ID   A0A0D0AM01_9HOMO        Unreviewed;      1590 AA.
AC   A0A0D0AM01;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   08-JUN-2016, entry version 11.
DE   RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|PIRNR:PIRNR000514};
GN   ORFNames=CY34DRAFT_804457 {ECO:0000313|EMBL:KIK42886.1};
OS   Suillus luteus UH-Slu-Lm8-n1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Suillineae; Suillaceae;
OC   Suillus.
OX   NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485};
RN   [1] {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK42886.1,
RC   ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RA   Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA   Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA   LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA   Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S.,
RA   Martin F., Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC       reactions in prechorismate polyaromatic amino acid biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00063920}.
CC   -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC       {ECO:0000256|SAAS:SAAS00063907}.
CC   -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
CC       = 3-dehydroquinate + phosphate. {ECO:0000256|SAAS:SAAS00312678}.
CC   -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
CC       {ECO:0000256|SAAS:SAAS00280981}.
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC       phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC       {ECO:0000256|SAAS:SAAS00063899}.
CC   -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC       NADPH. {ECO:0000256|SAAS:SAAS00063916}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000514};
CC       Note=Binds 2 Zn(2+) ions per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000514};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis. {ECO:0000256|SAAS:SAAS00540624}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 2/7. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00312729}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 3/7. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00063915}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 4/7. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00063894}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 5/7. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00280976}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 6/7. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00063895}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00063904}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00280982}.
CC   -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
CC       family. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00534655}.
CC   -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
CC       family. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00534726}.
CC   -!- SIMILARITY: In the 4th section; belongs to the type-I 3-
CC       dehydroquinase family. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00534671}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00534692}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       dehydroquinate synthase family. {ECO:0000256|PIRNR:PIRNR000514,
CC       ECO:0000256|SAAS:SAAS00534763}.
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DR   EMBL; KN835227; KIK42886.1; -; Genomic_DNA.
DR   EnsemblFungi; KIK42886; KIK42886; CY34DRAFT_804457.
DR   Proteomes; UP000054485; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:InterPro.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00109; Shikimate_kinase; 1.
DR   HAMAP; MF_00110; DHQ_synthase; 1.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   HAMAP; MF_03143; Pentafunct_AroM; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR006264; EPSP_synthase.
DR   InterPro; IPR023193; EPSP_synthase_CS.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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; IPR022893; Shikimate_DH_fam.
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; 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; 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.
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000514,
KW   ECO:0000256|SAAS:SAAS00448322};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR000514,
KW   ECO:0000256|SAAS:SAAS00448321};
KW   ATP-binding {ECO:0000256|SAAS:SAAS00415286};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054485};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR000514,
KW   ECO:0000256|SAAS:SAAS00415327};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415285};
KW   Lyase {ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415747};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000514,
KW   ECO:0000256|SAAS:SAAS00415337};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS00415250};
KW   NADP {ECO:0000256|SAAS:SAAS00415255};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00435981};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000514,
KW   ECO:0000256|SAAS:SAAS00415348};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054485};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000514,
KW   ECO:0000256|SAAS:SAAS00415343};
KW   Zinc {ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415282}.
FT   DOMAIN       80    363       DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
FT   DOMAIN      417    845       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   DOMAIN     1307   1388       Shikimate_dh_N. {ECO:0000259|Pfam:
FT                                PF08501}.
FT   DOMAIN     1424   1476       Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
SQ   SEQUENCE   1590 AA;  170223 MW;  EF30A9B7658682A2 CRC64;
     MDTVPDILKV SILGRESIHC GFHLIPYIAH TVLTTLPASV YVLVTDTNVA QFYLSAFEKA
     FSAEISKLSS AKPRFLSRVI FPGETTKSRE GKADIEDFLL LERCTRDTVI LALGGGVIGD
     LVGFVAATFM RGVRFVQIPT TLLAMVDSSV GGKTAIDTPA GKNLIGAFWQ PEYIFIDAAF
     LESLPEREFS NGMAEVVKTA AIWDETEFTS LESNAQLIYN AIRTPSTGNA GRHISTRSTS
     QSLLLSVIRG SIYVKSHIVT IDERETGLRN LVNFGHTIGH AIEAVLTPHM LHGECVSIGM
     IFEAEVSRAM GILKQVAVGR LVRCLRAYGL PVSLADQRVT RCPGARGLGV DRLLDIMRVD
     KKNSGPQKKV VILSSIGATY EQKATAVDDA LIAKVLSEAV TVKVDLSTTS GIQHVKMATP
     GSKSISNRAL VLAALAQGTC RLKNLLHSDD TQVMMAALQE LKGASFAWED GGETLVVTGG
     AGSLEVPTAG KEIYLGNAGT AARFLTTVCS LVSPSAAPDA GTATIITGNA RMKQRPIGPL
     VDALRANGSE ITYNESEGCL PLSIAPKGLQ GGVIRLAASV SSQYVSSILL CAPYAREAVT
     LELVGGAVIS QPYIDMTIAM MRTFGVLVTR DPGTDVYRIP QGTYVNPAQY AIESDASSAT
     YPLAIAAITG TKCTLENIGS ESLQGDARFA VDVLARMGCE VVQTANETTV TGPKRGELKA
     IGEVDMEPMT DAFLTACALA AVAQGGEGNT TRILGIANQR VKECNRIKAM IDQLAKFGVQ
     TKELDDGLEV YGCPFNTLTR GASVHCYDDH RVAMAFSVLG TVVPDTIIEE KRCVEKTWPN
     WWDDLENKIG LKVGGIELPR AEGSNTATSG TPSPAASASV ILIGMRGSGK SHIGKLASAA
     LSRQFIDADI YFETKHNIGV REFVSVNGWP AFRAAETELL KEIIQKAGTG HVISMGGGIV
     ETPQARDVLK DYAKTGPVVH VLRDIEEIVN YLGDETARPA YGEPITEVFK RREPWFIECA
     NYDFVNHITV GDSEATNSEI SRFFKHITGQ PNLSENVAAG KRSYFVALTY PDVIPALRHM
     SDLTTGVDAV ELRVDLLRAH NALGAIPSQA YVTAQLAALR RATSLPIIFT VRTISQGGAF
     PDNSERDAFE LLALALRLGV EYIDVEISAS ERLITELAAR KGFSQIIASW HDWSGKMKWN
     EDVVRSKYTL ASRFGDIVKI VGKADTLQDN FVLHDFVAKA NLQRGAKPII AINMGVEGQM
     SRILNATLSP VTHPLLPSKA APGQLSFAQI QKALNLLGQL PAKRYFLFGN PIAHSMSPTL
     HNTGFEVLGL PHTYELLETA SVGEELKATL AAPDFGGASV TIPFKLDVIP LLDKLSPAAE
     AIGAVNTIIP VIEEGNRILY GDNTDWLGIR ESIRSRAPSI GAPAAALVIG AGGTARAAIF
     ALQSLGAQRI YLFNRTASKA QALVDAFPDA PVKLIETLDV WPAEGPAPTV IVSTVPASAT
     TTDGTSPGAV LLPLALFDAT ANGVVVDMAY KPAETPLLTL AKSAAPKWAR VMGVEVLLEQ
     GYVQFETWTG RRCPKHVVSK SVLEKYFAAA
//