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ARO1_YEAS8
ID   ARO1_YEAS8              Reviewed;        1588 AA.
AC   C8Z543;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Pentafunctional AROM polypeptide {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=DHQS {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_03143};
DE     AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=SK {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_03143};
GN   Name=ARO1 {ECO:0000255|HAMAP-Rule:MF_03143}; ORFNames=EC1118_1D0_3829g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC       reactions in prechorismate polyaromatic amino acid biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC         dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC         Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC         EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC         carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03143};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit.;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
CC       cyclases superfamily. Dehydroquinate synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
CC       family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
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DR   EMBL; FN393063; CAY78632.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8Z543; -.
DR   SMR; C8Z543; -.
DR   TopDownProteomics; C8Z543; -.
DR   EnsemblFungi; CAY78632; CAY78632; EC1118_1D0_3829g.
DR   HOGENOM; CLU_001201_1_2_1; -.
DR   UniPathway; UPA00053; UER00085.
DR   UniPathway; UPA00053; UER00086.
DR   UniPathway; UPA00053; UER00087.
DR   UniPathway; UPA00053; UER00088.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000000286; Chromosome IV, Scaffold EC1118_1D0.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00502; DHQase_I; 1.
DR   CDD; cd01556; EPSP_synthase; 1.
DR   CDD; cd00464; SK; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   HAMAP; MF_03143; Pentafunct_AroM; 1.
DR   HAMAP; MF_00109; Shikimate_kinase; 1.
DR   InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR006264; EPSP_synthase.
DR   InterPro; IPR023193; EPSP_synthase_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008289; Pentafunct_AroM.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR010110; Shikimate_DH_AroM-type.
DR   InterPro; IPR000623; Shikimate_kinase/TSH1.
DR   InterPro; IPR023000; Shikimate_kinase_CS.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   Pfam; PF01202; SKI; 1.
DR   PIRSF; PIRSF000514; Pentafunct_AroM; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01356; aroA; 1.
DR   TIGRFAMs; TIGR01357; aroB; 1.
DR   TIGRFAMs; TIGR01093; aroD; 1.
DR   TIGRFAMs; TIGR01809; Shik-DH-AROM; 1.
DR   PROSITE; PS01028; DEHYDROQUINASE_I; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW   Cytoplasm; Kinase; Lyase; Metal-binding; Multifunctional enzyme; NADP;
KW   Nucleotide-binding; Oxidoreductase; Transferase; Zinc.
FT   CHAIN           1..1588
FT                   /note="Pentafunctional AROM polypeptide"
FT                   /id="PRO_0000406751"
FT   REGION          1..392
FT                   /note="3-dehydroquinate synthase"
FT   REGION          405..871
FT                   /note="EPSP synthase"
FT   REGION          890..1080
FT                   /note="Shikimate kinase"
FT   REGION          1081..1293
FT                   /note="3-dehydroquinase"
FT   REGION          1306..1588
FT                   /note="Shikimate dehydrogenase"
FT   ACT_SITE        268
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        283
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        853
FT                   /note="For EPSP synthase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1198
FT                   /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1227
FT                   /note="Schiff-base intermediate with substrate; for 3-
FT                   dehydroquinate dehydratase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         43..45
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         78..81
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         109..111
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         114
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         125
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         134..135
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         141
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         147
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         157
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         174..177
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         189..192
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         258
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         272..276
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         279
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         295
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         364
FT                   /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT                   /ligand_id="ChEBI:CHEBI:58394"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         895..902
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
SQ   SEQUENCE   1588 AA;  174739 MW;  B7CCED2C799B1080 CRC64;
     MVQLAKVPIL GNDIIHVGYN IHDHLVETII KHCPSSTYVI CNDTNLSKVP YYQQLVLEFK
     ASLPEGSRLL TYVVKPGETS KSRETKAQLE DYLLVEGCTR DTVMVAIGGG VIGDMIGFVA
     STFMRGVRVV QVPTSLLAMV DSSIGGKTAI DTPLGKNFIG AFWQPKFVLV DIKWLETLAK
     REFINGMAEV IKTACIWNAD EFTRLESNAS LFLNVVNGAK NVKVTNQLTN EIDEISNTDI
     EAMLDHTYKL VLESIKVKAE VVSSDERESS LRNLLNFGHS IGHAYEAILT PQALHGECVS
     IGMVKEAELS RYFGILSPTQ VARLSKILVA YGLPVSPDEK WFKELTLHKK TPLDILLKKM
     SIDKKNEGSK KKVVILESIG KCYGDSAQFV SDEDLRFILT DETLVYPFKD IPADQQKVVI
     PPGSKSISNR ALILAALGEG QCKIKNLLHS DDTKHMLTAV HELKGATISW EDNGETVVVE
     GHGGSTLSAC ADPLYLGNAG TASRFLTSLA ALVNSTPSQK YIVLTGNARM QQRPIAPLVD
     SLRANGTKIE YLNNEGSLPI KVYTDSVFKG GRIELAATVS SQYVSSILMC APYAEEPVTL
     ALVGGKPISK LYVDMTIKMM EKFGINVETS TTEPYTYYIP KGHYINPSEY VIESDASSAT
     YPLAFAAMTG TTVTVPNIGF ESLQGDARFA RDVLKPMGCK ITQTATSTTV SGPPVGTLKP
     LKHVDMEPMT DAFLTACVVA AISHDSDPNS ANTTTIEGIA NQRVKECNRI LAMATELAKF
     GVKTTELPDG IQVHGLNSIK DLKVPSDSSG PVGVCTYDDH RVAMSFSLLA GMVNSQNERD
     EVANPVRILE RHCTGKTWPG WWDVLHSELG AKLDGAEPLE CTSKKNSKKS VVIIGMRAAG
     KTTISKWCAS ALGYKLVDLD ELFEQQHNNQ SVKQFVVENG WEKFREEETR IFKEVIQNYG
     DDGYVFSTGG GIVESAESRK ALKDFASSGG YVLHLHRDIE ETIVFLQSDP SRPAYVEEIR
     EVWNRREGWY KECSNFSFFA PHCSAEAEFQ ALRRSFSKHI ATITGVREIE IPSGRSAFVC
     LTFDDLTEQT ENLTPICYGC EAVEVRVDHL ANYSADFVSK QLSILRKATD SIPIIFTVRT
     MKQGGNFPDE EFKTLRELYD IALKNGVEFL DLELTLPTDI QYEVINKRGN TKIIGSHHDF
     QGLYSWDDAE WENRFNQALT LDVDVVKFVG TAVNFEDNLR LEHFRDTHKN KPLIAVNMTS
     KGSISRVLNN VLTPVTSDLL PNSAAPGQLT VAQINKMYTS MGGIEPKELF VVGKPIGHSR
     SPILHNTGYE ILGLPHKFDK FETESAQLVK EKLLDGNKNF GGAAVTIPLK LDIMQYMDEL
     TDAAKVIGAV NTVIPLGNKK FKGDNTDWLG IRNALINNGV PEYVGHTAGL VIGAGGTSRA
     ALYALHSLGC KKIFIINRTT SKLKPLIESL PSEFNIIGIE STKSIEEIKE HVGVAVSCVP
     ADKPLDDELL SKLERFLVKG AHAAFVPTLL EAAYKPSVTP VMTISQDKYQ WHVVPGSQML
     VHQGVAQFEK WTGFKGPFKA IFDAVTKE
 
 
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