ID A0A9P5SQV5_9FUNG Unreviewed; 1610 AA. AC A0A9P5SQV5; DT 13-SEP-2023, integrated into UniProtKB/TrEMBL. DT 13-SEP-2023, sequence version 1. DT 08-NOV-2023, entry version 2. DE RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_03143}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=SK {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_03143}; DE Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143}; GN Name=ARO1 {ECO:0000313|EMBL:KAF9335765.1}; GN ORFNames=BG006_010655 {ECO:0000313|EMBL:KAF9335765.1}; OS Podila minutissima. OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina; OC Mortierellomycetes; Mortierellales; Mortierellaceae; Podila. OX NCBI_TaxID=64525 {ECO:0000313|EMBL:KAF9335765.1, ECO:0000313|Proteomes:UP000696485}; RN [1] {ECO:0000313|EMBL:KAF9335765.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NVP1 {ECO:0000313|EMBL:KAF9335765.1}; RX PubMed=33364917; RA Vandepol N., Liber J., Desiro A., Na H., Kennedy M., Barry K., RA Grigoriev I.V., Miller A.N., O'Donnell K., Stajich J.E., Bonito G.; RT "Resolving the Mortierellaceae phylogeny through synthesis of multi-gene RT phylogenetics and phylogenomics."; RL Fungal Divers. 104:267-289(2020). CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic CC reactions in prechorismate polyaromatic amino acid biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. 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:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; 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; CC Evidence={ECO:0000256|ARBA:ARBA00001901, ECO:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; 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:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; 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:0000256|ARBA:ARBA00000172, CC ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; 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:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 2/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 3/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 4/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 5/7. {ECO:0000256|ARBA:ARBA00004842, ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 6/7. {ECO:0000256|ARBA:ARBA00004811, ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000256|ARBA:ARBA00009948}. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase CC family. {ECO:0000256|ARBA:ARBA00006477}. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase CC family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate CC dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the N-terminal section; belongs to the dehydroquinate CC synthase family. {ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase CC family. {ECO:0000256|ARBA:ARBA00009349}. CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate CC cyclases superfamily. Dehydroquinate synthase family. CC {ECO:0000256|HAMAP-Rule:MF_03143}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAF9335765.1}. 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; JAAAUY010000086; KAF9335765.1; -; Genomic_DNA. DR Proteomes; UP000696485; Unassembled WGS sequence. DR CDD; cd00502; DHQase_I; 1. DR CDD; cd08195; DHQS; 1. DR CDD; cd01556; EPSP_synthase; 1. DR CDD; cd01065; NAD_bind_Shikimate_DH; 1. DR CDD; cd00464; SK; 1. DR Gene3D; 3.40.50.1970; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1. DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2. DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00210; EPSP_synth; 1. DR HAMAP; MF_03143; Pentafunct_AroM; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR046346; Aminoacid_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; 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 NCBIfam; TIGR01356; aroA; 1. DR NCBIfam; TIGR01357; aroB; 1. DR NCBIfam; TIGR01093; aroD; 1. DR NCBIfam; TIGR01809; Shik-DH-AROM; 1. DR PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1. DR PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1. DR Pfam; PF01761; DHQ_synthase; 1. DR Pfam; PF01487; DHquinase_I; 1. DR Pfam; PF00275; EPSP_synthase; 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 PRINTS; PR01100; SHIKIMTKNASE. DR SUPFAM; SSF51569; Aldolase; 1. DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1. DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_03143}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03143}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03143}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03143}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03143}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03143}. FT DOMAIN 80..367 FT /note="3-dehydroquinate synthase" FT /evidence="ECO:0000259|Pfam:PF01761" FT DOMAIN 417..849 FT /note="Enolpyruvate transferase" FT /evidence="ECO:0000259|Pfam:PF00275" FT DOMAIN 1329..1410 FT /note="Shikimate dehydrogenase substrate binding N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08501" FT DOMAIN 1447..1508 FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA FT reductase" FT /evidence="ECO:0000259|Pfam:PF01488" FT REGION 1..393 FT /note="3-dehydroquinate synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT REGION 1091..1311 FT /note="3-dehydroquinase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT REGION 1324..1610 FT /note="Shikimate dehydrogenase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 269 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 284 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 837 FT /note="For EPSP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1213 FT /note="Proton acceptor; for 3-dehydroquinate dehydratase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1242 FT /note="Schiff-base intermediate with substrate; for 3- FT dehydroquinate dehydratase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 47..49 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 86..89 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 117..119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 122 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 133 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 142..143 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 149 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 155 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 164 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 165 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 193 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 197..200 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 197 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 259 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 280 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 280 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 296 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 296 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 365 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 894..901 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" SQ SEQUENCE 1610 AA; 175192 MW; 0C82F6DA224CF172 CRC64; MSHPNPHIQK VSILGSETII LGFHIFDYLL RDTLSNFKAS TYVVVTDTNL QKLYLDRFLA SFHRISQELS SGTLPRLLTY VIPPGEESKS RAVKAEIEDY FLAQGCTRDT LVFAMGGGVI GDLVGFVAAT FMRGIPFVQV PTTLLAMVDS SIGGKTAIDT PMAKNPIGAF WQPKRIFIDL AVLETLPERE FVNGMAEVIK TAAIWNHDDF VLLENGAEAI RDAVLKPVRN VEFQGAILES RTAAQQLLLQ VVMASVAVKS YVVTHDERET GMRGLLNFGH SIGHAIEGLV TPKLLHGECV AIGMIKEAEI ARHCGYLSQV AVGRLTRCIQ AYGLPVTMED KFVKNHIGNQ YCSVDELMQV LRVDKKNMGS QKRIVMLSGI GQTLEQKPSN ISDDIIRKVL AASTVVHPRP INQPAVTLSP PGSKSISNRA LVLAALGQGT CRLTGLLHSD DTQVMLTALT KLGAATFEWE NNGDTLVVHG NGGKMHIPDS ELYLGNAGTA ARFLTTVSVL VPPSSISGQK TILTGNARMK QRPIAPLIDA LTANGSELKY MEGQGCLPLE VTPFSHGLAG GEIQLAASIS SQYVSSILLC APYATKEPVT LVLTGGQVIS QPYIDMTIAM MKSFGVNVEA LPNNTYRIPQ VHYVNPAAYL VEADASSATY PLAIAAITGT TCTVPNIGSA SLQGDAGFAV NVLRPMGCTV VQTETSTTVI GPAIGTLKPL AHIDMETMTD AFLTASVLAA VTQPATPGAE NITRISGIAN QRVKECNRIA AMMHELGKFG VTTSETPDGI IVHGHDIASL TPPKDGVKCY DDHRVAMSFS VLASVVPGGT IIREKKCVEK TWPTWWDDLE SKLNGRITDA DLGVPSDHHD YEVKSSSSKK SAGAKSDATI VVIGMRGAGK TSMGRFAART LKRPFEDVDH YFEKTLSTTI PEFIKEHGWP AFREQEAKML TELLAKYPTK HVISCGGGIV ETASSREAFK QYITQGGVVI HLVRNINEIE AYLNRDTTRP MYGESMRDVW ARREAWYREC CNYEFVVAGQ QLKGIEAEDA KEWALVESNF ERFLKVITRA GKGKYASRSQ VVAKPTFFLS LTFPDISPAL PHLSKLTLGS DVIELRVDLL KSSDASGISF RDHVAQQVSL LRRHSDLPIL YTVRSVSQGG QWPDKDIDGM VSLLKDGLEW GVEYLDVEIG LPRSRIDEVL PKKGNTLIVA SWHDCKGTVR WNSDTMEAQY KLAHSISPDV IKLIGTATSM KDNFDCSEFA ARHTKANDLP LIAMNMGAQG QLSRVLNNYL TPVTHKLLPV KAAPGQLTAR DILIARNAVG LLPAKQFYLF GTPIRQSLSP LMHNTSFQSL GLPYTYDLHE TETVDESVVA KMRSKDFGGA SVTIPHKIDV MSKLDEITEE AKAIGAVNTV VPVEQEGKPS ILVGDNTDWL GIYYQIERNL SSTSVAQPQQ MKGLVLGAGG TSRAALYALH RLGVEDISIF NRTMVKAQAV ADSFKNLFDV KVLSSNDLLK GSSASGFDLV VSTVPGTIES ASMFDDSVFG SAKKGVAVEL AYTPRFTRFL KMAQQSGWAT VEGGQVLVEQ GGWQALKWVG RRWDLESVQQ QMDLVQAGRE //