ALF_ECOLI
ID ALF_ECOLI Reviewed; 359 AA.
AC P0AB71; P11604; Q2M9R7;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Fructose-bisphosphate aldolase class 2;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
DE AltName: Full=Fructose-bisphosphate aldolase class II;
GN Name=fbaA; Synonyms=fba, fda; OrderedLocusNames=b2925, JW2892;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / CS520;
RX PubMed=2546007; DOI=10.1111/j.1365-2958.1989.tb00221.x;
RA Alefounder P.R., Perham R.N.;
RT "Identification, molecular cloning and sequence analysis of a gene cluster
RT encoding the class II fructose 1,6-bisphosphate aldolase, 3-
RT phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate
RT dehydrogenase of Escherichia coli.";
RL Mol. Microbiol. 3:723-732(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-27.
RX PubMed=2649077; DOI=10.1042/bj2570529;
RA Alefounder P.R., Baldwin S.A., Perham R.N., Short N.J.;
RT "Cloning, sequence analysis and over-expression of the gene for the class
RT II fructose 1,6-bisphosphate aldolase of Escherichia coli.";
RL Biochem. J. 257:529-534(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [7]
RP MUTAGENESIS OF HIS-108; HIS-111 AND CYS-112.
RX PubMed=8436219; DOI=10.1016/0014-5793(93)81317-s;
RA Berry A., Marshall K.E.;
RT "Identification of zinc-binding ligands in the class II fructose-1,6-
RT bisphosphate aldolase of Escherichia coli.";
RL FEBS Lett. 318:11-16(1993).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP REACTION MECHANISM, AND MUTAGENESIS OF ASN-36; GLN-60; SER-62 AND LYS-326.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10712619; DOI=10.1046/j.1432-1327.2000.01191.x;
RA Zgiby S.M., Thomson G.J., Qamar S., Berry A.;
RT "Exploring substrate binding and discrimination in fructose 1,6-
RT bisphosphate and tagatose 1,6-bisphosphate aldolases.";
RL Eur. J. Biochem. 267:1858-1868(2000).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [10]
RP MALONYLATION AT LYS-9.
RC STRAIN=K12;
RX PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [11]
RP SUCCINYLATION AT LYS-9; LYS-72; LYS-115; LYS-231; LYS-251; LYS-319; LYS-326
RP AND LYS-348.
RC STRAIN=K12;
RX PubMed=21151122; DOI=10.1038/nchembio.495;
RA Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
RT "Identification of lysine succinylation as a new post-translational
RT modification.";
RL Nat. Chem. Biol. 7:58-63(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=8836102; DOI=10.1038/nsb1096-856;
RA Blom N.S., Tetreault S., Coulombe R., Sygusch J.;
RT "Novel active site in Escherichia coli fructose 1,6-bisphosphate
RT aldolase.";
RL Nat. Struct. Biol. 3:856-862(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=8939754; DOI=10.1016/s0969-2126(96)00138-4;
RA Cooper S.J., Leonard G.A., McSweeney S.M., Thompson A.W., Naismith J.H.,
RA Qamar S., Plater A., Berry A., Hunter W.N.;
RT "The crystal structure of a class II fructose-1,6-bisphosphate aldolase
RT shows a novel binuclear metal-binding active site embedded in a familiar
RT fold.";
RL Structure 4:1303-1315(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION
RP STATE ANALOG, AND ACTIVE SITE.
RX PubMed=10080900; DOI=10.1006/jmbi.1999.2609;
RA Hall D.R., Leonard G.A., Reed C.D., Watt C.I., Berry A., Hunter W.N.;
RT "The crystal structure of Escherichia coli class II fructose-1, 6-
RT bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals
RT details of mechanism and specificity.";
RL J. Mol. Biol. 287:383-394(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CADMIUM, AND METAL
RP BINDING SITES.
RX PubMed=12595741; DOI=10.1107/s0907444902023661;
RA Hall D.R., Kemp L.E., Leonard G.A., Marshall K., Berry A., Hunter W.N.;
RT "The organization of divalent cations in the active site of cadmium
RT Escherichia coli fructose-1,6-bisphosphate aldolase.";
RL Acta Crystallogr. D 59:611-614(2003).
CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC the reverse reaction in glycolysis. {ECO:0000269|PubMed:10712619}.
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:10712619};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 mM for fructose-1,6-bisphosphate
CC {ECO:0000269|PubMed:10712619};
CC KM=0.35 mM for tagatose-1,6-bisphosphate
CC {ECO:0000269|PubMed:10712619};
CC Note=The catalytic efficiency measured with fructose-1,6-bisphosphate
CC as substrate is 1440-fold higher than that with tagatose-1,6-
CC bisphosphate.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10080900,
CC ECO:0000269|PubMed:12595741, ECO:0000269|PubMed:8836102,
CC ECO:0000269|PubMed:8939754}.
CC -!- INTERACTION:
CC P0AB71; P0A6Y8: dnaK; NbExp=3; IntAct=EBI-370916, EBI-542092;
CC P0AB71; P0AB71: fbaA; NbExp=4; IntAct=EBI-370916, EBI-370916;
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; X14436; CAA32605.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69092.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75962.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76989.1; -; Genomic_DNA.
DR PIR; S02177; ADEC2A.
DR RefSeq; NP_417400.1; NC_000913.3.
DR RefSeq; WP_000034372.1; NZ_STEB01000001.1.
DR PDB; 1B57; X-ray; 2.00 A; A/B=2-359.
DR PDB; 1DOS; X-ray; 1.67 A; A/B=2-359.
DR PDB; 1GYN; X-ray; 2.00 A; A=2-359.
DR PDB; 1ZEN; X-ray; 2.50 A; A=2-359.
DR PDB; 5GK3; X-ray; 1.80 A; A/B=1-359.
DR PDB; 5GK4; X-ray; 2.00 A; A/B=1-359.
DR PDB; 5GK5; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-359.
DR PDB; 5GK6; X-ray; 1.80 A; A/B=1-359.
DR PDB; 5GK7; X-ray; 1.80 A; A/B=1-359.
DR PDB; 5GK8; X-ray; 2.00 A; A/B=1-359.
DR PDB; 5VJD; X-ray; 1.70 A; A/B=2-359.
DR PDB; 5VJE; X-ray; 1.65 A; A/B=2-359.
DR PDBsum; 1B57; -.
DR PDBsum; 1DOS; -.
DR PDBsum; 1GYN; -.
DR PDBsum; 1ZEN; -.
DR PDBsum; 5GK3; -.
DR PDBsum; 5GK4; -.
DR PDBsum; 5GK5; -.
DR PDBsum; 5GK6; -.
DR PDBsum; 5GK7; -.
DR PDBsum; 5GK8; -.
DR PDBsum; 5VJD; -.
DR PDBsum; 5VJE; -.
DR AlphaFoldDB; P0AB71; -.
DR SMR; P0AB71; -.
DR BioGRID; 4262069; 20.
DR BioGRID; 851736; 2.
DR DIP; DIP-31872N; -.
DR IntAct; P0AB71; 7.
DR STRING; 511145.b2925; -.
DR BindingDB; P0AB71; -.
DR ChEMBL; CHEMBL4912; -.
DR DrugBank; DB03026; Phosphoglycolohydroxamic Acid.
DR iPTMnet; P0AB71; -.
DR SWISS-2DPAGE; P0AB71; -.
DR jPOST; P0AB71; -.
DR PaxDb; P0AB71; -.
DR PRIDE; P0AB71; -.
DR EnsemblBacteria; AAC75962; AAC75962; b2925.
DR EnsemblBacteria; BAE76989; BAE76989; BAE76989.
DR GeneID; 66673198; -.
DR GeneID; 947415; -.
DR KEGG; ecj:JW2892; -.
DR KEGG; eco:b2925; -.
DR PATRIC; fig|1411691.4.peg.3807; -.
DR EchoBASE; EB0278; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_036923_0_0_6; -.
DR InParanoid; P0AB71; -.
DR OMA; QAYCAEK; -.
DR PhylomeDB; P0AB71; -.
DR BioCyc; EcoCyc:FRUCTBISALD-CLASSII-MON; -.
DR BioCyc; MetaCyc:FRUCTBISALD-CLASSII-MON; -.
DR BRENDA; 4.1.2.13; 2026.
DR SABIO-RK; P0AB71; -.
DR UniPathway; UPA00109; UER00183.
DR EvolutionaryTrace; P0AB71; -.
DR PRO; PR:P0AB71; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:EcoCyc.
DR CDD; cd00946; FBP_aldolase_IIA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR PANTHER; PTHR30559; PTHR30559; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Glycolysis; Lyase;
KW Metal-binding; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2649077,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841"
FT CHAIN 2..359
FT /note="Fructose-bisphosphate aldolase class 2"
FT /id="PRO_0000178713"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:10080900"
FT BINDING 62
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000305"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10080900,
FT ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10080900,
FT ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10080900,
FT ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10080900,
FT ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT BINDING 228
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10080900,
FT ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT BINDING 266..268
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT BINDING 287..290
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT MOD_RES 9
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 9
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 9
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 72
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 115
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 231
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 251
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 319
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 326
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MOD_RES 348
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:21151122"
FT MUTAGEN 36
FT /note="N->A: 1.5% of wild-type activity. 5-fold decrease in
FT FBP affinity."
FT /evidence="ECO:0000269|PubMed:10712619"
FT MUTAGEN 60
FT /note="Q->A: 81% of wild-type activity. 1.3-fold decrease
FT in FBP affinity."
FT /evidence="ECO:0000269|PubMed:10712619"
FT MUTAGEN 62
FT /note="S->A: 8% of wild-type activity. 16-fold decrease in
FT FBP affinity."
FT /evidence="ECO:0000269|PubMed:10712619"
FT MUTAGEN 62
FT /note="S->T: 60% of wild-type activity. 2.5-fold decrease
FT in FBP affinity."
FT /evidence="ECO:0000269|PubMed:10712619"
FT MUTAGEN 108
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8436219"
FT MUTAGEN 111
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8436219"
FT MUTAGEN 112
FT /note="C->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:8436219"
FT MUTAGEN 326
FT /note="K->A: 6% of wild-type activity. 2.2-fold decrease in
FT FBP affinity."
FT /evidence="ECO:0000269|PubMed:10712619"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 81..97
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:5VJE"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5VJD"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1ZEN"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 290..306
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:5VJE"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:5VJE"
FT HELIX 331..352
FT /evidence="ECO:0007829|PDB:5VJE"
SQ SEQUENCE 359 AA; 39147 MW; 7A076D9EA62FBEC4 CRC64;
MSKIFDFVKP GVITGDDVQK VFQVAKENNF ALPAVNCVGT DSINAVLETA AKVKAPVIVQ
FSNGGASFIA GKGVKSDVPQ GAAILGAISG AHHVHQMAEH YGVPVILHTD HCAKKLLPWI
DGLLDAGEKH FAATGKPLFS SHMIDLSEES LQENIEICSK YLERMSKIGM TLEIELGCTG
GEEDGVDNSH MDASALYTQP EDVDYAYTEL SKISPRFTIA ASFGNVHGVY KPGNVVLTPT
ILRDSQEYVS KKHNLPHNSL NFVFHGGSGS TAQEIKDSVS YGVVKMNIDT DTQWATWEGV
LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL
