ARO1_EMENI
ID ARO1_EMENI Reviewed; 1583 AA.
AC P07547; C8VRD2; Q5BFH2;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Pentafunctional AROM polypeptide {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_03143};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=SK {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03143};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03143};
DE Includes:
DE RecName: Full=Shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03143};
DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_03143};
GN Name=aromA; Synonyms=aroA, aroM; ORFNames=AN0708;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R153;
RX PubMed=3515316; DOI=10.1093/nar/14.5.2201;
RA Charles I.G., Keyte J.W., Brammar W.J., Smith M., Hawkins A.R.;
RT "The isolation and nucleotide sequence of the complex AROM locus of
RT Aspergillus nidulans.";
RL Nucleic Acids Res. 14:2201-2213(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 843-1473.
RC STRAIN=R153;
RX PubMed=3906567; DOI=10.1093/nar/13.22.8119;
RA Charles I.G., Keyte J.W., Brammar W.J., Hawkins A.R.;
RT "Nucleotide sequence encoding the biosynthetic dehydroquinase function of
RT the penta-functional arom locus of Aspergillus nidulans.";
RL Nucleic Acids Res. 13:8119-8128(1985).
RN [5]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Hawkins A.R.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION OF INTRON.
RX PubMed=8611179; DOI=10.1042/bj3130941;
RA Lamb H.K., Moore J.D., Lakey J.H., Levett L.J., Wheeler K.A., Lago H.,
RA Coggins J.R., Hawkins A.R.;
RT "Comparative analysis of the QUTR transcription repressor protein and the
RT three C-terminal domains of the pentafunctional AROM enzyme.";
RL Biochem. J. 313:941-950(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-393 IN COMPLEX WITH NAD; ZINC
RP AND SUBSTRATE ANALOG, AND SUBUNIT.
RX PubMed=9685163; DOI=10.1038/28431;
RA Carpenter E.P., Hawkins A.R., Frost J.W., Brown K.A.;
RT "Structure of dehydroquinate synthase reveals an active site capable of
RT multistep catalysis.";
RL Nature 394:299-302(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-393 IN COMPLEX WITH ADP; NAD;
RP ZINC AND SUBSTRATE ANALOG.
RX PubMed=12614613; DOI=10.1016/s0022-2836(03)00086-x;
RA Nichols C.E., Ren J., Lamb H.K., Hawkins A.R., Stammers D.K.;
RT "Ligand-induced conformational changes and a mechanism for domain closure
RT in Aspergillus nidulans dehydroquinate synthase.";
RL J. Mol. Biol. 327:129-144(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-393.
RX PubMed=15103156; DOI=10.1107/s0907444904004743;
RA Nichols C.E., Hawkins A.R., Stammers D.K.;
RT "Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate
RT synthase at 1.7 A resolution from crystals grown following enzyme
RT turnover.";
RL Acta Crystallogr. D 60:971-973(2004).
CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC reactions in prechorismate polyaromatic amino acid biosynthesis.
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:0000255|HAMAP-Rule:MF_03143};
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:0000255|HAMAP-
CC Rule:MF_03143};
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:0000255|HAMAP-Rule:MF_03143};
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:0000255|HAMAP-Rule:MF_03143};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03143};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143,
CC ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
CC cyclases superfamily. Dehydroquinate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
CC family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28836.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA28836.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAA65484.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; X05204; CAA28836.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000010; EAA65484.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN001308; CBF88944.1; -; Genomic_DNA.
DR PIR; A24962; BVASA1.
DR RefSeq; XP_658312.1; XM_653220.1.
DR PDB; 1DQS; X-ray; 1.80 A; A/B=1-393.
DR PDB; 1NR5; X-ray; 2.10 A; A/B=1-393.
DR PDB; 1NRX; X-ray; 2.90 A; A/B=1-393.
DR PDB; 1NUA; X-ray; 2.85 A; A/B=1-393.
DR PDB; 1NVA; X-ray; 2.62 A; A/B=1-393.
DR PDB; 1NVB; X-ray; 2.70 A; A/B=1-393.
DR PDB; 1NVD; X-ray; 2.51 A; A/B=1-393.
DR PDB; 1NVE; X-ray; 2.58 A; A/B/C/D=1-393.
DR PDB; 1NVF; X-ray; 2.80 A; A/B/C=1-393.
DR PDB; 1SG6; X-ray; 1.70 A; A/B=1-393.
DR PDBsum; 1DQS; -.
DR PDBsum; 1NR5; -.
DR PDBsum; 1NRX; -.
DR PDBsum; 1NUA; -.
DR PDBsum; 1NVA; -.
DR PDBsum; 1NVB; -.
DR PDBsum; 1NVD; -.
DR PDBsum; 1NVE; -.
DR PDBsum; 1NVF; -.
DR PDBsum; 1SG6; -.
DR AlphaFoldDB; P07547; -.
DR SMR; P07547; -.
DR STRING; 162425.CADANIAP00001961; -.
DR EnsemblFungi; EAA65484; EAA65484; AN0708.2.
DR GeneID; 2876485; -.
DR KEGG; ani:AN0708.2; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_001201_0_2_1; -.
DR InParanoid; P07547; -.
DR OrthoDB; 39786at2759; -.
DR BRENDA; 1.1.1.25; 517.
DR BRENDA; 4.2.3.4; 517.
DR SABIO-RK; P07547; -.
DR UniPathway; UPA00053; UER00085.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR UniPathway; UPA00053; UER00088.
DR UniPathway; UPA00053; UER00089.
DR EvolutionaryTrace; P07547; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; 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; IBA:GO_Central.
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; IBA:GO_Central.
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_00109; Shikimate_kinase; 1.
DR InterPro; IPR018508; 3-dehydroquinate_DH_AS.
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; IPR000623; Shikimate_kinase/TSH1.
DR InterPro; IPR023000; Shikimate_kinase_CS.
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 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; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW ATP-binding; Cytoplasm; Kinase; Lyase; Metal-binding;
KW Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..1583
FT /note="Pentafunctional AROM polypeptide"
FT /id="PRO_0000140859"
FT REGION 1..384
FT /note="3-dehydroquinate synthase"
FT REGION 397..842
FT /note="EPSP synthase"
FT REGION 863..1055
FT /note="Shikimate kinase"
FT REGION 1056..1276
FT /note="3-dehydroquinase"
FT REGION 1289..1583
FT /note="Shikimate dehydrogenase"
FT ACT_SITE 260
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT ACT_SITE 275
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT ACT_SITE 824
FT /note="For EPSP synthase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1179
FT /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1207
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 44..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 81..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 114..116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 130
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 146
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 152
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 162
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 179..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 194..197
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 250
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 264..268
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 271
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 287
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143,
FT ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163"
FT BINDING 356
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT BINDING 870..877
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT CONFLICT 62
FT /note="A -> R (in Ref. 1; CAA28836)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="A -> R (in Ref. 1; CAA28836)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="R -> T (in Ref. 1; CAA28836)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="I -> T (in Ref. 1; CAA28836)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="Q -> H (in Ref. 1; CAA28836)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="A -> P (in Ref. 1; CAA28836)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="S -> C (in Ref. 1; CAA28836)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="A -> G (in Ref. 1; CAA28836 and 4; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="T -> S (in Ref. 1; CAA28836 and 4; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1048
FT /note="K -> G (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1093
FT /note="D -> N (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1154
FT /note="E -> D (in Ref. 1; CAA28836 and 4; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1345..1349
FT /note="SVTIP -> FRNNS (in Ref. 1; CAA28836)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 45..65
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:1SG6"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 204..222
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1NVA"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 236..255
FT /evidence="ECO:0007829|PDB:1SG6"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1NVF"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:1SG6"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 287..304
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 332..337
FT /evidence="ECO:0007829|PDB:1SG6"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:1SG6"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:1NVA"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:1SG6"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:1NVA"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:1SG6"
SQ SEQUENCE 1583 AA; 172664 MW; FBC8610B961840D8 CRC64;
MSNPTKISIL GRESIIADFG LWRNYVAKDL ISDCSSTTYV LVTDTNIGSI YTPSFEEAFR
KAAAEITPSP RLLIYNAPPG EVSKSRQTKA DIEDWMLSQN PPCGRDTVVI ALGGGVIGDL
TGFVASTYMR GVRYVQVPTT LLAMVDSSIG GKTAIDTPLG KNLIGAIWQP TKIYIDLEFL
ETLPVREFIN GMAEVIKTAA ISSEEEFTAL EENAETILKA VRREVRPGEH RFEGIEEILK
ARILASARHK AYVVSADERE GGLRNLLNWG HSIGHAIEAI LTPQILHGEC VAIGMVKEAE
LARHLGILKG VAVSRIVKCL AAYGLPTSLK DARIRKLTAG KHCSVDQLMF NMALDKKNDG
PKKKIVLLSA IGTPYETRAS VVANEDIRVV LAPSIEVHPG VAQSSNVICA PPGSKSISNR
ALVLAALGSG TCRIKNLLHS DDTEVMLNAL ERLGAATFSW EEEGEVLVVN GKGGNLQASS
SPLYLGNAGT ASRFLTTVAT LANSSTVDSS VLTGNNRMKQ RPIGDLVDAL TANGASIEYV
ERTGSLPLKI AASGGFAGGN INLAAKVSSQ YVSSLLMCAP YAKEPVTLRL VGGKPISQPY
IDMTTAMMRS FGIDVQKSTT EEHTYHIPQG RYVNPAEYVI ESDASSATYP LAVAAVTGTT
CTVPNIGSAS LQGDARFAVE VLRPMGCTVE QTETSTTVTG PSDGILRPLP NVDMEPMTDA
FLGASVLAAI ARGKESNHTT RIYGIANQRV KECNRIKAMK DELAKFGVIC REHDDGLEID
GIDRSNLRQP VGGVFCYDDH RVAFSFSVLS LVTPQPTLIL EKECVGKTWP GWWDTLRQLF
KVKLEGKELE EEPVAASGPD RANASIYIIG MRGAGKSTAG NWVSKALNRP FVDLDTELET
VEGMTIPDII KTRGWQGFRN AELEILKRTL KERSRGYVFA CGGGVVEMPE ARKLLTDYHK
TKGNVLLLMR DIKKIMDFLS IDKTRPAYVE DMMGVWLRRK PWFQECSNIQ YYSRDASPSG
LARASEDFNR FLQVATGQID SLSIIKEKEH SFFASLTLPD LREAGDILEE VCVGSDAVEL
RVDLLKDPAS NNDIPSVDYV VEQLSFLRSR VTLPIIFTIR TQSQGGRFPD NAHDAALELY
RLAFRSGCEF VDLEIAFPED MLRAVTEMKG FSKIIASHHD PKGELSWANM SWIKFYNKAL
EYGDIIKLVG VARNIDDNTA LRKFKNWAAE AHDVPLIAIN MGDQGQLSRI LNGFMTPVSH
PSLPFKAAPG QLSATEIRKG LSLMGEIKPK KFAIFGSPIS QSRSPALHNT LFAQVGLPHN
YTRLETTNAQ DVQEFIRSPD FGGASVTIPL KLDIMPLLDE VAAEAEIIGA VNTIIPVSTG
KNTPSRLVGR NTDWQGMILS LRKAGVYGPK RKDQEQSALV VGGGGTARAA IYALHNMGYS
PIYIVGRTPS KLENMVSTFP SSYNIRIVES PSSFESVPHV AIGTIPADQP IDPTMRETLC
HMFERAQEAD AEAVKAIEHA PRILLEMAYK PQVTALMRLA SDSGWKTIPG LEVLVGQGWY
QFKYWTGISP LYESARACSS PLI
