PUR8_ECOLI
ID PUR8_ECOLI Reviewed; 456 AA.
AC P0AB89; P25739;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Adenylosuccinate lyase {ECO:0000303|PubMed:1729205, ECO:0000303|PubMed:17531264};
DE Short=ASL {ECO:0000303|PubMed:1729205, ECO:0000303|PubMed:17531264};
DE EC=4.3.2.2 {ECO:0000269|PubMed:17531264};
DE AltName: Full=Adenylosuccinase;
DE Short=ASase;
GN Name=purB; OrderedLocusNames=b1131, JW1117;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1729205; DOI=10.1128/jb.174.1.130-136.1992;
RA He B., Smith J.M., Zalkin H.;
RT "Escherichia coli purB gene: cloning, nucleotide sequence, and regulation
RT by purR.";
RL J. Bacteriol. 174:130-136(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Green S.M., Drabble W.T.;
RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-456.
RC STRAIN=K12;
RX PubMed=1729240; DOI=10.1128/jb.174.2.492-498.1992;
RA Kasahara M., Nakata A., Shinagawa H.;
RT "Molecular analysis of the Escherichia coli phoP-phoQ operon.";
RL J. Bacteriol. 174:492-498(1992).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94 AND LYS-366, AND
RP IDENTIFICATION BY MASS 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 [8]
RP FUNCTION (MICROBIAL INFECTION), AND CATALYTIC ACTIVITY (MICROBIAL
RP INFECTION).
RX PubMed=33926954; DOI=10.1126/science.abe4882;
RA Zhou Y., Xu X., Wei Y., Cheng Y., Guo Y., Khudyakov I., Liu F., He P.,
RA Song Z., Li Z., Gao Y., Ang E.L., Zhao H., Zhang Y., Zhao S.;
RT "A widespread pathway for substitution of adenine by diaminopurine in phage
RT genomes.";
RL Science 372:512-516(2021).
RN [9] {ECO:0007744|PDB:2PTQ, ECO:0007744|PDB:2PTR, ECO:0007744|PDB:2PTS}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-171 AND
RP ASN-171 IN COMPLEX WITH AMP; FUMARATE AND N(6)-(1,2-DICARBOXYETHYL)-AMP,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, REACTION MECHANISM, MUTAGENESIS
RP OF HIS-171 AND SER-295, AND SUBUNIT.
RX PubMed=17531264; DOI=10.1016/j.jmb.2007.04.052;
RA Tsai M., Koo J., Yip P., Colman R.F., Segall M.L., Howell P.L.;
RT "Substrate and product complexes of Escherichia coli adenylosuccinate lyase
RT provide new insights into the enzymatic mechanism.";
RL J. Mol. Biol. 370:541-554(2007).
CC -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC and fumarate. {ECO:0000269|PubMed:17531264}.
CC -!- FUNCTION: (Microbial infection) Catalyzes the conversion of 2-amino-2'-
CC deoxyadenylo-succinate to dZMP and fumarate, when the bacterium is
CC infected by a phage that produces the substrate of this reaction, a
CC step in the synthesis of dZTP (2-amino-2'-deoxyadenosine 5'-
CC triphosphate), which is a nucleotide then used by the phage as a DNA
CC polymerase substrate. {ECO:0000269|PubMed:33926954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate;
CC Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567,
CC ChEBI:CHEBI:456215; EC=4.3.2.2;
CC Evidence={ECO:0000269|PubMed:17531264};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854;
CC Evidence={ECO:0000305|PubMed:17531264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
CC carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide + fumarate; Xref=Rhea:RHEA:23920,
CC ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, ChEBI:CHEBI:58475; EC=4.3.2.2;
CC Evidence={ECO:0000305|PubMed:17531264};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23921;
CC Evidence={ECO:0000305|PubMed:17531264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-amino-2'-deoxyadenylo-succinate = dZMP + fumarate;
CC Xref=Rhea:RHEA:67636, ChEBI:CHEBI:29806, ChEBI:CHEBI:172924,
CC ChEBI:CHEBI:172927; Evidence={ECO:0000269|PubMed:33926954};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67637;
CC Evidence={ECO:0000305|PubMed:33926954};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 2/2. {ECO:0000305|PubMed:17531264}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
CC {ECO:0000305|PubMed:17531264}.
CC -!- PATHWAY: Purine metabolism. {ECO:0000269|PubMed:33926954}.
CC -!- SUBUNIT: Homotetramer. Residues from neighboring subunits contribute
CC catalytic and substrate-binding residues to each active site.
CC {ECO:0000269|PubMed:17531264}.
CC -!- INTERACTION:
CC P0AB89; P0AFG8: aceE; NbExp=2; IntAct=EBI-556534, EBI-542683;
CC -!- INDUCTION: Its expression is under the control of the transcriptional
CC repressor PurR. {ECO:0000269|PubMed:1729205}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M74924; AAA92731.1; -; Genomic_DNA.
DR EMBL; X59307; CAA41996.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74215.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35953.1; -; Genomic_DNA.
DR PIR; S19212; S19212.
DR RefSeq; NP_415649.1; NC_000913.3.
DR RefSeq; WP_000423742.1; NZ_STEB01000016.1.
DR PDB; 2PTQ; X-ray; 2.00 A; A/B=1-456.
DR PDB; 2PTR; X-ray; 1.85 A; A/B=1-456.
DR PDB; 2PTS; X-ray; 2.00 A; A=1-456.
DR PDBsum; 2PTQ; -.
DR PDBsum; 2PTR; -.
DR PDBsum; 2PTS; -.
DR AlphaFoldDB; P0AB89; -.
DR SMR; P0AB89; -.
DR BioGRID; 4262847; 280.
DR DIP; DIP-10608N; -.
DR IntAct; P0AB89; 11.
DR STRING; 511145.b1131; -.
DR iPTMnet; P0AB89; -.
DR jPOST; P0AB89; -.
DR PaxDb; P0AB89; -.
DR PRIDE; P0AB89; -.
DR EnsemblBacteria; AAC74215; AAC74215; b1131.
DR EnsemblBacteria; BAA35953; BAA35953; BAA35953.
DR GeneID; 945695; -.
DR KEGG; ecj:JW1117; -.
DR KEGG; eco:b1131; -.
DR PATRIC; fig|1411691.4.peg.1135; -.
DR EchoBASE; EB1290; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_025566_2_0_6; -.
DR InParanoid; P0AB89; -.
DR OMA; TQVNPCD; -.
DR PhylomeDB; P0AB89; -.
DR BioCyc; EcoCyc:ASL-MON; -.
DR BioCyc; MetaCyc:ASL-MON; -.
DR BRENDA; 4.3.2.2; 2026.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR EvolutionaryTrace; P0AB89; -.
DR PRO; PR:P0AB89; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IDA:EcoCyc.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR Gene3D; 1.10.275.10; -; 1.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR004769; Pur_lyase.
DR InterPro; IPR013539; PurB_C.
DR Pfam; PF08328; ASL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00928; purB; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Lyase;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..456
FT /note="Adenylosuccinate lyase"
FT /id="PRO_0000137878"
FT REGION 90..92
FT /note="AMP"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT ACT_SITE 171
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:17531264"
FT ACT_SITE 295
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:17531264"
FT BINDING 15..16
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 15..16
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTR"
FT BINDING 90..92
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTR"
FT BINDING 91
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 122..123
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 122..123
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTR"
FT BINDING 247
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 247
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 247
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTR"
FT BINDING 296
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 296
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTR"
FT BINDING 301..303
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 301..303
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTR"
FT BINDING 309
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 309
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTR"
FT BINDING 335
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 335
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTR"
FT BINDING 340..344
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTQ"
FT BINDING 340..344
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000269|PubMed:17531264,
FT ECO:0007744|PDB:2PTR"
FT MOD_RES 94
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 366
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 171
FT /note="H->A,N: Reduces catalytic activity about 500-fold."
FT /evidence="ECO:0000269|PubMed:17531264"
FT MUTAGEN 295
FT /note="S->A: Reduces catalytic activity about 1000-fold."
FT /evidence="ECO:0000269|PubMed:17531264"
FT CONFLICT 145
FT /note="P -> A (in Ref. 1; AAA92731)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="I -> L (in Ref. 1; AAA92731)"
FT /evidence="ECO:0000305"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:2PTR"
FT TURN 11..16
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 29..49
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:2PTR"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 143..160
FT /evidence="ECO:0007829|PDB:2PTR"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2PTR"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:2PTR"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 180..200
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:2PTR"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 252..280
FT /evidence="ECO:0007829|PDB:2PTR"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 305..327
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 346..366
FT /evidence="ECO:0007829|PDB:2PTR"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 371..378
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 401..407
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:2PTR"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 430..437
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:2PTR"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:2PTR"
SQ SEQUENCE 456 AA; 51543 MW; 8D1F4546B66795BC CRC64;
MELSSLTAVS PVDGRYGDKV SALRGIFSEY GLLKFRVQVE VRWLQKLAAH AAIKEVPAFA
ADAIGYLDAI VASFSEEDAA RIKTIERTTN HDVKAVEYFL KEKVAEIPEL HAVSEFIHFA
CTSEDINNLS HALMLKTARD EVILPYWRQL IDGIKDLAVQ YRDIPLLSRT HGQPATPSTI
GKEMANVAYR MERQYRQLNQ VEILGKINGA VGNYNAHIAA YPEVDWHQFS EEFVTSLGIQ
WNPYTTQIEP HDYIAELFDC VARFNTILID FDRDVWGYIA LNHFKQKTIA GEIGSSTMPH
KVNPIDFENS EGNLGLSNAV LQHLASKLPV SRWQRDLTDS TVLRNLGVGI GYALIAYQST
LKGVSKLEVN RDHLLDELDH NWEVLAEPIQ TVMRRYGIEK PYEKLKELTR GKRVDAEGMK
QFIDGLALPE EEKARLKAMT PANYIGRAIT MVDELK
