ID K5VT63_AGABU Unreviewed; 1590 AA. AC K5VT63; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 13-SEP-2023, entry version 78. 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=AGABI1DRAFT_61742 {ECO:0000313|EMBL:EKM77624.1}; OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC OS 10392) (White button mushroom). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus. OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM77624.1, ECO:0000313|Proteomes:UP000008493}; RN [1] {ECO:0000313|Proteomes:UP000008493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392 RC {ECO:0000313|Proteomes:UP000008493}; RX PubMed=23045686; DOI=10.1073/pnas.1206847109; RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G., RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M., RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D., RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A., RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V., RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S., RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B., RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.; RT "Genome sequence of the button mushroom Agaricus bisporus reveals RT mechanisms governing adaptation to a humic-rich ecological niche."; RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012). 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; CC Evidence={ECO:0000256|ARBA:ARBA00001864, 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|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 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 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 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; JH971395; EKM77624.1; -; Genomic_DNA. DR RefSeq; XP_007331715.1; XM_007331653.1. DR STRING; 597362.K5VT63; -. DR GeneID; 18830378; -. DR KEGG; abp:AGABI1DRAFT61742; -. DR eggNOG; KOG0692; Eukaryota. DR HOGENOM; CLU_001201_1_2_1; -. DR InParanoid; K5VT63; -. DR OMA; SWANMSW; -. DR OrthoDB; 865at2759; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000008493; 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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00502; DHQase_I; 1. DR CDD; cd08195; DHQS; 1. DR CDD; cd01556; EPSP_synthase; 1. DR CDD; cd01065; NAD_bind_Shikimate_DH; 1. DR CDD; cd00464; SK; 1. DR Gene3D; 3.40.50.1970; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1. DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2. DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. 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; IPR018508; 3-dehydroquinate_DH_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR046346; Aminoacid_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 NCBIfam; TIGR01356; aroA; 1. DR NCBIfam; TIGR01357; aroB; 1. DR NCBIfam; TIGR01093; aroD; 1. DR NCBIfam; TIGR01809; Shik-DH-AROM; 1. DR PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1. DR PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1. 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; PF08501; Shikimate_dh_N; 1. DR Pfam; PF01202; SKI; 1. DR PIRSF; PIRSF000514; Pentafunct_AroM; 1. DR PRINTS; PR01100; SHIKIMTKNASE. DR SUPFAM; SSF51569; Aldolase; 1. DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1. DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {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:UP000008493}; 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 79..364 FT /note="3-dehydroquinate synthase" FT /evidence="ECO:0000259|Pfam:PF01761" FT DOMAIN 416..844 FT /note="Enolpyruvate transferase" FT /evidence="ECO:0000259|Pfam:PF00275" FT DOMAIN 1312..1393 FT /note="Shikimate dehydrogenase substrate binding N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08501" FT DOMAIN 1555..1580 FT /note="SDH C-terminal" FT /evidence="ECO:0000259|Pfam:PF18317" FT REGION 1..390 FT /note="3-dehydroquinate synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT REGION 1307..1590 FT /note="Shikimate dehydrogenase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 266 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 281 FT /note="Proton acceptor; for 3-dehydroquinate synthase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 832 FT /note="For EPSP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1196 FT /note="Proton acceptor; for 3-dehydroquinate dehydratase FT activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT ACT_SITE 1224 FT /note="Schiff-base intermediate with substrate; for 3- FT dehydroquinate dehydratase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 45..47 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 85..88 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 116..118 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 132 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 141..142 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 148 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 154 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 163 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 164 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 181..184 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 192 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 196..199 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 196 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 256 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 270..274 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 277 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 277 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 293 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 293 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143" FT BINDING 362 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" SQ SEQUENCE 1590 AA; 171224 MW; 10E9617755A2190E CRC64; MPEADIFKVP ILGKDSIHCG FHLIPYIAHT VISTLPSSTY VLITDTNIAK FHLKSFEDVF QSTLDTHNAS GAKPRFISLV IPPGETSKSR DGKAQIEDFL LLNKCTRDTV VLALGGGVIG DLVGFVSATF MRGVRFVQIP TTLLAMVDSS VGGKTAIDTP HGKNLIGAFW QPEYIFIDAA FLETLPQREF SNGMAEVVKT AAIWNENEFL SLEARSAEIF TAIQTPSENF AGRTKDTRSA AQELLLSVIV GSISVKAHIV TIDERETGLR NLVNFGHSIG HAIEAVLTPT ILHGECVSIG MILEAELSRQ MGILSQVGVG RLSRCLKAYN LPISVSDPRI ASLPAARLLT VDRLLDIMRI DKKNSGNEKK IVILSRIGAT YEQKATVVKD ALIFKTLSEA AKVIPGIPSH NPVVMSTPGS KSISNRALVL AALGKGTCRL RNLLHSDDTQ VMMAALGELK GAKFSWEDNG DTLVVEGGQG FLAVPPKGKE LYLGNAGTAA RFLTTVCTLV QASPKDNADV TIITGNARMK QRPNGPLVTA LRTNGSQIKC LETEGCLPLA IAPEGLKGGT IQLAASVSSQ YVSSILLCAP YAAQPVTLEL TGGQVISQPY IDMTIAMMKT FGVEVKRRVD SASGKLLDTY DIPKAVYVSP PNYSIESDAS SATYPLAIAA ITGTSCTIDN IGTSSLQGDA KFAKEVLEKM GCTVSQTETQ TTVQGPPIGG LKAIEEVDME IMTDAFLTAT VVAAVAHGKT RILGIANQRV KECNRIRAMI DQLAKFGVEC IELDDGLEVI GKPISELKRG ASVHCYDDHR VAMAFSVLST VVENTIIEEK RCVEKTWPNW WDDLENKIGI KVEGVDLAGL HAKASVSGTR NFDPSASVVL IGMRGVGKSF IGDLAANALG WPQLDADDYF AEVKKQALRD FVTEHGWPAF REAEVEVLGE LLKEKATGHV ISLGGGIVET PAARELIKQY ASTTGPVVHV TRPLDEILAY LGAESARPAY GEPVADVYHR RHPWYTDISN YEFLNPVGAS SVVTSPSAGV HEEVARFFKH ITGQKPNLSS NVGAGKRSYF LSLTYPDITE ALSIVEQISE GVDALELRVD LLKSSKESDA IPSTDYVASQ LAALRRVTSL PIVYTVRTSS QGGKHPDKAE KEALELLELG LKAAVEYLDV EITLPEQKVR ELASKKGRSQ IIASYHDFSG NLKWNSVAVK EKYDIAEGLG DIIKIIGTAN AIQDNFELHN FITSVNSKPN AKPIIAVNMG TQGQLSRILN ETFTPVTHPL LPIKAAPGQL SFKQIQEALT LVGQLPAKQF YLFGNPIAHS MSPTLHNTGF QVLGLPHKYS LLETQQFNEQ NKEAITAANF GGASVTIPYK LDVIPSLDEL TPAAKAIGAV NTVIPTISGG KRVLVGDNTD WIGIRKSIIA QLSTGVVGNG LVIGGGGTAR AAIYALQSLN AETVYLWNRT KSKAEDLARA FPNARVQVLD RLGAWTSAPP NVIVGTVPAS ATTLEEGAPS ATLLTADLYQ YRDGPAVVVD MAYKPAQTPL LQLASVTSNW KTVRGLDVLL EQGYEQFELW TGRRCPRKIV GEKVTEKYDA //