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).
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; 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
//