ID A0A1Q3R2Y9_9BURK Unreviewed; 274 AA. AC A0A1Q3R2Y9; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 29-SEP-2021, entry version 18. DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00015230, ECO:0000256|HAMAP-Rule:MF_00222}; DE Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222}; DE EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962, ECO:0000256|HAMAP-Rule:MF_00222}; GN Name=aroE {ECO:0000256|HAMAP-Rule:MF_00222}; GN ORFNames=BGO22_20515 {ECO:0000313|EMBL:OJV51593.1}; OS Hydrogenophaga sp. 70-12. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Hydrogenophaga. OX NCBI_TaxID=1895769 {ECO:0000313|EMBL:OJV51593.1, ECO:0000313|Proteomes:UP000186676}; RN [1] {ECO:0000313|EMBL:OJV51593.1, ECO:0000313|Proteomes:UP000186676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70-12 {ECO:0000313|EMBL:OJV51593.1}; RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K., RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.; RT "Genome-resolved meta-omics ties microbial dynamics to process performance RT in biotechnology for thiocyanate degradation."; RL Submitted (SEP-2016) 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|ARBA:ARBA00001648, ECO:0000256|HAMAP- CC 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|ARBA:ARBA00004871, 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OJV51593.1}. 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; MKSS01000203; OJV51593.1; -; Genomic_DNA. DR EnsemblBacteria; OJV51593; OJV51593; BGO22_20515. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000186676; Unassembled WGS sequence. 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:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. 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 PANTHER; PTHR21089; PTHR21089; 1. 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; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00222}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_00222}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00222}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222}. FT DOMAIN 7..88 FT /note="Shikimate_dh_N" FT /evidence="ECO:0000259|Pfam:PF08501" FT DOMAIN 115..193 FT /note="Shikimate_DH" FT /evidence="ECO:0000259|Pfam:PF01488" FT DOMAIN 240..265 FT /note="SDH_C" FT /evidence="ECO:0000259|Pfam:PF18317" FT NP_BIND 128..132 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT NP_BIND 152..157 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 78 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 87 FT /note="Shikimate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 103 FT /note="Shikimate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 216 FT /note="NADP; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 218 FT /note="Shikimate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 240 FT /note="NADP; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 247 FT /note="Shikimate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" SQ SEQUENCE 274 AA; 28546 MW; 85C02F0DE4ACC8AD CRC64; MTDRYAVIGH PISHSKSPQI HAAFAQATGQ DIDYTAIEAP LDGFAATLRA FREQGGRGAN VTLPFKLQAC ELATDPSEAA RLAGAANALR FEPGDRIRAE NFDGVGLVND IQRNLGHALK GRRVLLLGAG GATRGALLPL AQQGPAALAV ANRTADKAHA LRADFAAHAT LQSGGYADLA GERFDVVINA TSAGLSGEAL PLPGGLFAPG ALAYDMVYGK GLTPFLRQAR EAGVHALADG VGMLVEQAAE AFAWWRGVRP GTREVIARLS VPLV //