ID A0A286UDT6_9HOMO Unreviewed; 1761 AA. AC A0A286UDT6; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 12-SEP-2018, entry version 7. DE RecName: Full=Pentafunctional AROM polypeptide {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 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 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 dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143}; GN ORFNames=PNOK_0623600 {ECO:0000313|EMBL:PAV17750.1}; OS Phellinus noxius. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Hymenochaetales; Hymenochaetaceae; Phellinus. OX NCBI_TaxID=418867 {ECO:0000313|EMBL:PAV17750.1, ECO:0000313|Proteomes:UP000217199}; RN [1] {ECO:0000313|Proteomes:UP000217199} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199}; RA Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., RA Ke H.-M., Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., RA Tsai J.-N., Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., RA Liou R.-F., Kikuchi T., Tsai I.J.; RT "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its RT Hymenochaetales Members."; RL bioRxivorg 0:0-0(2017). 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|SAAS:SAAS00712173}. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712185}. CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate CC = 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00858949}. CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00629607}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|RuleBase:RU004164, CC ECO:0000256|SAAS:SAAS00712174}. CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate + CC NADPH. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00712180}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03143}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_03143}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00858971}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00712175}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00712177}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00629576}. 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|RuleBase:RU004164, ECO:0000256|SAAS:SAAS00712169}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00712187}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|SAAS:SAAS00629599}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000256|RuleBase:RU004164}. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase CC family. {ECO:0000256|HAMAP-Rule:MF_03143, CC 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|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|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|SAAS:SAAS00712181}. 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PAV17750.1}. 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; NBII01000006; PAV17750.1; -; Genomic_DNA. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000217199; Chromosome 6. 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-UniRule. 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_00109; Shikimate_kinase; 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; 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 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 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|RuleBase:RU004164, ECO:0000256|SAAS:SAAS00858961}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|RuleBase:RU004164, ECO:0000256|SAAS:SAAS00858978}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00629580}; KW Complete proteome {ECO:0000313|Proteomes:UP000217199}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00629621}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00629577}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00629772}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00727050}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00629584}; 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:SAAS00858973}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|SAAS:SAAS00712172}; KW Reference proteome {ECO:0000313|Proteomes:UP000217199}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|RuleBase:RU004164, ECO:0000256|SAAS:SAAS00629569}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712179}. FT DOMAIN 114 400 DHQ_synthase. {ECO:0000259|Pfam:PF01761}. FT DOMAIN 453 904 EPSP_synthase. {ECO:0000259|Pfam: FT PF00275}. FT DOMAIN 1421 1502 Shikimate_dh_N. {ECO:0000259|Pfam: FT PF08501}. FT NP_BIND 119 122 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 150 152 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 175 176 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 215 218 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 952 959 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}. FT REGION 1 426 3-dehydroquinate synthase. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT REGION 230 233 Substrate binding 2. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT REGION 306 310 Substrate binding 2. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT REGION 1416 1761 Shikimate dehydrogenase. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT ACT_SITE 302 302 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 317 317 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 892 892 For EPSP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT ACT_SITE 1305 1305 Proton acceptor; for 3-dehydroquinate FT dehydratase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 1333 1333 Schiff-base intermediate with substrate; FT for 3-dehydroquinate dehydratase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 230 230 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 313 313 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 329 329 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 155 155 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 166 166 Substrate 1. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 182 182 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 188 188 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 197 197 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 198 198 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 226 226 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 292 292 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 313 313 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 329 329 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 398 398 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. SQ SEQUENCE 1761 AA; 190948 MW; C885679856E34154 CRC64; MMVAASVRTH HQRHCHICVN NAGDTTMAVR ASSESENGIR KVSILGKNSI HCGFELIPYI VSTVLNTLPS STYVLITDTV VASYHLKKFQ DEFKLAIKTA KEGGKSAPRF IHKVIPPGET SKSRQGKADI EDFLLEHKCT RDTVVLALGG GVIGDLVGFV AATFMRGVRF VQIPTTLLAM VDSSVGGKTA IDTPHGKNLI GAFWQPEYIF IDASFLSTLP AREFANGMAE VIKTAAIWDE HEFLKLEERS AEIFAAISGS GNSQGEDVSD EEKVKQQREL LLSVIAGSIG VKAHIVTVDE RETGLRNLVN FGHTIGHAIE AVLTPSLLHG ECVAIGMVLE AEVARAKGVL TQVAVGRITR TLKAYNLPTS LSDARVRAIP ASAGLDVERL LDIMAIDKKN SGKEKKVVLL SRIGKTYEEK ASVVADDIIR RTLCEAAKVI PRPLSSEESC EVTMTTPGSK SISNRALLLA ALSRGTCRLT NLLHSDDTQV MMAALQDLRG ARFSWEDGGE TVVVEGGEGR LSVPDAGKEI YLGNAGTAAR FLTTVCTLVQ DGDLSAAGEN VRETVITGNA RMKQRPVGPL VSALQSNGSS IKYLESQGCL PLSITPGGLY GGHIQLAASI SSQYVSSILL CAPYAQEEVT LELVGGSVIS QPYIDMTLAM MSSFGITATR HKGADGKLLD IYTIPKGCYV SPPEYAIESD ASSATYPLAV AAITGTTCTV LNIGSASLQG DARFAIEVLR PMGCEVIQSE NKTTVRGPPL GKLKAVGEID MEVMTDAFLT ACVLAAVANE PVEEARRLPA EDGRDKLRTT RIIGIANQRV KECNRIKAMI DELAKFGVET TELPDGLEVH GRPLSELVKG ASIHCYDDHR VAMAFSVLGS VVPETMIEEK RCVEKTWPNW WDDLENKLGF KVEGVELPSA PKGSPSLSTS STVVNESDVA AADTDASVVI IGMRGSGKTC IGTLAAQSDW KFVDADHLFE SIYKTTVREF VHSRGWEAFR SSELEVLRSL LTTAEYSKKH VISLGGGIVE TPAARDLIKE YASSYGPVVE VRRETEEIVR YLGAETARPQ YASGEPIADV CKRRAPWFEE CASYLFVNYT GTNHLGPNGK IRDHLSPGAI ALEHRREVER FFGHVTGVKR NTVPLVDAKG ELRRSYFLSL TYPDVTFALD KLETLTVGAD AIELRVDLLR APEYWQDASP YKFEGKGYIP PVSYVLSQLA ALRQATTLPI VFTVRTLAQG GSFPNPEGPS ASNIENAAFE LFELAARMGA EYLDVELVWD ESRVETFLAK WRKRGCKPEV IASWHDWSGN LKWDGNEVET IYERASRIGD IVKIVGKATE LEDNTKLHAF AVTKRESVNN KPLIAINTSP LGQLSRILNV TLTPITHPDL PAAAAPGQLS FAQIQQGLHL HGVIPSKKFY LFGSPISQSP SPTLHNTGFR LLGLPWNYGL LESGVVDERI EEAIRKDDFG GASVTIPLKL DIMKALDQLS EHVKAIGAVN TVAVAYDKTN KKILYGDNTD WLGIKRCIIT QSRGLSTTLN FSTSTGMVIG AGGTARAALY ALHSLGIRTI YLINRTRAKA ELLRDDPTFK GYGIKVLDAN IFSSGKKPEW VSGPPSVIVS TVPGSATTTS LSESKTGASL YLSRELFSVA QGVVVDMAYK PAETPFLSLA GLENPTKWRI VRGVDVLLEQ GYAQFQLWTD RRCPESEVKK AVWEKYAENG SSGSTLVAWE RVGGRYSWLV AGVTAGAIAA TTLSRWVKKG L //