ID A0A0D0AM01_9AGAM Unreviewed; 1590 AA. AC A0A0D0AM01; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 12-OCT-2022, entry version 52. DE RecName: Full=Pentafunctional AROM polypeptide {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 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 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 dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143}; DE EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143}; GN ORFNames=CY34DRAFT_804457 {ECO:0000313|EMBL:KIK42886.1}; OS Suillus luteus UH-Slu-Lm8-n1. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus. OX NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485}; RN [1] {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK42886.1, RC ECO:0000313|Proteomes:UP000054485}; RG DOE Joint Genome Institute; RA Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G., RA Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., RA LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., RA Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F., RA Nordberg H.P., Cantor M.N., Hua S.X.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000054485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485}; RG DOE Joint Genome Institute; RG Mycorrhizal Genomics Consortium; RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W., RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A., RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A., RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.; RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. 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 -!- 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:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; 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; CC Evidence={ECO:0000256|ARBA:ARBA00001901, ECO:0000256|HAMAP- CC Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; 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:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; 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:0000256|ARBA:ARBA00000172, CC ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}; 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:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 2/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 3/7. {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 4/7. {ECO:0000256|ARBA:ARBA00004871, ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 5/7. {ECO:0000256|ARBA:ARBA00004842, ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 6/7. {ECO:0000256|ARBA:ARBA00004811, ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000256|ARBA:ARBA00009948}. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase CC family. {ECO:0000256|ARBA:ARBA00006477}. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase CC family. {ECO:0000256|HAMAP-Rule:MF_03143, CC ECO:0000256|PIRNR:PIRNR000514}. 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}. CC -!- SIMILARITY: In the N-terminal section; belongs to the dehydroquinate CC synthase family. {ECO:0000256|PIRNR:PIRNR000514}. CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase CC family. {ECO:0000256|ARBA:ARBA00009349}. CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate CC cyclases superfamily. Dehydroquinate synthase family. CC {ECO:0000256|HAMAP-Rule:MF_03143}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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; KN835227; KIK42886.1; -; Genomic_DNA. DR STRING; 930992.A0A0D0AM01; -. DR EnsemblFungi; KIK42886; KIK42886; CY34DRAFT_804457. DR HOGENOM; CLU_001201_1_2_1; -. DR OrthoDB; 39786at2759; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000054485; Unassembled WGS sequence. 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:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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; 3.40.50.300; -; 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_00222; Shikimate_DH_AroE; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR046346; Aminiacid_DH-like_N_sf. 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; IPR022893; Shikimate_DH_fam. 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; SSF53223; SSF53223; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_03143}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03143}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03143}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03143}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03143}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_03143}; Reference proteome {ECO:0000313|Proteomes:UP000054485}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03143}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03143}. FT DOMAIN 80..363 FT /note="DHQ_synthase" FT /evidence="ECO:0000259|Pfam:PF01761" FT DOMAIN 417..845 FT /note="EPSP_synthase" FT /evidence="ECO:0000259|Pfam:PF00275" FT DOMAIN 1307..1388 FT /note="Shikimate_dh_N" FT /evidence="ECO:0000259|Pfam:PF08501" FT DOMAIN 1424..1476 FT /note="Shikimate_DH" FT /evidence="ECO:0000259|Pfam:PF01488" FT DOMAIN 1553..1582 FT /note="SDH_C" FT /evidence="ECO:0000259|Pfam:PF18317" FT REGION 1..389 FT /note="3-dehydroquinate synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT REGION 1302..1590 FT /note="Shikimate dehydrogenase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 265 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 280 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 833 FT /note="For EPSP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1191 FT /note="Proton acceptor; for 3-dehydroquinate dehydratase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1219 FT /note="Schiff-base intermediate with substrate; for 3- FT dehydroquinate dehydratase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 46..48 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 84..87 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 115..117 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 120 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 131 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 140..141 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 147 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 153 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 162 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 163 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 180..183 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 191 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 195..198 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 195 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 255 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 269..273 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 276 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 276 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 292 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 292 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 361 FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate" FT /ligand_id="ChEBI:CHEBI:58394" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 884..891 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" SQ SEQUENCE 1590 AA; 170223 MW; EF30A9B7658682A2 CRC64; MDTVPDILKV SILGRESIHC GFHLIPYIAH TVLTTLPASV YVLVTDTNVA QFYLSAFEKA FSAEISKLSS AKPRFLSRVI FPGETTKSRE GKADIEDFLL LERCTRDTVI LALGGGVIGD LVGFVAATFM RGVRFVQIPT TLLAMVDSSV GGKTAIDTPA GKNLIGAFWQ PEYIFIDAAF LESLPEREFS NGMAEVVKTA AIWDETEFTS LESNAQLIYN AIRTPSTGNA GRHISTRSTS QSLLLSVIRG SIYVKSHIVT IDERETGLRN LVNFGHTIGH AIEAVLTPHM LHGECVSIGM IFEAEVSRAM GILKQVAVGR LVRCLRAYGL PVSLADQRVT RCPGARGLGV DRLLDIMRVD KKNSGPQKKV VILSSIGATY EQKATAVDDA LIAKVLSEAV TVKVDLSTTS GIQHVKMATP GSKSISNRAL VLAALAQGTC RLKNLLHSDD TQVMMAALQE LKGASFAWED GGETLVVTGG AGSLEVPTAG KEIYLGNAGT AARFLTTVCS LVSPSAAPDA GTATIITGNA RMKQRPIGPL VDALRANGSE ITYNESEGCL PLSIAPKGLQ GGVIRLAASV SSQYVSSILL CAPYAREAVT LELVGGAVIS QPYIDMTIAM MRTFGVLVTR DPGTDVYRIP QGTYVNPAQY AIESDASSAT YPLAIAAITG TKCTLENIGS ESLQGDARFA VDVLARMGCE VVQTANETTV TGPKRGELKA IGEVDMEPMT DAFLTACALA AVAQGGEGNT TRILGIANQR VKECNRIKAM IDQLAKFGVQ TKELDDGLEV YGCPFNTLTR GASVHCYDDH RVAMAFSVLG TVVPDTIIEE KRCVEKTWPN WWDDLENKIG LKVGGIELPR AEGSNTATSG TPSPAASASV ILIGMRGSGK SHIGKLASAA LSRQFIDADI YFETKHNIGV REFVSVNGWP AFRAAETELL KEIIQKAGTG HVISMGGGIV ETPQARDVLK DYAKTGPVVH VLRDIEEIVN YLGDETARPA YGEPITEVFK RREPWFIECA NYDFVNHITV GDSEATNSEI SRFFKHITGQ PNLSENVAAG KRSYFVALTY PDVIPALRHM SDLTTGVDAV ELRVDLLRAH NALGAIPSQA YVTAQLAALR RATSLPIIFT VRTISQGGAF PDNSERDAFE LLALALRLGV EYIDVEISAS ERLITELAAR KGFSQIIASW HDWSGKMKWN EDVVRSKYTL ASRFGDIVKI VGKADTLQDN FVLHDFVAKA NLQRGAKPII AINMGVEGQM SRILNATLSP VTHPLLPSKA APGQLSFAQI QKALNLLGQL PAKRYFLFGN PIAHSMSPTL HNTGFEVLGL PHTYELLETA SVGEELKATL AAPDFGGASV TIPFKLDVIP LLDKLSPAAE AIGAVNTIIP VIEEGNRILY GDNTDWLGIR ESIRSRAPSI GAPAAALVIG AGGTARAAIF ALQSLGAQRI YLFNRTASKA QALVDAFPDA PVKLIETLDV WPAEGPAPTV IVSTVPASAT TTDGTSPGAV LLPLALFDAT ANGVVVDMAY KPAETPLLTL AKSAAPKWAR VMGVEVLLEQ GYVQFETWTG RRCPKHVVSK SVLEKYFAAA //