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-FEB-2021, entry version 131. 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 / NRRL OS Y-65) (Yeast) (Torulopsis glabrata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC 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., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., RA Weissenbach J., 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: CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3- CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; 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:0000255|HAMAP- CC Rule:MF_03143}; 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; EC=1.1.1.25; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); CC Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; CC EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1- CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, CC ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP- CC 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 biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 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 phosphate CC cyclases superfamily. Dehydroquinate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_03143}. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase CC 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 SMR; Q6FIV4; -. DR STRING; 5478.XP_449840.1; -. DR EnsemblFungi; CAG62820; CAG62820; CAGL0M11484g. DR GeneID; 2891409; -. DR KEGG; cgr:CAGL0M11484g; -. DR CGD; CAL0136537; CAGL0M11484g. DR VEuPathDB; FungiDB:CAGL0M11484g; -. DR eggNOG; KOG0692; Eukaryota. DR HOGENOM; CLU_001201_1_2_1; -. DR InParanoid; Q6FIV4; -. DR OMA; PAYVEDM; -. 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; IPR041121; SDH_C. 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; PF18317; SDH_C; 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; ATP-binding; KW Cytoplasm; Kinase; Lyase; Metal-binding; Multifunctional enzyme; NADP; KW Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase; Zinc. FT CHAIN 1..1579 FT /note="Pentafunctional AROM polypeptide" FT /id="PRO_0000406711" FT NP_BIND 40..42 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT NP_BIND 75..78 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT NP_BIND 106..108 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT NP_BIND 131..132 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT NP_BIND 171..174 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT NP_BIND 886..893 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT REGION 1..383 FT /note="3-dehydroquinate synthase" FT REGION 186..189 FT /note="Substrate binding 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT REGION 263..267 FT /note="Substrate binding 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT REGION 396..862 FT /note="EPSP synthase" FT REGION 881..1071 FT /note="Shikimate kinase" FT REGION 1072..1284 FT /note="3-dehydroquinase" FT REGION 1297..1579 FT /note="Shikimate dehydrogenase" FT ACT_SITE 259 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT ACT_SITE 274 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT ACT_SITE 844 FT /note="For EPSP synthase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT ACT_SITE 1189 FT /note="Proton acceptor; for 3-dehydroquinate dehydratase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT ACT_SITE 1218 FT /note="Schiff-base intermediate with substrate; for 3- FT dehydroquinate dehydratase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT METAL 186 FT /note="Zinc; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT METAL 270 FT /note="Zinc; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT METAL 286 FT /note="Zinc; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 111 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 122 FT /note="Substrate 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 138 FT /note="Substrate 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 144 FT /note="Substrate 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 153 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 154 FT /note="Substrate 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 182 FT /note="NAD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 249 FT /note="Substrate 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 270 FT /note="Substrate 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 286 FT /note="Substrate 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143" FT BINDING 355 FT /note="Substrate 2" FT /evidence="ECO:0000255|HAMAP-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 //