ARODE_CHLPN
ID ARODE_CHLPN Reviewed; 477 AA.
AC Q9Z6M4; Q9JQ99;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Shikimate biosynthesis protein AroDE {ECO:0000305};
DE Includes:
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000250|UniProtKB:P58687};
DE Short=3-dehydroquinase {ECO:0000250|UniProtKB:P58687};
DE EC=4.2.1.10 {ECO:0000250|UniProtKB:P58687};
DE AltName: Full=Type I DHQase {ECO:0000250|UniProtKB:P58687};
DE AltName: Full=Type I dehydroquinase {ECO:0000250|UniProtKB:P58687};
DE Short=DHQ1 {ECO:0000250|UniProtKB:P58687};
DE Includes:
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000250|UniProtKB:O67049};
DE Short=SDH {ECO:0000250|UniProtKB:O67049};
DE EC=1.1.1.25 {ECO:0000250|UniProtKB:O67049};
GN Name=aroE {ECO:0000250|UniProtKB:O67049};
GN Synonyms=aroD {ECO:0000250|UniProtKB:P58687};
GN OrderedLocusNames=CPn_1035, CP_0817, CpB1075;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of
CC the aromatic amino acids biosynthetic pathway. In the first reaction,
CC the AroD domain catalyzes the cis-dehydration of 3-dehydroquinate (DHQ)
CC and introduces the first double bond of the aromatic ring to yield 3-
CC dehydroshikimate; in the second reaction, the AroE domain catalyzes the
CC reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield
CC shikimate (SA). {ECO:0000250|UniProtKB:O67049,
CC ECO:0000250|UniProtKB:P58687}.
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:0000250|UniProtKB:P58687};
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:0000250|UniProtKB:O67049};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000250|UniProtKB:P58687}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000250|UniProtKB:O67049}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the type-I 3-
CC dehydroquinase family. {ECO:0000250|UniProtKB:P58687}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC dehydrogenase family. {ECO:0000250|UniProtKB:O67049}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP99004.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE001363; AAD19172.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38612.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99242.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP99004.1; ALT_INIT; Genomic_DNA.
DR PIR; G72003; G72003.
DR PIR; H86619; H86619.
DR RefSeq; NP_225229.1; NC_000922.1.
DR RefSeq; WP_010883668.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z6M4; -.
DR SMR; Q9Z6M4; -.
DR STRING; 115711.CP_0817; -.
DR EnsemblBacteria; AAD19172; AAD19172; CPn_1035.
DR EnsemblBacteria; AAF38612; AAF38612; CP_0817.
DR GeneID; 45051093; -.
DR KEGG; cpa:CP_0817; -.
DR KEGG; cpj:aroE; -.
DR KEGG; cpn:CPn_1035; -.
DR KEGG; cpt:CpB1075; -.
DR PATRIC; fig|115713.3.peg.1133; -.
DR eggNOG; COG0169; Bacteria.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_019120_1_1_0; -.
DR OrthoDB; 1054867at2; -.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProt.
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; ISS:UniProtKB.
DR GO; GO:0019632; P:shikimate metabolic process; ISS:UniProtKB.
DR CDD; cd00502; DHQase_I; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00214; AroD; 1.
DR HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR001381; DHquinase_I.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR011342; Shikimate_DH.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21089; PTHR21089; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR TIGRFAMs; TIGR00507; aroE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Multifunctional enzyme; NADP; Oxidoreductase; Schiff base.
FT CHAIN 1..477
FT /note="Shikimate biosynthesis protein AroDE"
FT /id="PRO_0000138823"
FT REGION 1..209
FT /note="3-dehydroquinate dehydratase"
FT /evidence="ECO:0000305"
FT REGION 210..477
FT /note="Shikimate 5-dehydrogenase"
FT /evidence="ECO:0000305"
FT ACT_SITE 111
FT /note="Proton donor/acceptor; for 3-dehydroquinate
FT dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT ACT_SITE 134
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT ACT_SITE 279
FT /note="Proton acceptor; for shikimate dehydrogenase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 21
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 29..31
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 56..58
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 172
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 197
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 228..230
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 300
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 315
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 339..343
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 362..364
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 438
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 445
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:O67049"
SQ SEQUENCE 477 AA; 52945 MW; 3B57DD86C163E935 CRC64;
MLCATVSGPS FCEAKQQILK SLHLVDIIEL RLDLINELDD QELHTLITTA QNPILTFRQH
KEMSTALWIQ KLYSLAKLEP KWMDIDVSLP KTALQTIRKS HPKIKLILSY HTDKNEDLDA
IYNEMLATPA EIYKIVLSPE NSSEALNYIK KARLLPKPST VLCMGTHGLP SRVLSPLISN
AMNYAAGISA PQVAPGQPKL EELLSYNYSK LSEKSHIYGL IGDPVDRSIS HLSHNFLLSK
LSLNATYIKF PVTIGEVVTF FSAIRDLPFS GLSVTMPLKT AIFDHVDALD ASAQLCESIN
TLVFRNQKIL GYNTDGEGVA KLLKQKNISV NNKHIAIVGA GGAAKAIAAT LAMQGANLHI
FNRTLSSAAA LATCCKGKAY PLGSLENFKT IDIIINCLPP EVTFPWRFPP IVMDINTKPH
PSPYLERAQK HGSLIIHGYE MFIEQALLQF ALWFPDFLTP ESCDSFRNYV KNFMAKV
