ID A0A6L5EEI6_9ENTR Unreviewed; 264 AA. AC A0A6L5EEI6; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 25-MAY-2022, entry version 6. DE RecName: Full=Quinate/shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01578}; DE EC=1.1.1.282 {ECO:0000256|HAMAP-Rule:MF_01578}; DE AltName: Full=NAD-dependent shikimate 5-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01578}; GN Name=ydiB {ECO:0000256|HAMAP-Rule:MF_01578, GN ECO:0000313|EMBL:MPQ53874.1}; GN ORFNames=GBB84_23575 {ECO:0000313|EMBL:MPQ53874.1}; OS Citrobacter telavivensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=2653932 {ECO:0000313|EMBL:MPQ53874.1, ECO:0000313|Proteomes:UP000475079}; RN [1] {ECO:0000313|EMBL:MPQ53874.1, ECO:0000313|Proteomes:UP000475079} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NMI7905_11 {ECO:0000313|EMBL:MPQ53874.1, RC ECO:0000313|Proteomes:UP000475079}; RA Goncalves Ribeiro T., Izdebski R., Urbanowicz P., Carmeli Y., RA Gniadkowski M., Peixe L.; RT "Characterization of a new Citrobacter species."; RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The actual biological function of YdiB remains unclear, nor CC is it known whether 3-dehydroshikimate or quinate represents the CC natural substrate. Catalyzes the reversible NAD-dependent reduction of CC both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate CC (SA) and quinate, respectively. It can use both NAD or NADP for CC catalysis, however it has higher catalytic efficiency with NAD. CC {ECO:0000256|HAMAP-Rule:MF_01578}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH; CC Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, CC ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=1.1.1.282; Evidence={ECO:0000256|HAMAP-Rule:MF_01578}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH; CC Xref=Rhea:RHEA:18425, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, CC ChEBI:CHEBI:32364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.1.1.282; Evidence={ECO:0000256|HAMAP-Rule:MF_01578}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH; CC Xref=Rhea:RHEA:17741, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=1.1.1.282; Evidence={ECO:0000256|HAMAP-Rule:MF_01578}; 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=1.1.1.282; Evidence={ECO:0000256|HAMAP-Rule:MF_01578}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 4/7. {ECO:0000256|HAMAP-Rule:MF_01578}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01578}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000256|HAMAP-Rule:MF_01578}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01578}. 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:MPQ53874.1}. 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; WHIY01000020; MPQ53874.1; -; Genomic_DNA. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000475079; Unassembled WGS sequence. DR GO; GO:0030266; F:quinate 3-dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0052733; F:quinate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0052734; F:shikimate 3-dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. 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 HAMAP; MF_01578; Shikimate_DH_YdiB; 1. DR InterPro; IPR046346; Aminiacid_DH-like_N_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR022872; Quinate/Shikimate_DH. DR InterPro; IPR041121; SDH_C. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR022893; Shikimate_DH_fam. DR PANTHER; PTHR21089; PTHR21089; 1. DR Pfam; PF18317; SDH_C; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF53223; SSF53223; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_01578}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_01578}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01578}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01578}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01578}. FT DOMAIN 1..70 FT /note="Shikimate_dh_N" FT /evidence="ECO:0000259|Pfam:PF08501" FT DOMAIN 231..259 FT /note="SDH_C" FT /evidence="ECO:0000259|Pfam:PF18317" FT NP_BIND 108..111 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01578" FT NP_BIND 208..211 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01578" FT BINDING 47 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01578" FT BINDING 83 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01578" FT BINDING 181 FT /note="NAD; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01578" FT BINDING 231 FT /note="NAD; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01578" SQ SEQUENCE 264 AA; 28589 MW; 9D5B8012A4C6CD48 CRC64; MQNKALEKAG LPFTYMAFEV DNSTFAGAIE GLKALKMRGT GVSMPNKQLA CEFVDELTPA AKLVGAINTI VNDDGYLRGY NTDGTGHIRA IKESGFDIRG KTMVLLGAGG ASTAIGAQAA IEGIKEIKLF NRNDEFFQKA LDFAKRVNEN TDCVVTVTDL ADQQAFADAL ATADILTNGT KVGMKPLDNE SIVSDVSLLR PELLVTECVY NPHMTKLLQQ AQQAGCKTID GYGMLLWQGA EQFKLWTGKD FPLEYVKQVM GFAA //