ID K5VT63_AGABU Unreviewed; 1590 AA. AC K5VT63; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 14-MAY-2014, entry version 14. DE RecName: Full=Pentafunctional AROM polypeptide; GN ORFNames=AGABI1DRAFT_61742; OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / OS FGSC 10392) (White button mushroom). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Agaricales; Agaricaceae; Agaricus. OX NCBI_TaxID=597362; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392; RX PubMed=23045686; DOI=10.1073/pnas.1206847109; RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., RA Nagy L.G., Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., RA Bailey A.M., Billette C., Coutinho P.M., Deakin G., Doddapaneni H., RA Floudas D., Grimwood J., Hilden K., Kuees U., LaButti K.M., RA Lapidus A., Lindquist E.A., Lucas S.M., Murat C., Riley R.W., RA Salamov A.A., Schmutz J., Subramanian V., Woesten H.A.B., Xu J., RA Eastwood D.C., Foster G.D., Sonnenberg A.S., Cullen D., de Vries R.P., RA Lundell T., Hibbett D.S., Henrissat B., Burton K.S., Kerrigan R.W., RA Challen M.P., Grigoriev I.V., Martin F.; RT "Genome sequence of the button mushroom Agaricus bisporus reveals RT mechanisms governing adaptation to a humic-rich ecological niche."; RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012). CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic CC reactions in prechorismate polyaromatic amino acid biosynthesis CC (By similarity). CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate CC = 3-dehydroquinate + phosphate. CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate + CC NADPH. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 3/7. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 4/7. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 5/7. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 6/7. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase CC family. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase CC family. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3- CC dehydroquinase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate CC dehydrogenase family. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC dehydroquinate synthase family. 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; JH971395; EKM77624.1; -; Genomic_DNA. DR OrthoDB; EOG7KQ28X; -. DR UniPathway; UPA00053; UER00085. 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; IPR018508; 3-dehydroquinate_DH_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016037; DHQ_synth_AroB. 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; 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; IPR022893; Shikimate_quinate_DH. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR PANTHER; PTHR21090:SF1; PTHR21090:SF1; 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; 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; 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; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Lyase; KW Metal-binding; Multifunctional enzyme; NADP; Nucleotide-binding; KW Oxidoreductase; Transferase; Zinc. SQ SEQUENCE 1590 AA; 171224 MW; 10E9617755A2190E CRC64; MPEADIFKVP ILGKDSIHCG FHLIPYIAHT VISTLPSSTY VLITDTNIAK FHLKSFEDVF QSTLDTHNAS GAKPRFISLV IPPGETSKSR DGKAQIEDFL LLNKCTRDTV VLALGGGVIG DLVGFVSATF MRGVRFVQIP TTLLAMVDSS VGGKTAIDTP HGKNLIGAFW QPEYIFIDAA FLETLPQREF SNGMAEVVKT AAIWNENEFL SLEARSAEIF TAIQTPSENF AGRTKDTRSA AQELLLSVIV GSISVKAHIV TIDERETGLR NLVNFGHSIG HAIEAVLTPT ILHGECVSIG MILEAELSRQ MGILSQVGVG RLSRCLKAYN LPISVSDPRI ASLPAARLLT VDRLLDIMRI DKKNSGNEKK IVILSRIGAT YEQKATVVKD ALIFKTLSEA AKVIPGIPSH NPVVMSTPGS KSISNRALVL AALGKGTCRL RNLLHSDDTQ VMMAALGELK GAKFSWEDNG DTLVVEGGQG FLAVPPKGKE LYLGNAGTAA RFLTTVCTLV QASPKDNADV TIITGNARMK QRPNGPLVTA LRTNGSQIKC LETEGCLPLA IAPEGLKGGT IQLAASVSSQ YVSSILLCAP YAAQPVTLEL TGGQVISQPY IDMTIAMMKT FGVEVKRRVD SASGKLLDTY DIPKAVYVSP PNYSIESDAS SATYPLAIAA ITGTSCTIDN IGTSSLQGDA KFAKEVLEKM GCTVSQTETQ TTVQGPPIGG LKAIEEVDME IMTDAFLTAT VVAAVAHGKT RILGIANQRV KECNRIRAMI DQLAKFGVEC IELDDGLEVI GKPISELKRG ASVHCYDDHR VAMAFSVLST VVENTIIEEK RCVEKTWPNW WDDLENKIGI KVEGVDLAGL HAKASVSGTR NFDPSASVVL IGMRGVGKSF IGDLAANALG WPQLDADDYF AEVKKQALRD FVTEHGWPAF REAEVEVLGE LLKEKATGHV ISLGGGIVET PAARELIKQY ASTTGPVVHV TRPLDEILAY LGAESARPAY GEPVADVYHR RHPWYTDISN YEFLNPVGAS SVVTSPSAGV HEEVARFFKH ITGQKPNLSS NVGAGKRSYF LSLTYPDITE ALSIVEQISE GVDALELRVD LLKSSKESDA IPSTDYVASQ LAALRRVTSL PIVYTVRTSS QGGKHPDKAE KEALELLELG LKAAVEYLDV EITLPEQKVR ELASKKGRSQ IIASYHDFSG NLKWNSVAVK EKYDIAEGLG DIIKIIGTAN AIQDNFELHN FITSVNSKPN AKPIIAVNMG TQGQLSRILN ETFTPVTHPL LPIKAAPGQL SFKQIQEALT LVGQLPAKQF YLFGNPIAHS MSPTLHNTGF QVLGLPHKYS LLETQQFNEQ NKEAITAANF GGASVTIPYK LDVIPSLDEL TPAAKAIGAV NTVIPTISGG KRVLVGDNTD WIGIRKSIIA QLSTGVVGNG LVIGGGGTAR AAIYALQSLN AETVYLWNRT KSKAEDLARA FPNARVQVLD RLGAWTSAPP NVIVGTVPAS ATTLEEGAPS ATLLTADLYQ YRDGPAVVVD MAYKPAQTPL LQLASVTSNW KTVRGLDVLL EQGYEQFELW TGRRCPRKIV GEKVTEKYDA //