ARODE_CHLMU
ID ARODE_CHLMU Reviewed; 478 AA.
AC P56961;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
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}; OrderedLocusNames=TC_0649;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
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).
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}.
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DR EMBL; AE002160; AAF39475.1; -; Genomic_DNA.
DR PIR; G81679; G81679.
DR RefSeq; WP_010231110.1; NZ_CP027217.1.
DR AlphaFoldDB; P56961; -.
DR SMR; P56961; -.
DR STRING; 243161.TC_0649; -.
DR EnsemblBacteria; AAF39475; AAF39475; TC_0649.
DR GeneID; 1246010; -.
DR KEGG; cmu:TC_0649; -.
DR eggNOG; COG0169; Bacteria.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_019120_1_1_0; -.
DR OMA; TTSVGME; -.
DR OrthoDB; 1054867at2; -.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000000800; 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 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; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
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..478
FT /note="Shikimate biosynthesis protein AroDE"
FT /id="PRO_0000138822"
FT REGION 1..208
FT /note="3-dehydroquinate dehydratase"
FT /evidence="ECO:0000305"
FT REGION 209..478
FT /note="Shikimate 5-dehydrogenase"
FT /evidence="ECO:0000305"
FT ACT_SITE 110
FT /note="Proton donor/acceptor; for 3-dehydroquinate
FT dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT ACT_SITE 133
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT ACT_SITE 277
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 55..57
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 171
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 196
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000250|UniProtKB:P58687"
FT BINDING 226..228
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 298
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 313
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 337..341
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 360..362
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 435
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O67049"
FT BINDING 442
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:O67049"
SQ SEQUENCE 478 AA; 53211 MW; 199EEF5251205AB9 CRC64;
MLCTIIRGPS FLEARNQLLR SLKKCRCFEM RADLLTVSDA ELQKLILLAP ISVLTWKKPP
SCTPQAWVKK IQSLAKLHPT YLDLDKDFPE EEILHIRHLH PNIKIIRSLH TSEHTDITQL
YTQMLASSID YYKLAVSPAS TTDLLNICRQ KHSLPQNTTV LCLGKIGQSS RILSPILQNP
FTYTIPTGAD PVAPGQLSLN HHYFYNFTNL SPQSQICALI GDTSRSIGHL THNPFFSQLS
IPCPYVKLPL TPQELPEFFS SIRALPFLGI SVTSPLKTAI IPFLDKQDSS VKLSGSCNTL
VIRQGEIIGY DTDGEGLFSV LTQHNMDLSN QRVAILGAGG AARSIAARLS RTGCELLIFN
RTKIHAEAIA SRYQAQAFDI KDLPLHSVSL IINCLPPSSI IPQALAPLIV DINTLPKHNS
FTQYARLKGC SIIYGHEMFA QQALLQFRLW FPTHSFNHLE KNFSRRAAVL ASLFSIAA
