ID E9EGX3_METAQ Unreviewed; 1570 AA. AC E9EGX3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 31-JAN-2018, entry version 59. DE RecName: Full=Pentafunctional AROM polypeptide {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=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-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=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}; GN ORFNames=MAC_09121 {ECO:0000313|EMBL:EFY84835.1}; OS Metarhizium acridum (strain CQMa 102). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae; OC Metarhizium. OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499}; RN [1] {ECO:0000313|EMBL:EFY84835.1, ECO:0000313|Proteomes:UP000002499} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY84835.1, RC ECO:0000313|Proteomes:UP000002499}; RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264; RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., RA Hu X., Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., RA Wang S., Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., RA Feng M.G., Xia Y., Wang C.; RT "Genome sequencing and comparative transcriptomics of the model RT entomopathogenic fungi Metarhizium anisopliae and M. acridum."; RL PLoS Genet. 7:E1001264-E1001264(2011). 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: 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|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, 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 2/7. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514, 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|PIRNR:PIRNR000514, 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|PIRNR:PIRNR000514, 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|PIRNR:PIRNR000514, 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|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:SAAS00629599}. 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; GL698603; EFY84835.1; -; Genomic_DNA. DR RefSeq; XP_007815461.1; XM_007817270.1. DR ProteinModelPortal; E9EGX3; -. DR EnsemblFungi; EFY84835; EFY84835; MAC_09121. DR GeneID; 19253432; -. DR KEGG; maw:MAC_09121; -. DR InParanoid; E9EGX3; -. DR KO; K13830; -. DR OrthoDB; EOG092C02JU; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000002499; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi. 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_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 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|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:SAAS00629580}; KW Complete proteome {ECO:0000313|Proteomes:UP000002499}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629621}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00629772}; 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: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|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172}; KW Reference proteome {ECO:0000313|Proteomes:UP000002499}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03143, KW ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629569}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00712179}. FT DOMAIN 78 356 DHQ_synthase. {ECO:0000259|Pfam:PF01761}. FT DOMAIN 401 830 EPSP_synthase. {ECO:0000259|Pfam: FT PF00275}. FT DOMAIN 1287 1367 Shikimate_dh_N. {ECO:0000259|Pfam: FT PF08501}. FT DOMAIN 1404 1485 Shikimate_DH. {ECO:0000259|Pfam:PF01488}. FT NP_BIND 49 51 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 84 87 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 115 117 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 140 141 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT NP_BIND 868 875 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}. FT REGION 1 382 3-dehydroquinate synthase. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT REGION 195 198 Substrate binding 2. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT REGION 262 266 Substrate binding 2. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT REGION 1282 1570 Shikimate dehydrogenase. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT ACT_SITE 258 258 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 273 273 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 818 818 For EPSP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_03143}. FT ACT_SITE 1172 1172 Proton acceptor; for 3-dehydroquinate FT dehydratase activity. {ECO:0000256|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 1200 1200 Schiff-base intermediate with substrate; FT for 3-dehydroquinate dehydratase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 195 195 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 269 269 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT METAL 285 285 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 120 120 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 131 131 Substrate 1. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 147 147 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 153 153 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 162 162 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 163 163 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 191 191 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}. FT BINDING 248 248 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 269 269 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 285 285 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. FT BINDING 354 354 Substrate 2. {ECO:0000256|HAMAP-Rule: FT MF_03143}. SQ SEQUENCE 1570 AA; 170852 MW; C0ACFE1DC33729B5 CRC64; MSTVDMGSPQ KISILGEDSI IADYGLWPEF VATDLVNHVQ SSTYVLITDT NLHDIYVPPF QAWFKSQQLA DNARLLTYAI PPGEASKSRE TKAEIEDWML SQKCTRDTVI IALGGGVIGD MIGYVAATFM RGVRCVQVPT TLLAMVDSSI GGKTAIDTPM GKNLVGAFWQ PKRIYIDLAF MKTLPVREFI NGMAEVIKTA AIWNEDDFTI LEQSAADILA CVRSKGLDRL LPIKDTLTRI VVGSARVKAE VVSADEREGG LRNLLNFGHS IGHAIEAILT PQLLHGEAVA IGMVKEAELA RFLGILRPHA VSRLSKCIAS YGLPTSLKDK RVIKLTAGKK CGIDTLLEKM SVDKKNDGDR KKIVLLSRIG QTFESKASFV ADSDIRTILS ASISVTPGIP NGLKVTVTPP GSKSISNRAL ILAALGSGPC KIKNLLHSDD TEFMLSAIQQ LGGASYSWYD AGEILEVTGN GGKLSASRED LYIGNAGTAS RFLTTVLTLC SSTQESNSTV LTGNTRMKVR PIGPLVDALR QNGAQIEYLE QEKSLPIRVH STGGFQGGMI ELAATVSSQY VSSILMAAPY AKTPVTLRLI GGKPISQPYI DMTISMMSSF GISVTKSTTD MDTYHIPLGA YKNPSEYVIE SDASSATYPL AVAAITGTTC TIPNIGSASL QGDARFAIDV LRPMGCSVQQ DEHSTTVTGP VTGQLKPLPH VDMEPMTDAF LTASVLAAVA NGETQITGIA NQRVKECDRI AAMKEQLAKF GVTCTELDDG IQISGKSLSD IRTPNVGIHC YDDHRVAMSL SVLSVVAPGS TIITERECVG KTWPGWWDTL AQSFKVKLDG PDTTDGDSDI KHASPQRLHA KRSIFVIGMR GAGKTTAGRW MAKLLDWKFI DLDEELERRS GKTIPEIINS PKGWDGFRQD ELDLLQDVAE NMPECHVLSC GGGIVEMPKA RELLQNYCNS GGMVVLVHRN TDQVIEYLMR DTTRPAYTTE IRQVYERRKA WYEVCCNHIY YSPHSAPNTG YNSIPDDFKR FVTSITVGNS SVKNIAKKDE SFFVSLTVPK LNESLHAISS ASVGSDAVEI RVDLLDDWSL EAVTEQLSLL RFVSKLPVIF TVRTVSQGGR FPDAANDHRY DLYRLALRLG VEYLDAEVTS TDEILQELTE SRRNTLIVSS HHDPSGSLSW KNASWVPFYN RALQYGDVIK LVGNAKSIED NFDLANFKSR MMADHKTPII AINMGVAGQL SRILNGFLTP VSHPNLPFKA APGQLSASEI RQGRALLGQI RKREFYLFGS PISQSRSPAL HNALFGITGL PHEYHLHETS SAENLGEVLH SESFGGASVT IPLKRDVMAL VDELTPAAQA IGAVNTIIPL NDDISSNRRR LLGDNTDWKG MVYTLSEAGV ISPVQNESAA VIGSGGTTRA AIYALHFMGF DTIYVVGRDA HKVNTLASEF PRDYNVNAIT EQAQAADLAH SPSVIISTIP ADQPIDDGVK GAVFTLLSLS AVSRVKRVLL EMAYKPHHTQ IVQMAESTST WTVIPGLEVL ASQGWYQFEA WTGIQPLYRQ ARDAVVGSTL //