(data stored in ACNUC7421 zone)

SWISSPROT: D1CDM4_THET1

ID   D1CDM4_THET1            Unreviewed;       289 AA.
AC   D1CDM4;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00321572};
DE            Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
DE            EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00321538};
GN   Name=aroE {ECO:0000256|HAMAP-Rule:MF_00222};
GN   OrderedLocusNames=Tter_0108 {ECO:0000313|EMBL:ACZ41030.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41030.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41030.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:SAAS00554845}.
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;
CC         EC=1.1.1.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00222,
CC         ECO:0000256|SAAS:SAAS01121538};
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:SAAS00315122}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222,
CC       ECO:0000256|SAAS:SAAS01143539}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00541574}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}.
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DR   EMBL; CP001825; ACZ41030.1; -; Genomic_DNA.
DR   STRING; 525904.Tter_0108; -.
DR   EnsemblBacteria; ACZ41030; ACZ41030; Tter_0108.
DR   KEGG; ttr:Tter_0108; -.
DR   eggNOG; ENOG4105E2X; Bacteria.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237875; -.
DR   KO; K00014; -.
DR   OMA; FGNPIKH; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000000323; Chromosome 1.
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; D1CDM4.
DR   SWISS-2DPAGE; D1CDM4.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00315106};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00315132};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00320209};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00320235, ECO:0000313|EMBL:ACZ41030.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   DOMAIN        6     88       Shikimate_dh_N. {ECO:0000259|Pfam:
FT                                PF08501}.
FT   DOMAIN      115    226       Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
FT   DOMAIN      249    278       SDH_C. {ECO:0000259|Pfam:PF18317}.
FT   REGION       14     16       Shikimate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00222}.
FT   ACT_SITE     65     65       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING      61     61       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING      86     86       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     101    101       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     226    226       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   BINDING     228    228       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     249    249       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   BINDING     256    256       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
SQ   SEQUENCE   289 AA;  31780 MW;  F21DC5FF0DD94AF5 CRC64;
     MKQVGVIGYP IKHSISPVFQ QAAFDALGIE AIYKAYEVPP EDLRSFFFNL RNGNWLGVNV
     TIPHKSAAAK LADERSQEVS FTGAANTIIS MNGRLKAHNT DISGFILALE ENGFQIKSKR
     AVVLGSGGTT RAVVYALAIC EAQSIAVIGR SQDKVHSLIS ELKPFFEHKQ VTVTGHSWEK
     DSIRRQIQNS DILINTTPIG MKGTDQEHLS PVSKEDLSSD LIVFDVVYNP IMTPLLTYAK
     DVGASTISGI EMLIYQGAES FRLWTGQEPP VDIMRKAAIK AMEEKSRDV
//

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