FBPAP_SULTO
ID FBPAP_SULTO Reviewed; 384 AA.
AC F9VMT6;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000303|PubMed:20348906, ECO:0000303|PubMed:21983966};
DE Short=FBP A/P {ECO:0000303|PubMed:21983966};
DE Short=FBP aldolase/phosphatase {ECO:0000303|PubMed:20348906, ECO:0000303|PubMed:21983966};
DE EC=3.1.3.11 {ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983966};
DE EC=4.1.2.13 {ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983966};
DE AltName: Full=Fructose-1,6-bisphosphatase {ECO:0000303|PubMed:15274916};
DE Short=FBPase {ECO:0000303|PubMed:15274916};
GN Name=fbp {ECO:0000303|PubMed:15274916, ECO:0000312|EMBL:BAK54233.1};
GN OrderedLocusNames=STK_03180 {ECO:0000312|EMBL:BAK54233.1};
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=20348906; DOI=10.1038/nature08884;
RA Say R.F., Fuchs G.;
RT "Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral
RT gluconeogenic enzyme.";
RL Nature 464:1077-1081(2010).
RN [3] {ECO:0007744|PDB:1UMG}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-363 IN COMPLEX WITH MAGNESIUM
RP AND FBP (FBPASE FORM), FUNCTION AS A FBPASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, ACTIVE SITE, AND
RP MUTAGENESIS OF ASP-11; HIS-18; ASP-52; ASP-53; GLN-94; ASP-131; ASP-232 AND
RP ASP-233.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=15274916; DOI=10.1016/j.str.2004.03.026;
RA Nishimasu H., Fushinobu S., Shoun H., Wakagi T.;
RT "The first crystal structure of the novel class of fructose-1,6-
RT bisphosphatase present in thermophilic archaea.";
RL Structure 12:949-959(2004).
RN [4] {ECO:0007744|PDB:3R1M}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND DHAP
RP (ALDOLASE FORM), SCHIFF BASE FORMATION WITH DHAP, FUNCTION AS BOTH FBPASE
RP AND FBP ALDOLASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, REACTION MECHANISM, ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF
RP TYR-228.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=21983966; DOI=10.1038/nature10457;
RA Fushinobu S., Nishimasu H., Hattori D., Song H.J., Wakagi T.;
RT "Structural basis for the bifunctionality of fructose-1,6-bisphosphate
RT aldolase/phosphatase.";
RL Nature 478:538-541(2011).
CC -!- FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol
CC condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-
CC phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the
CC dephosphorylation of FBP to fructose-6-phosphate (F6P).
CC {ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:20348906,
CC ECO:0000269|PubMed:21983966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:20348906,
CC ECO:0000269|PubMed:21983966};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983966};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15274916};
CC Note=Can also use Zn(2+) or Mn(2+) in vitro, although with much less
CC efficiency than Mg(2+). {ECO:0000269|PubMed:15274916};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.027 mM for D-fructose 1,6-bisphosphate (when assaying the FBPase
CC activity, at 80 degrees Celsius) {ECO:0000269|PubMed:15274916};
CC KM=0.027 mM for D-fructose 1,6-bisphosphate (when assaying the FBPase
CC activity, at 48 degrees Celsius) {ECO:0000269|PubMed:21983966};
CC KM=0.19 mM for triosephosphates (when assaying the FBP aldolase
CC activity in the anabolic direction, at 48 degrees Celsius)
CC {ECO:0000269|PubMed:21983966};
CC Note=kcat is 2.5 sec(-1) for the FBPase activity (at 80 degrees
CC Celsius) (PubMed:15274916). kcat is 0.62 sec(-1) for the FBPase
CC activity (at 48 degrees Celsius). kcat is 0.91 sec(-1) for the FBP
CC aldolase activity in the anabolic direction (at 48 degrees Celsius).
CC kcat is 0.027 sec(-1) for the FBP aldolase activity in the catabolic
CC direction (at 48 degrees Celsius) (PubMed:21983966).
CC {ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:21983966};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15274916};
CC Temperature dependence:
CC Optimum temperature is over 100 degrees Celsius.
CC {ECO:0000269|PubMed:15274916};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000305|PubMed:20348906, ECO:0000305|PubMed:21983966}.
CC -!- SUBUNIT: Homooctamer; dimer of tetramers.
CC {ECO:0000269|PubMed:15274916}.
CC -!- DOMAIN: Consists of a single catalytic domain, but remodels its active-
CC site architecture via a large structural change to exhibit dual
CC activities. {ECO:0000269|PubMed:21983966}.
CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC {ECO:0000255|HAMAP-Rule:MF_02067, ECO:0000305}.
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DR EMBL; BA000023; BAK54233.1; -; Genomic_DNA.
DR RefSeq; WP_052846263.1; NC_003106.2.
DR PDB; 1UMG; X-ray; 1.80 A; A=2-363.
DR PDB; 3R1M; X-ray; 1.50 A; A=1-384.
DR PDBsum; 1UMG; -.
DR PDBsum; 3R1M; -.
DR AlphaFoldDB; F9VMT6; -.
DR SMR; F9VMT6; -.
DR DIP; DIP-59164N; -.
DR STRING; 273063.STK_03180; -.
DR MoonProt; F9VMT6; -.
DR EnsemblBacteria; BAK54233; BAK54233; STK_03180.
DR GeneID; 42799818; -.
DR KEGG; sto:STK_03180; -.
DR PATRIC; fig|273063.9.peg.371; -.
DR eggNOG; arCOG04180; Archaea.
DR OMA; YMRRHGP; -.
DR OrthoDB; 21175at2157; -.
DR BRENDA; 3.1.3.11; 15396.
DR BRENDA; 4.1.2.13; 15396.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:CAFA.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:CAFA.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0016311; P:dephosphorylation; IDA:CAFA.
DR GO; GO:0006094; P:gluconeogenesis; IDA:CAFA.
DR GO; GO:0006740; P:NADPH regeneration; IDA:CAFA.
DR HAMAP; MF_02067; FBP_aldolase_phosphatase; 1.
DR InterPro; IPR002803; FBPase_V.
DR InterPro; IPR036076; FBPase_V_sf.
DR PANTHER; PTHR38341; PTHR38341; 1.
DR Pfam; PF01950; FBPase_3; 1.
DR PIRSF; PIRSF015647; FBPtase_archl; 1.
DR SUPFAM; SSF111249; SSF111249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Gluconeogenesis; Hydrolase; Lyase;
KW Magnesium; Metal-binding; Reference proteome; Schiff base.
FT CHAIN 1..384
FT /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT /id="PRO_0000437184"
FT ACT_SITE 11
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000305|PubMed:15274916,
FT ECO:0000305|PubMed:21983966"
FT ACT_SITE 228
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000305|PubMed:21983966"
FT ACT_SITE 231
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000269|PubMed:21983966"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG,
FT ECO:0007744|PDB:3R1M"
FT BINDING 18
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0007744|PDB:1UMG"
FT BINDING 18
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000269|PubMed:21983966,
FT ECO:0007744|PDB:3R1M"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG,
FT ECO:0007744|PDB:3R1M"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG,
FT ECO:0007744|PDB:3R1M"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG,
FT ECO:0007744|PDB:3R1M"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG,
FT ECO:0007744|PDB:3R1M"
FT BINDING 90
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0007744|PDB:1UMG"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG,
FT ECO:0007744|PDB:3R1M"
FT BINDING 103..104
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0007744|PDB:1UMG"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG,
FT ECO:0007744|PDB:3R1M"
FT BINDING 132
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0007744|PDB:1UMG"
FT BINDING 132
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000269|PubMed:21983966,
FT ECO:0007744|PDB:3R1M"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21983966"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15274916"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15274916"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG,
FT ECO:0007744|PDB:3R1M"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0000269|PubMed:21983966"
FT BINDING 241..242
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0007744|PDB:1UMG"
FT BINDING 265
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0007744|PDB:1UMG"
FT BINDING 265
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000269|PubMed:21983966,
FT ECO:0007744|PDB:3R1M"
FT BINDING 286
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0007744|PDB:1UMG"
FT BINDING 286
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000269|PubMed:21983966,
FT ECO:0007744|PDB:3R1M"
FT BINDING 347
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:15274916,
FT ECO:0007744|PDB:1UMG"
FT MUTAGEN 11
FT /note="D->A: 930-fold decrease in FBPase catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:15274916"
FT MUTAGEN 18
FT /note="H->A: 1.7-fold increase in FBPase catalytic activity
FT and 5-fold decrease in FBP affinity, leading to a 2.7-fold
FT decrease in FBPase catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:15274916"
FT MUTAGEN 52
FT /note="D->A: 175-fold decrease in FBPase catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:15274916"
FT MUTAGEN 53
FT /note="D->A: 1000-fold decrease in FBPase catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:15274916"
FT MUTAGEN 94
FT /note="Q->A: 1.3-fold increase in FBPase catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:15274916"
FT MUTAGEN 131
FT /note="D->A: 2-fold increase in FBP affinity and 10-fold
FT decrease in FBPase catalytic activity, leading to a 5.5-
FT fold decrease in FBPase catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:15274916"
FT MUTAGEN 228
FT /note="Y->F: Retains the FBPase activity, but loses the FBP
FT aldolase activity."
FT /evidence="ECO:0000269|PubMed:21983966"
FT MUTAGEN 232
FT /note="D->A: 275-fold decrease in FBPase catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:15274916"
FT MUTAGEN 233
FT /note="D->A: 2000-fold decrease in FBPase catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:15274916"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 67..86
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 91..95
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1UMG"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 290..299
FT /evidence="ECO:0007829|PDB:3R1M"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 316..330
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:3R1M"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:3R1M"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:1UMG"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:1UMG"
SQ SEQUENCE 384 AA; 42574 MW; 587904A135E62146 CRC64;
MKTTISVIKA DIGSLAGHHI VHPDTMAAAN KVLASAKEQG IILDYYITHV GDDLQLIMTH
TRGELDTKVH ETAWNAFKEA AKVAKDLGLY AAGQDLLSDS FSGNVRGLGP GVAEMEIEER
ASEPIAIFMA DKTEPGAYNL PLYKMFADPF NTPGLVIDPT MHGGFKFEVL DVYQGEAVML
SAPQEIYDLL ALIGTPARYV IRRVYRNEDN LLAAVVSIER LNLIAGKYVG KDDPVMIVRL
QHGLPALGEA LEAFAFPHLV PGWMRGSHYG PLMPVSQRDA KATRFDGPPR LLGLGFNVKN
GRLVGPTDLF DDPAFDETRR LANIVADYMR RHGPFMPHRL EPTEMEYTTL PLILEKLKDR
FKKESDVYKA KESIYAKEES QGHD
