ID K5VT63_AGABU Unreviewed; 1590 AA. AC K5VT63; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 05-DEC-2018, entry version 56. DE RecName: Full=Pentafunctional AROM polypeptide {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=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}; 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=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}; GN ORFNames=AGABI1DRAFT_61742 {ECO:0000313|EMBL:EKM77624.1}; 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 {ECO:0000313|EMBL:EKM77624.1, ECO:0000313|Proteomes:UP000008493}; RN [1] {ECO:0000313|Proteomes:UP000008493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392 RC {ECO:0000313|Proteomes:UP000008493}; 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 {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514, CC ECO:0000256|SAAS:SAAS00712173}. 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 ECO:0000256|SAAS:SAAS00712185}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1- CC carboxyvinyl)-3-phosphoshikimate + phosphate; CC Xref=Rhea:RHEA:21256, ChEBI:CHEBI:145989, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57701, ChEBI:CHEBI:58702; EC=2.5.1.19; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712174}; CC -!- CATALYTIC ACTIVITY: CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3- CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, CC ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; CC EC=4.2.3.4; Evidence={ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); CC Xref=Rhea:RHEA:13121, ChEBI:CHEBI:145989, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:456216; CC EC=2.7.1.71; Evidence={ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00287328}; 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; CC EC=1.1.1.25; Evidence={ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712169}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712187}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00336886}. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase CC family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712186}. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase CC family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712182}. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3- CC dehydroquinase family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712184}. 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, ECO:0000256|SAAS:SAAS00712181}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC dehydroquinate synthase family. {ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar CC phosphate cyclases superfamily. Dehydroquinate synthase family. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00858969}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}. 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 RefSeq; XP_007331715.1; XM_007331653.1. DR EnsemblFungi; EKM77624; EKM77624; AGABI1DRAFT_61742. DR GeneID; 18830378; -. DR KEGG; abp:AGABI1DRAFT61742; -. DR InParanoid; K5VT63; -. DR KO; K13830; -. DR OrthoDB; EOG092C02JU; -. DR UniPathway; UPA00053; UER00089. DR Proteomes; UP000008493; 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:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. 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; 3.65.10.10; -; 2. DR HAMAP; MF_00210; EPSP_synth; 1. DR HAMAP; MF_03143; Pentafunct_AroM; 1. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. DR InterPro; IPR018508; 3-dehydroquinate_DH_AS. 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; 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; IPR022893; Shikimate_DH_fam. DR InterPro; IPR000623; Shikimate_kinase/TSH1. DR InterPro; IPR023000; Shikimate_kinase_CS. DR Pfam; PF01761; DHQ_synthase; 1. DR Pfam; PF01487; DHquinase_I; 1. DR Pfam; PF00275; EPSP_synthase; 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; 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 {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858961}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00415286}; KW Complete proteome {ECO:0000313|Proteomes:UP000008493}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415327}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415285}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00415747}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00727050}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00415250}; KW NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS01080154}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172}; KW Reference proteome {ECO:0000313|Proteomes:UP000008493}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415343}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00712179}. FT DOMAIN 79 364 DHQ_synthase. {ECO:0000259|Pfam:PF01761}. FT DOMAIN 416 844 EPSP_synthase. {ECO:0000259|Pfam: FT PF00275}. FT DOMAIN 1312 1393 Shikimate_dh_N. {ECO:0000259|Pfam: FT PF08501}. FT NP_BIND 45 47 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 85 88 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 116 118 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 141 142 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 181 184 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT REGION 1 390 3-dehydroquinate synthase. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT REGION 196 199 Substrate binding 2. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT REGION 270 274 Substrate binding 2. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT REGION 1307 1590 Shikimate dehydrogenase. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT ACT_SITE 266 266 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 281 281 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 832 832 For EPSP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT ACT_SITE 1196 1196 Proton acceptor; for 3-dehydroquinate FT dehydratase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 1224 1224 Schiff-base intermediate with substrate; FT for 3-dehydroquinate dehydratase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 196 196 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 277 277 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 293 293 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 121 121 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 132 132 Substrate 1. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 148 148 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 154 154 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 163 163 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 164 164 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 192 192 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 256 256 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 277 277 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 293 293 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 362 362 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. 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 //