"
FT BINDING 455..456
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|PubMed:15288789,
FT ECO:0007744|PDB:1UXU"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1UXT"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1UXT"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1UXT"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1UXU"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1UXV"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 307..322
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 342..357
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 398..408
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 419..428
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 432..441
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:1UXP"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:1UXT"
FT TURN 475..478
FT /evidence="ECO:0007829|PDB:1UXT"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 483..491
FT /evidence="ECO:0007829|PDB:1UXT"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:1UXT"
SQ SEQUENCE 501 AA; 54090 MW; 22F1C0084282EE1B CRC64;
MRAGLLEGVI KEKGGVPVYP SYLAGEWGGS GQEIEVKSPI DLATIAKVIS PSREEVERTL
DVLFKRGRWS ARDMPGTERL AVLRKAADII ERNLDVFAEV LVMNAGKPKS AAVGEVKAAV
DRLRLAELDL KKIGGDYIPG DWTYDTLETE GLVRREPLGV VAAITPFNYP LFDAVNKITY
SFIYGNAVVV KPSISDPLPA AMAVKALLDA GFPPDAIALL NLPGKEAEKI VADDRVAAVS
FTGSTEVGER VVKVGGVKQY VMELGGGDPA IVLEDADLDL AADKIARGIY SYAGQRCDAI
KLVLAERPVY GKLVEEVAKR LSSLRVGDPR DPTVDVGPLI SPSAVDEMMA AIEDAVEKGG
RVLAGGRRLG PTYVQPTLVE APADRVKDMV LYKREVFAPV ASAVEVKDLD QAIELANGRP
YGLDAAVFGR DVVKIRRAVR LLEVGAIYIN DMPRHGIGYY PFGGRKKSGV FREGIGYAVE
AVTAYKTIVF NYKGKGVWKY E
