ID ARO1_CANGA Reviewed; 1579 AA. AC Q6FIV4; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 10-OCT-2018, entry version 115. DE RecName: Full=Pentafunctional AROM polypeptide {ECO:0000255|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_03143}; DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_03143}; DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_03143}; DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_03143}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_03143}; DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_03143}; DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_03143}; DE Short=SK {ECO:0000255|HAMAP-Rule:MF_03143}; DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03143}; DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03143}; DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03143}; DE Includes: DE RecName: Full=Shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03143}; DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_03143}; GN Name=ARO1 {ECO:0000255|HAMAP-Rule:MF_03143}; GN OrderedLocusNames=CAGL0M11484g; OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / OS NRRL Y-65) (Yeast) (Torulopsis glabrata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces; OC Nakaseomyces/Candida clade. OX NCBI_TaxID=284593; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic CC reactions in prechorismate polyaromatic amino acid biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate CC = 3-dehydroquinate + phosphate. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate + CC NADPH. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit.; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar CC phosphate cyclases superfamily. Dehydroquinate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase CC family. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase CC family. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3- CC dehydroquinase family. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate CC dehydrogenase family. {ECO:0000255|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; CR380959; CAG62820.1; -; Genomic_DNA. DR RefSeq; XP_449840.1; XM_449840.1. DR ProteinModelPortal; Q6FIV4; -. DR SMR; Q6FIV4; -. DR STRING; 284593.XP_449840.1; -. DR PRIDE; Q6FIV4; -. DR EnsemblFungi; CAG62820; CAG62820; CAGL0M11484g. DR GeneID; 2891409; -. DR KEGG; cgr:CAGL0M11484g; -. DR CGD; CAL0136537; CAGL0M11484g. DR EuPathDB; FungiDB:CAGL0M11484g; -. DR eggNOG; KOG0692; Eukaryota. DR eggNOG; COG0128; LUCA. DR eggNOG; COG0169; LUCA. DR eggNOG; COG0337; LUCA. DR eggNOG; COG0703; LUCA. DR eggNOG; COG0710; LUCA. DR HOGENOM; HOG000205493; -. DR InParanoid; Q6FIV4; -. DR KO; K13830; -. DR OMA; KVSSQYV; -. DR OrthoDB; EOG092C02JU; -. DR UniPathway; UPA00053; UER00085. DR UniPathway; UPA00053; UER00086. DR UniPathway; UPA00053; UER00087. DR UniPathway; UPA00053; UER00088. DR UniPathway; UPA00053; UER00089. DR Proteomes; UP000002428; Chromosome M. 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_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; 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; 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; Reference proteome; Transferase; Zinc. FT CHAIN 1 1579 Pentafunctional AROM polypeptide. FT /FTId=PRO_0000406711. FT NP_BIND 40 42 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}. FT NP_BIND 75 78 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}. FT NP_BIND 106 108 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}. FT NP_BIND 131 132 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}. FT NP_BIND 171 174 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}. FT NP_BIND 886 893 ATP. {ECO:0000255|HAMAP-Rule:MF_03143}. FT REGION 1 383 3-dehydroquinate synthase. FT REGION 186 189 Substrate binding 2. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT REGION 263 267 Substrate binding 2. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT REGION 396 862 EPSP synthase. FT REGION 881 1071 Shikimate kinase. FT REGION 1072 1284 3-dehydroquinase. FT REGION 1297 1579 Shikimate dehydrogenase. FT ACT_SITE 259 259 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 274 274 Proton acceptor; for 3-dehydroquinate FT synthase activity. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 844 844 For EPSP synthase activity. FT {ECO:0000255|HAMAP-Rule:MF_03143}. FT ACT_SITE 1189 1189 Proton acceptor; for 3-dehydroquinate FT dehydratase activity. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT ACT_SITE 1218 1218 Schiff-base intermediate with substrate; FT for 3-dehydroquinate dehydratase FT activity. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT METAL 186 186 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT METAL 270 270 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT METAL 286 286 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT BINDING 111 111 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}. FT BINDING 122 122 Substrate 1. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT BINDING 138 138 Substrate 2. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT BINDING 144 144 Substrate 2. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT BINDING 153 153 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}. FT BINDING 154 154 Substrate 2. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT BINDING 182 182 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}. FT BINDING 249 249 Substrate 2. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT BINDING 270 270 Substrate 2. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT BINDING 286 286 Substrate 2. {ECO:0000255|HAMAP- FT Rule:MF_03143}. FT BINDING 355 355 Substrate 2. {ECO:0000255|HAMAP- FT Rule:MF_03143}. SQ SEQUENCE 1579 AA; 174232 MW; 51A302AA2AA7CCF8 CRC64; MLVKVPILGR ETIHVGYGVR SHIVETIVGL KSSTYVVIND SNVGRVPYFQ ELLSDFEAQL PAGSRLLRYV VKPGEANKTR ATKEQIEDYL LSEGCTRDTV IVAVGGGIIG DMIGYVAATF MRGVRVVQVP TSLLAMVDSS IGGKTAVDTP LGKNFIGAFW QPEFVLVDIK WLQSLPKREF INGMAEVIKT ACIWNADEFQ RLETHADEFL HVVNTPKISE KEGFQLYDTD IESIKEHIFK LVLESIKVKA EVVSSDERES SLRNLLNFGH SIGHAYEAIL TPQALHGECV SIGMVKEAEL SRYLGILSAT QVARLSKILV AYGLPVSKDE KWFRELTLNK KTPLDTLLKK MSIDKKNDGS KKKVVLLETI GKCYGKSAHV VSDEDLRFVL TDETLVYPFN NIPRDQNKTV TPPGSKSISN RALVLAALGK GTCRIKNLLH SDDTKHMLTA VQELKGANIS WEDNGETVVL EGQGGSTLVA CENDLYLGNA GTASRFLTSV AALVNSTSQK DHVILTGNAR MQQRPIGPLV DSLRNNGIKI DYVKNEGCLP LKVHTDSVFK GGRIELAATV SSQYVSSILM CAPYAENPVT LALVGGKPIS ILYVEMTIKM MEKFGIKVEK STTEEYTYII PKGHYVNPAE YVIESDASSA TYPLAFAALT GTTVTVPNIG SASLQGDARF ATDVLQPMGC SVTQTATSTT VTGPPVGHLK PLKHVDMEPM TDAFLTACVV AAVAHDNDPT SKNTTTIEGI ANQRVKECNR IEAMCTQLAK FGVRTNELPD GIQVHGLHSI NDLKVPSIGN EAVGVCTYDD HRVAMSFSLL AGMVNSEQPN SSNPTPVRIL ERHCTGKTWP GWWDVLHTEL GAQLDGAEPL ELNSMKNAKK SVVIIGMRAA GKTTISRWCA AALGYKLVDL DTLFEERYGH GMIKDFVSQH GWEKFREEEA RIFKEVIENY GDAGYVFSSG GGLVESSESR RILKSFSKSG GYVLHLHRDI EETIMFLQKD PTRPAYVEEI REVWNRRESW YKDCSNFSFF APHCNSEVEF QNLRRAFTKF IRTITGVTTV DIPTRRSAFV CLTFENLTEY TNSLKAITYG CDAVEVRVDH LSNMDEDFVS KQISILRAST DGLPIIFTVR TKKQGGKFPD EDYETLQKLL ITALKVGVDY IDLELTLPIG IQYKVLNMKR NTKIIGSHHD FASAYPWDHS EWENRYNQAL AMDVDIVKFV GMAKSFEDNL MLERFRDSHT TKPLIAINMG AHGRVSRVLN TILTPVTSEH LSEVAAPGQL TVAEINRIYT EMGGITKKDF FVVGSPIGHS RSPVLHNTGY SVLGLPHHFD KFETTSAEEV KKHLLDNKAN LGGLAVTIPL KLDIIKYMDE LTESAKVIGA VNTVIPLGNS KFKGDNTDWL GIRNSLVSNG VPESVSGLSG LVVGAGGTSR AAIFALHKLG CQKIFIVNRT TEKLEELVKF FPEEYNIVPI KEAEEAEAVN ETIGVAVNCV PADKPLDAKL ESLLERLLLK SSHTHFVSTL VEAAYKPSVT PVMKLAKDKY QWRVVPGAQM LVHQGVAQFE TWNNCRAPFK AIYDAVTEI //