(data stored in SCRATCH zone)

SWISSPROT: D5E9C0_METMS

ID   D5E9C0_METMS            Unreviewed;       268 AA.
AC   D5E9C0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 61.
DE   RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222};
DE            Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
DE            EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_00222};
GN   Name=aroE {ECO:0000256|HAMAP-Rule:MF_00222};
GN   OrderedLocusNames=Mmah_0238 {ECO:0000313|EMBL:ADE35771.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35771.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35771.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of the chorismate, which leads
CC       to the biosynthesis of aromatic amino acids. Catalyzes the reversible
CC       NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate
CC       (SA). {ECO:0000256|HAMAP-Rule:MF_00222}.
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:0000256|HAMAP-Rule:MF_00222};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       4/7. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}.
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DR   EMBL; CP001994; ADE35771.1; -; Genomic_DNA.
DR   RefSeq; WP_013036714.1; NC_014002.1.
DR   EnsemblBacteria; ADE35771; ADE35771; Mmah_0238.
DR   GeneID; 8982370; -.
DR   KEGG; mmh:Mmah_0238; -.
DR   eggNOG; arCOG01033; Archaea.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237875; -.
DR   KO; K00014; -.
DR   OMA; FGNPIKH; -.
DR   OrthoDB; 98644at2157; -.
DR   BioCyc; MMAH547558:G1GHT-236-MONOMER; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041121; SDH_C.
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   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00507; aroE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9C0.
DR   SWISS-2DPAGE; D5E9C0.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00222};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000313|EMBL:ADE35771.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          7..88
FT                   /note="Shikimate_dh_N"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          114..187
FT                   /note="Shikimate_DH"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          234..264
FT                   /note="SDH_C"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   NP_BIND         124..128
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   NP_BIND         147..152
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   REGION          15..17
FT                   /note="Shikimate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         62
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         86
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         100
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         211
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         213
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         234
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         241
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ   SEQUENCE   268 AA;  28443 MW;  32BF42A8706EFF70 CRC64;
     MKKVFGVLGD PIEHSLSPAM HNAAFRELEM DCEYHAFRVR HKYLKNAILG AQAMGFGGLN
     ITVPHKEKAL EFTNPDTLAR RIGAVNTVSF NDGIRGHNTD GLGAEMALLE AGVGINASNV
     VLVGAGGAAR AIAFHFAEKG AGVTIANRTP EKAEVLAEDV GCSHAGLENL KELLQDSDIL
     INATSAGMHP HIDSTIASRD ILHPGLAVFD IVYNPLQTKL LHQAELAGAK PIGGVAMLVH
     QGAEAFRIWT GQKPPVEVMR NAVLEGLG
//

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