ID E9EGX3_METAQ Unreviewed; 1570 AA. AC E9EGX3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-SEP-2015, entry version 36. DE RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|PIRNR:PIRNR000514}; 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., RA Fang W., Wang S., Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., RA Pei Y., 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|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:SAAS00063919}. 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; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. {ECO:0000256|PIRNR:PIRNR000514, CC ECO:0000256|SAAS:SAAS00063891}. 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 3/7. 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 4/7. 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 5/7. 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 -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 6/7. 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 -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase CC family. {ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3- CC dehydroquinase family. {ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC dehydroquinate synthase family. {ECO:0000256|PIRNR:PIRNR000514}. 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; EOG7KQ28X; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000002499; 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_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; 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; 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:SAAS00063914}; KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00063912}; KW ATP-binding {ECO:0000256|SAAS:SAAS00280977}; KW Complete proteome {ECO:0000313|Proteomes:UP000002499}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00280978}; KW Kinase {ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00280971}; KW Lyase {ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00063893}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00063890}; KW Multifunctional enzyme {ECO:0000256|SAAS:SAAS00280980}; KW NADP {ECO:0000256|SAAS:SAAS00063897}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00280979}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00063913}; KW Reference proteome {ECO:0000313|Proteomes:UP000002499}; KW Transferase {ECO:0000256|PIRNR:PIRNR000514, KW ECO:0000256|SAAS:SAAS00280970}; KW Zinc {ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00063900}. 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 //