ID A0A1Q3R2Y9_9BURK Unreviewed; 274 AA. AC A0A1Q3R2Y9; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 27-SEP-2017, entry version 5. 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, ECO:0000256|SAAS:SAAS00216361}; 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., RA Anantharaman K., Tringe S., Hettich R.L., Harrison S.T., RA Banfield J.F.; RT "Genome-resolved meta-omics ties microbial dynamics to process RT performance 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 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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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: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; 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:UP000186676}; 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 88 Shikimate_dh_N. {ECO:0000259|Pfam: FT PF08501}. FT DOMAIN 115 193 Shikimate_DH. {ECO:0000259|Pfam:PF01488}. FT NP_BIND 128 132 NADP. {ECO:0000256|HAMAP-Rule:MF_00222}. FT NP_BIND 152 157 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 216 216 NADP; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00222}. FT BINDING 218 218 Shikimate. {ECO:0000256|HAMAP-Rule: FT MF_00222}. FT BINDING 240 240 NADP; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00222}. FT BINDING 247 247 Shikimate. {ECO:0000256|HAMAP-Rule: FT 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 //