ID   ARODE_CHLTR             Reviewed;         478 AA.
AC   O84375;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Shikimate biosynthesis protein aroDE;
DE   Includes:
DE     RecName: Full=3-dehydroquinate dehydratase;
DE              Short=3-dehydroquinase;
DE              EC=4.2.1.10;
DE     AltName: Full=Type I DHQase;
DE   Includes:
DE     RecName: Full=Shikimate dehydrogenase;
DE              EC=1.1.1.25;
GN   Name=aroE; Synonyms=aroD/E; OrderedLocusNames=CT_370;
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   MEDLINE=99000809; PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V.,
RA   Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans:
RT   Chlamydia trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps
CC       of the aromatic amino acids biosynthetic pathway. The first
CC       reaction is catalyzed by the 3-dehydroquinate dehydratase, coded
CC       by the aroD domain; the second reaction is catalyzed by the
CC       shikimate 5-dehydrogenase, coded by the aroE domain.
CC   -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC   -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC       NADPH.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and PEP:
CC       step 3/7.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and PEP:
CC       step 4/7.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the type-I 3-
CC       dehydroquinase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC       dehydrogenase family.
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DR   EMBL; AE001273; AAC67966.1; -; Genomic_DNA.
DR   PIR; C71523; C71523.
DR   RefSeq; NP_219879.1; -.
DR   GeneID; 884748; -.
DR   GenomeReviews; AE001273_GR; CT_370.
DR   KEGG; ctr:CT370; -.
DR   HOGENOM; O84375; -.
DR   OMA; O84375; ISHLSHN.
DR   BioCyc; CTRA315277:CT370-MON; -.
DR   BRENDA; 1.1.1.25; 108.
DR   BRENDA; 4.2.1.10; 108.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 5-dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic pro...; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00214; fused; 1.
DR   HAMAP; MF_00222; fused; 1.
DR   InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR011342; Quinate/shikimate_5-DH.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   ProDom; PD005337; DHquinase_I; 1.
DR   TIGRFAMs; TIGR00507; aroE; 1.
DR   PROSITE; PS01028; DEHYDROQUINASE_I; FALSE_NEG.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Multifunctional enzyme; NADP;
KW   Oxidoreductase; Schiff base.
FT   CHAIN         1    478       Shikimate biosynthesis protein aroDE.
FT                                /FTId=PRO_0000138824.
FT   NP_BIND     337    341       NADP (By similarity).
FT   REGION        1    208       3-dehydroquinate dehydratase.
FT   REGION      209    478       Shikimate 5-dehydrogenase.
FT   COMPBIAS    137    140       Poly-Ser.
FT   ACT_SITE    110    110       Proton acceptor (By similarity).
FT   ACT_SITE    133    133       Schiff-base intermediate with substrate
FT                                (By similarity).
SQ   SEQUENCE   478 AA;  53098 MW;  200DB65E1B081D53 CRC64;
     MLCTTISGPS FLEAKKQILR SLKECHCFEM RVDLLSVSCL ELKKLMELAP ISILAWKKPE
     SCSQADWIDK MQSLAELNPN YLDLEKDFPE EDMIRIRQLH PQIKIIRSLH TSEHTDIIQL
     YAHMRSSAAD YYKFAVSSSS TTDLLDICHQ KRSLPENTTV VCLGGMGRPS RILSPILQNP
     FTYARSTGSS PVAPGQFSLK HHYFYNFASL SAQSPICALI GDTSRSIGHL THNPFFSQLG
     VACPYIKLPL TPQELPKFFS TIRTQPFLGV SVTSPLKTAV LPFLDKQAPS VKASGSCNTL
     VIRQGEIEGH DTDGEGLFSV LMQHQIPLNN QRVAIIGAGG AAQSIATRLS RANCELLIFN
     RTKAHAEDLA SRCQAKAFSL EELPLHRVSL IINCLPPSCT IPKAVAPCVV DINTIPKHST
     FTQYARSQGS SIIYGHEMFT QQALLQFRLW FPTLSFKHLE KTFIRRAAVL ASLFSIAP
//