ID A0A072PNT6_9EURO Unreviewed; 1599 AA.
AC A0A072PNT6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=A1O9_02572 {ECO:0000313|EMBL:KEF61008.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF61008.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF61008.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF61008.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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|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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEF61008.1}.
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DR EMBL; AMGV01000002; KEF61008.1; -; Genomic_DNA.
DR RefSeq; XP_013263598.1; XM_013408144.1.
DR STRING; 1182545.A0A072PNT6; -.
DR GeneID; 25277514; -.
DR VEuPathDB; FungiDB:A1O9_02572; -.
DR HOGENOM; CLU_001201_1_0_1; -.
DR OrthoDB; 865at2759; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000027920; 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; 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_00109; Shikimate_kinase; 1.
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; 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 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; 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; 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:UP000027920};
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 82..364
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT DOMAIN 410..841
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT DOMAIN 1305..1385
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT REGION 1..390
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT REGION 76..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..1061
FT /note="Shikimate kinase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT REGION 1300..1599
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 829
FT /note="For EPSP synthase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT ACT_SITE 1188
FT /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT ACT_SITE 1217
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT BINDING 50..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT BINDING 87..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT BINDING 120..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT BINDING 136
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 145..146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT BINDING 152
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 158
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 167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT BINDING 168
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 185..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT BINDING 200..203
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 200
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"
FT BINDING 876..883
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
SQ SEQUENCE 1599 AA; 173309 MW; 839ECE4A7A6F891C CRC64;
MPLPNGTAKE VRVSLLGKES IIINFGLWRN YVASDLLDTL ESSTYVLITD TNIGGLYTES
FRKAFEAAKS KESSPSRLLV HEIPPGESSK SRQTKDDIED WLLSQSPPCG RDTVIIALGG
GVVGDLTGFV AATYMRGVRF VQVPTTLLAM VDSAIGGKTA IDTPLGKNLV GAIWQPQRIY
IDLDFLGTLP RRELINGMAE VIKTAAISDE NEFIALESNS DKIMAAVNSD IKQGAARFKD
IEPILIRVIS ASAKFKAHVV TIDERETGLR NLLNFGHSIG HAMEAFLTPQ VLHGECVAIG
MIKEAELARY LGVLSGVAVG RLQKCLTAYG LPTRLDDEKI RKLSGGKVCT VDGMLKKMGV
DKKNDGAKKK VVLLSAIGRT YEQKASVVSD SDLRVVLSPS VDVLPGVPQD LNVVCAPPGS
KSISNRALVL AALGKGTCRV KNLLTSADTE VMLEALSKLG ATTFSWEEDG EVLVVDGKGG
QLYASQSELY LGNAGTAARF LTTVVTLTHL SHVSSTVLTG NARMKQRPIG DLVDALKTNG
AGIEYLETVG CLPLNITASG GFNGGVIELA AKVSSQYVSS LLMCAPYAKQ PVTLKLIGGK
PVSQPYIDMT IAMMAAFGIE VRKSQAEEHT YHIPQGGYVN PEEYVVESDA SSATYPLAIA
AITGTTCTIP NIGSTSLQGD SRFAIDVLRP MGCEVKQTRT STTVTGPSSG VLQPLPNIDM
EPMTDAFLTA SVLAAVAQGG KSNTTRIYGI ANQRVKECNR IQAMQDELAK FGVKCRQFDD
GIEIDGIDRR QLQQPKAGVH CYDDHRVAMS FSVLALAAPQ PSLILEKECT GKTWPGWWDT
LTQQFLVKLE GKELEATTVH TKKKLDRASA SVFIIGMRGA GKTTSGRWAS RSLGKKLIDL
DTELEKREKA TIPDIVRQHG WDYFRARELA LLKAVVKELP TGHIFACGGG VVETAEARKL
FIDWHQKTGH VLLVERNINE VMDFLQIDKT RPAYVEDMMG VWLRRKPWFE QCSNILYYSQ
SIPNEQMSEA AEDFDRFLKM VSGKIDALGK LKRKPESFFV SLTFPDLRPH LSILPEVCLG
SDAVELRVDL LKDPQSASDI PSQEYVTSQL SLLRATVPLP VVFTIRTTSQ GGKFPDAAYD
EYLGLNTLAI RMGSEFVDLE VGTFPDDMLK KIHDLKNDSH SKIIASHHDP QGRLSWSKPG
SWIPIYNKCL QFGDVVKLIG IASSLDDNFS LRRFKQWSAS QHPDLPLIAI NMGRAGQVSR
ILNRFMTPVS HPALPFKAAP GQLSATEIRQ GLSLMGEIVP KQYYLFGSPI SASKSPALHN
TFFQKTGLPH SYSLCETTSV EVMREKIRAE DFGGASITIP LKLDVMGLLD VIDASARLIG
AVNTIVPVID PKTGKKLLEG RNTDFLGMGD CLRAAGASAA LGEGPQSGLV IGGGGTARAA
IQTLYSMGYG PVYLIARNKG KLAELKATFP PFYDLHVLDA GDKSSLQAIT REPPSVAIAT
IPANEPIDPA LGAALHAMFA ASTQNKKPGG GVPTLLELAY KPVHTAVMAM AEEVGGWSTV
QGLETLVTQG LWQFEYWTDI RVRGVGQRIA RVSSFFSPL
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