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Database: UniProt
Entry: H6N0Q2_GORPV
LinkDB: H6N0Q2_GORPV
Original site: H6N0Q2_GORPV 
ID   H6N0Q2_GORPV            Unreviewed;       295 AA.
AC   H6N0Q2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Shikimate dehydrogenase AroE {ECO:0000313|EMBL:AFA73264.1};
DE            EC=1.1.1.25 {ECO:0000313|EMBL:AFA73264.1};
GN   Name=aroE1 {ECO:0000313|EMBL:AFA73264.1};
GN   OrderedLocusNames=GPOL_c22320 {ECO:0000313|EMBL:AFA73264.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA73264.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA73264.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
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DR   EMBL; CP003119; AFA73264.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6N0Q2; -.
DR   STRING; 1112204.GPOL_c22320; -.
DR   KEGG; gpo:GPOL_c22320; -.
DR   eggNOG; COG0169; Bacteria.
DR   HOGENOM; CLU_044063_0_0_11; -.
DR   Proteomes; UP000009154; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR010110; Shikimate_DH_AroM-type.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   NCBIfam; TIGR01809; Shik-DH-AROM; 1.
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; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:AFA73264.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT   DOMAIN          21..103
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          259..286
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
SQ   SEQUENCE   295 AA;  30033 MW;  823433DA3C6B9A92 CRC64;
     MLARPPLCAP VGGRTARRAT VLGSPVSHSR SPDLHLAAYR ALGLEDWTYT RRECTAADLP
     GVVAAAPAEQ IGFSVTMPNK LAALAVADER TERAVLVGSA NTLVRTVTGW RADCTDIDGM
     TGALEHLGVA ANVVGGDLPD SAVLVGAGGT ALPSVAALAA VGIGELTVVA RSAQRAADVL
     TLARDLGMSV QVADFVSTDD LSRRCRDAAV TVSTVPASAT TPVIDAVSGS ARLVDVIYDP
     WPTPLATAVR AAGGRVAGGL VMLLNQAFSQ VEQFTGLPAP RTVMAEVFAG ADAAS
//
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