ID A0A0D2FBH4_9EURO Unreviewed; 1617 AA.
AC A0A0D2FBH4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=Z517_03203 {ECO:0000313|EMBL:KIW83957.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW83957.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW83957.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW83957.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
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|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}.
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DR EMBL; KN846970; KIW83957.1; -; Genomic_DNA.
DR RefSeq; XP_013287765.1; XM_013432311.1.
DR AlphaFoldDB; A0A0D2FBH4; -.
DR STRING; 1442368.A0A0D2FBH4; -.
DR GeneID; 25302693; -.
DR VEuPathDB; FungiDB:Z517_03203; -.
DR HOGENOM; CLU_001201_1_2_1; -.
DR OrthoDB; 865at2759; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000053029; 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:UP000053029};
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 409..841
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT DOMAIN 1306..1386
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 870..1062
FT /note="Shikimate kinase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT REGION 1301..1617
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 1189
FT /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
FT ACT_SITE 1218
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 877..884
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03143"
SQ SEQUENCE 1617 AA; 175571 MW; 82B350042E98CF86 CRC64;
MPLANGTAKE VRVSLLGKES IIINFGLWRD YVAPDLLSNL ESSTYVLITD TNLGSLYTQS
FREAFENAAR QTGKSARLLI HQIPPGESSK SRQTKDDIED WLLSQSPPCG RDTVIIALGG
GVVGDLTGFV AATYMRGVRF VQVPTTLLAM VDSSIGGKTA IDTPLGKNLV GAIWQPQRIY
IDLDFLGTLP RRELINGMAE VIKTAAISDE AEFIELERHA DRIMAAVNAD ISQGAARFKD
VEATMIRIIS ASAKFKAHVV TIDERETGLR NLLNFGHSIG HAMEAFLTPQ VLHGECVAIG
MIKEAELARY LGVLSGVAVG RLQKCLTTYG LPIRLDDEKV RKLSGGKVCT VDGMLKKMGV
DKKNDGAKKK VVLLSAIGRT YEQKASVVSD SDLRVVLSPS IEVVPGVPKD LNVVCTPPGS
KSISNRALVL AALGHGTCRI KNLLTSADTE VMLEALTRLG AATFSWEEDG EVLVVNGNGG
RLEATQHELY LGNAGTAARF LTSVATLTRQ SHVASTVLTG NARMKQRPIG DLVDALRQNG
AGIEYMENAG SLPLNIAASA GFNGGEIKLA AKVSSQYVSS LLMCAPYAKN PVTLRLVGGK
PVSQPYIDMT IAMMASFGVS VQKSKTEDHT YHIPQGVYKN PDEYVVESDA SSATYPLAIA
AITGTTCTIP NIGSASLQGD SAFATDVLRP MGCEVKQTPS STTVTGPRDG RLTPLTNIDM
EPMTDAFLTA SVLAAVAQGG KSNTTRIYGI ANQRVKECNR IQAMEDELAK FGVTCRQFDD
GIEVDGIDRT RLRRPEGGVY CYDDHRVAMS FSVLALAAPQ PTLILEKECT GKTWPGWWDT
LARQFNVKLE GVELQENSEH ARGKILDRSA ASIFIIGMRG AGKTTSGRWA ARSLGKKLVD
LDTELEKREG KSIPEIIKGH GWEHFRQREL ELLKSVMKEM PNDYVFACGG GIVETQESRN
LLIEWREKKG HVLLVQRDIG EVMGFLQVDK TRPAYVEDMM GVWLRRKPWY EQCSNLLYYS
QSIPNEQMSE AAEDFDRFLQ MVTGKVDVLS QFKRKPETFF AALTFPDLRP HLKLLPEVCL
GSDAVELRVD LLKDPNSDSA IPSAEYVTAQ LSLLRAAVPL PVVFTIRTKS QGGRFPDDAH
AEYLHLCTLA IRMGSEFLDL EVASFPESIL SPIFNFKNKS STRIIASHHD PQGTLSWSKP
GSWIAVYNKC LQYGDIVKLI GIADNLDDNF ALRRFKQWSK SQHPDLPLIA INMGRTGQIS
RILNGFMTPV SHPALPFKAA PGQLSASEIR QGLTLVGEIV PKKFYLFGSP IGASKSPALH
NTLFKETGLP HVYSLCETTD LAVIKEKIRA EDFGGASVTI PLKLDVMPLL DDVDASARLI
GAVNTIVPVH NPVSGKNTLV GYNTDYLGMM DCLRAAGASA ALGEGEQSGL VVGGGGTARA
AIHTLHAMGY KPIYLIGRNQ SKMVELAKTF PPTYDLVLLD TGAAAGKTTK PTTLEQQMPT
VPVVAIATIP ADKPVDPALA STLQSIFSRS AQLATSTAPQ GQGTSAPTRT LLELAYKPAH
TAVMQMAEQV GGWKTVQGLE TLVTQGLWQF EFWTGIRVRG LGGRISRVSL SKGFRYY
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