GenomeNet

Database: UniProt
Entry: A0A067T7Q3_GALM3
LinkDB: A0A067T7Q3_GALM3
Original site: A0A067T7Q3_GALM3 
ID   A0A067T7Q3_GALM3        Unreviewed;      1612 AA.
AC   A0A067T7Q3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 63.
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=GALMADRAFT_62938 {ECO:0000313|EMBL:KDR79171.1};
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX   NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR79171.1, ECO:0000313|Proteomes:UP000027222};
RN   [1] {ECO:0000313|Proteomes:UP000027222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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 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}.
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DR   EMBL; KL142373; KDR79171.1; -; Genomic_DNA.
DR   STRING; 685588.A0A067T7Q3; -.
DR   HOGENOM; CLU_001201_1_2_1; -.
DR   OrthoDB; 865at2759; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000027222; 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; 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   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
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; PF01488; Shikimate_DH; 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:UP000027222};
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          77..362
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
FT   DOMAIN          414..842
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   DOMAIN          1316..1397
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          1425..1483
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          1575..1604
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   REGION          1..388
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   REGION          1311..1612
FT                   /note="Shikimate dehydrogenase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        264
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        279
FT                   /note="Proton acceptor; for 3-dehydroquinate synthase
FT                   activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        830
FT                   /note="For EPSP synthase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1200
FT                   /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT                   activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   ACT_SITE        1228
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         83..86
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         114..116
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         130
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         139..140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         146
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         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         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         162
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         179..182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         194..197
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         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         254
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         268..272
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         275
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         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         291
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         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT   BINDING         360
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         880..887
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
SQ   SEQUENCE   1612 AA;  173340 MW;  CA94BA12242AB605 CRC64;
     MVPTTDVYRV SILGKESIHC GFHLIPYIAR TVLTTLPSST YILITDTNVA KFHLKTFEHE
     FAYIAESLGS KSRFLSLVIP PGETSKSRDG KAHIEDFLLA NKCTRDSVIL ALGGGVIGDL
     VGFVAATFMR GVRFVQVPTT LLAMVDSSVG GKTAIDTPHG KNLIGAFWQP EYIFIDAAFL
     ETLPPREFSN GMAEVVKTAA IWNEDEFISL ESRSAEIFAA IQTPSTNFAG RSNSTRSPAQ
     ELLLSVIVGS ISVKAHIVTI DERETGLRNL VNFGHTIGHA IEAVLTPTIL HGECVSIGMI
     LEAEVSRQMG VLSQVGVGRV NRCLKAYNLP VTLSDARIAS LPAAKLLTVD RLLDIMRIDK
     KNSGPEKKIV ILSRIGATYE PKATVVPDST IAKTLSEAVK VVPAIPKHHP VKMATPGSKS
     ISNRVLVLAA LGKGTCRLKN LLHSDDTQVM MAALHELKGA KFSWEDGGET LVVEGGEGSL
     VVPPKGKELY LGNAGTAARF LTTVCTLVQT TPGATTETTV ITGNARMKQR PIGPLVTALQ
     ANGSKIAFLE SQGCLPLAIA PQGLNGGLIQ LAASVSSQYV SSILLCAPYA SAPVTLELTG
     GQVISQPYID MTVAMMATFG VKVVRRTDKA TGKLLDIYDI PTSTYINPAE YNIESDASSA
     TYPLAIAAIT GTSCTIQNIG SASLQGDAKF AKEVLERMGC DVVQTATETT VRGPAMGGLK
     AIEEVDMEEM TDAFLTASVL AAVAGGRTRI LGIANQRVKE CNRIRAMIDE LAKFGVETVE
     LDDGLEIVGK PIDQLKTGVS VHCYDDHRVA MAFSVLSTIV GDTVIEEKRC VEKTWPNWWD
     DLENKIGINV EGVQLDNSTS AASASGTHSH EPSASVILIG MRGTGKTTIG NLAASALSWP
     CVDADAYFEE TQKIGVREFV HRHGWAAFRD AEFATLQKLV KEKATSHIIS LGGGIVETPA
     ARDLLKAYAA KGPVVHVVRP LEDVIAYLSA ETARPAYDES VSDVFRRREP WFEECCNYIF
     DNTFVPADGG SEYEAAKKDT FNEVSRFFQH ITGQQPNLAA NLNPNGRSYF LSLTYPDIKQ
     AYPHIEELTE GVDALELRVD LLKSPKNYET FGESIPPLDY VQAQVSALRR VSSLPIVFTV
     RTKSQGGAFP DAAHKEAFEL LHLALKMGVE YIDAEITLPE KQLKDLNAKK GFSKVIASWH
     DWSGGLKWDG TPVQEKYDAA CQLGDIVKIV GKATSLRDNF ALYDFVDAAN KKPSAKPIIA
     INMGVEGQMS RVLNATFSPV SHPLQPTKAA PGQLSFRQIQ QALHLIGLLP ARTFYLFGTP
     ISQSMSPTLH NKAFEVLGLP HRYELLETRE VGEEIKLAIT APDFGGASVT IPFKLDVIPL
     LDRLTPAAEA IGAVNTIVPQ VVDGSGRVLV GDNTDWIGIK SAIQRKIGSS PIRAALVIGA
     GGTARAAIYA LQALGADVIY LYNRTARKAE ELADAFPEAR VKVLHQIGQW GDGASGLVPP
     SVIVSTVPAS ATAVAAEDGG RQDGSAAAAM VLPNELFAYR AGPAVVVDMA YRPAETPLLR
     LAKGVVGGQW AAVPGLEVLL EQGYEQFKLW TGRRCPRGVV AKEVWEKYES SA
//
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