(data stored in SCRATCH zone)

SWISSPROT: A8FP83_SHESH

ID   A8FP83_SHESH            Unreviewed;       271 AA.
AC   A8FP83;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 83.
DE   RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00228653};
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=Ssed_0043 {ECO:0000313|EMBL:ABV34656.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34656.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34656.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34656.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of the chorismate, which
CC       leads to the biosynthesis of aromatic amino acids. Catalyzes the
CC       reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to
CC       yield shikimate (SA). {ECO:0000256|HAMAP-Rule:MF_00222,
CC       ECO:0000256|SAAS:SAAS00642229}.
CC   -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC       NADPH. {ECO:0000256|HAMAP-Rule:MF_00222,
CC       ECO:0000256|SAAS:SAAS00048714}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_00222,
CC       ECO:0000256|SAAS:SAAS00179153}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222,
CC       ECO:0000256|SAAS:SAAS00179298}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00634670}.
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DR   EMBL; CP000821; ABV34656.1; -; Genomic_DNA.
DR   RefSeq; WP_012004182.1; NC_009831.1.
DR   ProteinModelPortal; A8FP83; -.
DR   STRING; 425104.Ssed_0043; -.
DR   EnsemblBacteria; ABV34656; ABV34656; Ssed_0043.
DR   KEGG; sse:Ssed_0043; -.
DR   eggNOG; ENOG4105E2X; Bacteria.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237876; -.
DR   KO; K00014; -.
DR   OMA; PLIHNAC; -.
DR   OrthoDB; POG091H02DY; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP.
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; IPR016040; NAD(P)-bd_dom.
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; 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; A8FP83.
DR   SWISS-2DPAGE; A8FP83.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00179157};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00179155};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00058194};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00808825}.
FT   DOMAIN        7     89       Shikimate_dh_N. {ECO:0000259|Pfam:
FT                                PF08501}.
FT   DOMAIN      112    192       Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
FT   NP_BIND     127    131       NADP. {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   NP_BIND     151    156       NADP. {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   REGION       15     17       Shikimate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00222}.
FT   ACT_SITE     66     66       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING      62     62       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING      78     78       NADP. {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   BINDING      87     87       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     103    103       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     214    214       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   BINDING     216    216       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     238    238       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   BINDING     245    245       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
SQ   SEQUENCE   271 AA;  29108 MW;  19B890F7D395544A CRC64;
     MTDKYAVFGN PIAHSKSPLI HGLFAKETAQ VLEYEAILAP VDEFASCLDE FWKGEGKGAN
     VTVPFKEQAF NLCDELSEEA KLAGAVNTLT VQANGVIRGD NTDGLGLVAD LKRHMGELNG
     LSVLLVGAGG AARGSILPLL QSGISKLTIV NRTQGKAERL VDIFSEYGEV CALPMEHEDK
     SYDIIINSTS SSLTGEVPNL STQVIDTSTV CYDMMYGKEP TSFNVWAKEQ GAKLTLDGLG
     MLVGQAAQSF AIWRKVKPSV EPVLAELRTL L
//

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