ARO1_COPC7
ID ARO1_COPC7 Reviewed; 1677 AA.
AC A8NMB4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 80.
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 ORFNames=CC1G_09809;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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; AACS02000012; EAU86952.2; -; Genomic_DNA.
DR RefSeq; XP_001834882.2; XM_001834830.2.
DR AlphaFoldDB; A8NMB4; -.
DR SMR; A8NMB4; -.
DR STRING; 5346.XP_001834882.2; -.
DR EnsemblFungi; EAU86952; EAU86952; CC1G_09809.
DR GeneID; 6011401; -.
DR KEGG; cci:CC1G_09809; -.
DR VEuPathDB; FungiDB:CC1G_09809; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_001201_1_2_1; -.
DR InParanoid; A8NMB4; -.
DR OMA; YCYDDHR; -.
DR OrthoDB; 39786at2759; -.
DR UniPathway; UPA00053; UER00085.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR UniPathway; UPA00053; UER00088.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000001861; Unassembled WGS sequence.
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; 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 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; 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; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 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..1677
FT /note="Pentafunctional AROM polypeptide"
FT /id="PRO_0000406715"
FT REGION 1..394
FT /note="3-dehydroquinate synthase"
FT REGION 407..858
FT /note="EPSP synthase"
FT REGION 885..1113
FT /note="Shikimate kinase"
FT REGION 1114..1341
FT /note="3-dehydroquinase"
FT REGION 1354..1677
FT /note="Shikimate dehydrogenase"
FT ACT_SITE 270
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 285
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 840
FT /note="For EPSP synthase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1243
FT /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1271
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 50..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 89..92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 120..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 136
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 145..146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 152
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 158
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 167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 168
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 185..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 200..203
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 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 260
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 274..278
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 281
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 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 297
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 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 366
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 892..899
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
SQ SEQUENCE 1677 AA; 180971 MW; 275A2C712F6E4A30 CRC64;
MAVADDTKAD LLKVSILGKE SIHCGFHLTP YIVQTVLTTL PSSTYVLITD DNIAKLHLNK
FEEAFAKGIE KSAANPKPRF LSHVIPPGET SKSREGKARI EDFLLFHKCT RDSVILALGG
GVIGDLVGFV AATFMRGVRF CQIPTTLLAM VDSSVGGKTA IDTPHGKNLI GAFWQPEYIF
IDAAYLETLP TREFSNGMAE VVKTAAIWDE KEFTSLESRS AELFAAIQTP STNYAGRTLE
TRSEAQKLLL STIAASIGVK AHIVTIDERE TGLRNLVNFG HSIGHAIEAV LTPTILHGEC
VSIGMILEAE LSRQLGILTQ VGVGRLTRCL KAYNLPTSLS APLIASLPQA SLLTVPRLLD
IMRIDKKNSG TNKKIVLLKR IGETYEQKAS IVEDKAIEKT LAEAVTVVPS IPTGNVKGSP
GEVRMSTPGS KSISNRALVL AALAKGTCRL RNLLHSDDTQ GAVFTWEDGG ETLVVEGGEG
TLTVPTPGKE LYLGNAGTAA RFLTTVCALA QPAPASVQPP STNTVITGNA RMKQRPIGPL
VDALRANGCS IGYRESEGCL PLSIPPNSFK GGKIQLAASV SSQYVSSILL CAPYAQDANG
VTLELVGGEV ISQPYIDMTI AMMKTFGVEV TRRTDASGKL LDIYDIPRGT YVNPPVYNIE
SDASSATYPL AVAAITGTKC TIENIGSSSL QGDAKFAVEV LQKMGCEVHQ TADETTVQGP
PLGQLKAIEE VDMEVMTDAF LTASVLAAVA NGGENKAMKI TGIANQRVKE CNRIRAMMDE
LAKFGVHTTE QELGLTIYAV PISQLKKNVS VHCYDDHRVA MAFSVLSTVV EGAIIEEKRC
VEKTWPGWWD DLENKIGIKV EGVDLAGLRA ESSSAGVKES KPIDNSSILL IGMRGTGKTH
IGQLAAASLP GWSFVDADHY FESKLKTGVK DFVKNEGWEK FREEELAVLA ELIGLGVDGK
AVSSPSSYSK NHVISLGGGI VETPAARSLL KAYLAKGGRV VHITRPIDEI VRYLNVETAR
PAYEEPILDV WKRREPWYKE CSGWEFGNVV VEAPQGQAQA ANVEAGPGKT KCVKTLAGRN
EVKRFFGHLA GINPNFTHGG SVEGQQRRTY FLCLTYPDVR HAFPYIDELT EGADALELRV
DLLKDAKAPE APFPSVAYVK DQVTALRRVT GLPIIYTVRT KAQGGAFPDG NAKEYKELVE
AGVRLGVEYL DVEVASIFSD KEVADLSKRT KKAGSTLVIA SWHDWSGKMQ WDGEDVKRKY
DEARKFGDLV KIVGKAEKLE DNFKLLSFVK SATSLPNSPP IIAINMSTLG QSSRILNTTF
TPVSHPLLPT KAAPGQLSFK QIQQALHLLG LLPSKHFHLF GTPIAHSMSP TLHNTGFELL
GLPFKYGLLE SKEVDCKEVR DVISDKEGFG GASVTIPFKV DVIELLDELT ESAKEIGAVN
TIIPVHRSSI NAQGQEETTR VLVGDNTDWV GIRVCITQRV SEGELRNENT SGLVIGAGGT
ARAAIYALQD LGVPVIYLFN RTKEKAEDLA KAFVGGADKK WNGQLVVLDK LGGGWGDVGV
APRVIVSTVP ASATALPSAS TAAIAGQVDK STNQIVLPAD VFAYTSGSAV VVDMAYKPAE
TPLLKLAKEL KEEGNWACVQ GLEVLLEQGY IQFEKWTGRR CPKEQVSTRV WEKYGEV
