ID   AROE_BRUME              Reviewed;         289 AA.
AC   Q8YE20;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-NOV-2008, entry version 43.
DE   RecName: Full=Shikimate dehydrogenase;
DE            EC=1.1.1.25;
GN   Name=aroE; OrderedLocusNames=BMEI2058;
OS   Brucella melitensis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094 / Biotype 1;
RX   MEDLINE=20020109; PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen
RT   Brucella melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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 4/7.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
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DR   EMBL; AE009638; AAL53239.1; -; Genomic_DNA.
DR   PIR; AD3509; AD3509.
DR   RefSeq; NP_540975.1; -.
DR   HSSP; P15770; 1NYT.
DR   GeneID; 1197769; -.
DR   GenomeReviews; AE008917_GR; BMEI2058.
DR   KEGG; bme:BMEI2058; -.
DR   NMPDR; fig|224914.1.peg.2057; -.
DR   HOGENOM; Q8YE20; -.
DR   BioCyc; BMEL224914:BMEI2058-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0050661; F:NADP 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_00222; -; 1.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR011342; Quinate/shikimate_5-DHase.
DR   InterPro; IPR013708; Shikimate_DHase-bd_N.
DR   InterPro; IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   TIGRFAMs; TIGR00507; aroE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; NADP; Oxidoreductase.
FT   CHAIN         1    289       Shikimate dehydrogenase.
FT                                /FTId=PRO_0000135993.
FT   NP_BIND     134    138       NADP (By similarity).
FT   ACT_SITE     73     73       Proton acceptor (Potential).
SQ   SEQUENCE   289 AA;  30490 MW;  AC07A13B436754D7 CRC64;
     MDDKSMARGR KAFVTGFPIR HSRSPLIHGF WLKELGIDGS YEAVEVKPED FSSFAASLAA
     NGFAGGNVTI PHKEAAYAAA ESLDEAARAI GAVNTLWLEN GRLCGGNTDA YGFAANLDAS
     APGWDKADRA LVLGAGGASR AVVHALLSRG VCHVSVVNRT LSRAEELAAH FGARVYAHGW
     DEAQALVSNA GLIVNTTALG MSGHGEGQDF PIDLTCAPKE AVATDIVYVP LRTAFLNKAE
     KAGLKTVDGL GMLLHQAVPG FERWFGQRPQ VTQALREHIL ADMAKAGAL
//