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ARO1_CANGA
ID   ARO1_CANGA              Reviewed;        1579 AA.
AC   Q6FIV4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 135.
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};
GN   OrderedLocusNames=CAGL0M11484g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380959; CAG62820.1; -; Genomic_DNA.
DR   RefSeq; XP_449840.1; XM_449840.1.
DR   AlphaFoldDB; Q6FIV4; -.
DR   SMR; Q6FIV4; -.
DR   STRING; 5478.XP_449840.1; -.
DR   EnsemblFungi; CAG62820; CAG62820; CAGL0M11484g.
DR   GeneID; 2891409; -.
DR   KEGG; cgr:CAGL0M11484g; -.
DR   CGD; CAL0136537; CAGL0M11484g.
DR   VEuPathDB; FungiDB:CAGL0M11484g; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_001201_1_2_1; -.
DR   InParanoid; Q6FIV4; -.
DR   OMA; YCYDDHR; -.
DR   UniPathway; UPA00053; UER00085.
DR   UniPathway; UPA00053; UER00086.
DR   UniPathway; UPA00053; UER00087.
DR   UniPathway; UPA00053; UER00088.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000002428; Chromosome M.
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; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..1579
FT                   /note="Pentafunctional AROM polypeptide"
FT                   /id="PRO_0000406711"
FT   REGION          1..383
FT                   /note="3-dehydroquinate synthase"
FT   REGION          396..862
FT                   /note="EPSP synthase"
FT   REGION          881..1071
FT                   /note="Shikimate kinase"
FT   REGION          1072..1284
FT                   /note="3-dehydroquinase"
FT   REGION          1297..1579
FT                   /note="Shikimate dehydrogenase"
FT   ACT_SITE        259
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        274
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        844
FT                   /note="For EPSP synthase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1189
FT                   /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1218
FT                   /note="Schiff-base intermediate with substrate; for 3-
FT                   dehydroquinate dehydratase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         40..42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         75..78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         106..108
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         111
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         122
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         131..132
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         138
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         144
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         153
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         154
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         171..174
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         186..189
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         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         249
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         263..267
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         270
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         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         286
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         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT   BINDING         355
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         886..893
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
SQ   SEQUENCE   1579 AA;  174232 MW;  51A302AA2AA7CCF8 CRC64;
     MLVKVPILGR ETIHVGYGVR SHIVETIVGL KSSTYVVIND SNVGRVPYFQ ELLSDFEAQL
     PAGSRLLRYV VKPGEANKTR ATKEQIEDYL LSEGCTRDTV IVAVGGGIIG DMIGYVAATF
     MRGVRVVQVP TSLLAMVDSS IGGKTAVDTP LGKNFIGAFW QPEFVLVDIK WLQSLPKREF
     INGMAEVIKT ACIWNADEFQ RLETHADEFL HVVNTPKISE KEGFQLYDTD IESIKEHIFK
     LVLESIKVKA EVVSSDERES SLRNLLNFGH SIGHAYEAIL TPQALHGECV SIGMVKEAEL
     SRYLGILSAT QVARLSKILV AYGLPVSKDE KWFRELTLNK KTPLDTLLKK MSIDKKNDGS
     KKKVVLLETI GKCYGKSAHV VSDEDLRFVL TDETLVYPFN NIPRDQNKTV TPPGSKSISN
     RALVLAALGK GTCRIKNLLH SDDTKHMLTA VQELKGANIS WEDNGETVVL EGQGGSTLVA
     CENDLYLGNA GTASRFLTSV AALVNSTSQK DHVILTGNAR MQQRPIGPLV DSLRNNGIKI
     DYVKNEGCLP LKVHTDSVFK GGRIELAATV SSQYVSSILM CAPYAENPVT LALVGGKPIS
     ILYVEMTIKM MEKFGIKVEK STTEEYTYII PKGHYVNPAE YVIESDASSA TYPLAFAALT
     GTTVTVPNIG SASLQGDARF ATDVLQPMGC SVTQTATSTT VTGPPVGHLK PLKHVDMEPM
     TDAFLTACVV AAVAHDNDPT SKNTTTIEGI ANQRVKECNR IEAMCTQLAK FGVRTNELPD
     GIQVHGLHSI NDLKVPSIGN EAVGVCTYDD HRVAMSFSLL AGMVNSEQPN SSNPTPVRIL
     ERHCTGKTWP GWWDVLHTEL GAQLDGAEPL ELNSMKNAKK SVVIIGMRAA GKTTISRWCA
     AALGYKLVDL DTLFEERYGH GMIKDFVSQH GWEKFREEEA RIFKEVIENY GDAGYVFSSG
     GGLVESSESR RILKSFSKSG GYVLHLHRDI EETIMFLQKD PTRPAYVEEI REVWNRRESW
     YKDCSNFSFF APHCNSEVEF QNLRRAFTKF IRTITGVTTV DIPTRRSAFV CLTFENLTEY
     TNSLKAITYG CDAVEVRVDH LSNMDEDFVS KQISILRAST DGLPIIFTVR TKKQGGKFPD
     EDYETLQKLL ITALKVGVDY IDLELTLPIG IQYKVLNMKR NTKIIGSHHD FASAYPWDHS
     EWENRYNQAL AMDVDIVKFV GMAKSFEDNL MLERFRDSHT TKPLIAINMG AHGRVSRVLN
     TILTPVTSEH LSEVAAPGQL TVAEINRIYT EMGGITKKDF FVVGSPIGHS RSPVLHNTGY
     SVLGLPHHFD KFETTSAEEV KKHLLDNKAN LGGLAVTIPL KLDIIKYMDE LTESAKVIGA
     VNTVIPLGNS KFKGDNTDWL GIRNSLVSNG VPESVSGLSG LVVGAGGTSR AAIFALHKLG
     CQKIFIVNRT TEKLEELVKF FPEEYNIVPI KEAEEAEAVN ETIGVAVNCV PADKPLDAKL
     ESLLERLLLK SSHTHFVSTL VEAAYKPSVT PVMKLAKDKY QWRVVPGAQM LVHQGVAQFE
     TWNNCRAPFK AIYDAVTEI
 
 
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