ID   O52420_NEIME            Unreviewed;       163 AA.
AC   O52420;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Shikimate dehydrogenase {ECO:0000313|EMBL:AAC08644.1};
DE   Flags: Fragment;
GN   Name=aroE {ECO:0000313|EMBL:AAC08644.1};
OS   Neisseria meningitidis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=487 {ECO:0000313|EMBL:AAC08644.1};
RN   [1] {ECO:0000313|EMBL:AAC08644.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Maiden M.C.J., Bygraves J.A., Feil E., Morelli G., Russell J.E., Urwin R.,
RA   Zhang Q., Zhou J., Zurth K., Caugant D.A., Feavers I.M., Achtman M.,
RA   Spratt B.G.;
RT   "Multilocus sequence typing: a portable approach to the identification of
RT   clones within populations of pathogenic microorganisms.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABQ44238.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B151 {ECO:0000313|EMBL:ABQ44238.1};
RX   PubMed=18215423; DOI=10.1016/j.jinf.2007.12.005;
RA   Yang L., Shao Z., Zhang X., Xu L., Peng J., Xu X., Liang X., Qi Y., Jin Q.;
RT   "Genotypic characterization of Neisseria meningitidis serogroup B strains
RT   circulating in China.";
RL   J. Infect. 56:211-218(2008).
RN   [3] {ECO:0000313|EMBL:ACS82660.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=125 {ECO:0000313|EMBL:ACS82660.1}, 395
RC   {ECO:0000313|EMBL:ACS82835.1}, and 398 {ECO:0000313|EMBL:ACS82839.1};
RA   de Filippis Capasso I., Bash M.C., Lemos A.P.S., Hostetler J.,
RA   Dunning-Hotopp J., Radune D., Szczypinski B., Papazisi L., Prevots D.R.;
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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; AF037794; AAC08644.1; -; Genomic_DNA.
DR   EMBL; EF564219; ABQ44238.1; -; Genomic_DNA.
DR   EMBL; GQ170762; ACS82660.1; -; Genomic_DNA.
DR   EMBL; GQ170937; ACS82835.1; -; Genomic_DNA.
DR   EMBL; GQ170941; ACS82839.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52420; -.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR   CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NADP {ECO:0000256|ARBA:ARBA00022857}.
FT   DOMAIN          14..83
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          131..157
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAC08644.1"
FT   NON_TER         163
FT                   /evidence="ECO:0000313|EMBL:AAC08644.1"
SQ   SEQUENCE   163 AA;  17253 MW;  AC8A9C0AFF519B60 CRC64;
     IGLANDITQV KNIAIEGKTI LLLGAGGAVR GVIPVLKEHR PARIVIANRT RAKAEELAQL
     FGIEAVPMAD LNGGFDIIIN GTSGGLNGQI PDIPPDIFQN CALAYDMVYG CAAKPFLDFA
     RQSGAKKTAD GLGMLVGQAA ASYALWRGFT PDIRPVIEYM KAM
//