ID A0A417HX11_9FIRM Unreviewed; 461 AA. AC A0A417HX11; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 24-JUL-2024, entry version 19. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00109, ECO:0000256|HAMAP-Rule:MF_00222}; DE Includes: DE RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_00109}; DE Short=SK {ECO:0000256|HAMAP-Rule:MF_00109}; DE EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_00109}; DE Includes: DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222}; DE Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222}; DE EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_00222}; GN Name=aroK {ECO:0000256|HAMAP-Rule:MF_00109}; GN Synonyms=aroE {ECO:0000256|HAMAP-Rule:MF_00222}; GN ORFNames=DW742_02195 {ECO:0000313|EMBL:RHT79076.1}; OS Butyricicoccus sp. AM28-25. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Butyricicoccaceae; OC Butyricicoccus. OX NCBI_TaxID=2292294 {ECO:0000313|EMBL:RHT79076.1, ECO:0000313|Proteomes:UP000283242}; RN [1] {ECO:0000313|EMBL:RHT79076.1, ECO:0000313|Proteomes:UP000283242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM28-25 {ECO:0000313|EMBL:RHT79076.1, RC ECO:0000313|Proteomes:UP000283242}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl CC group of shikimic acid using ATP as a cosubstrate. {ECO:0000256|HAMAP- CC Rule:MF_00109}. 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=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); CC Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; CC EC=2.7.1.71; Evidence={ECO:0000256|ARBA:ARBA00000172, CC ECO:0000256|HAMAP-Rule:MF_00109}; 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00109}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00109}; 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 -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 5/7. {ECO:0000256|ARBA:ARBA00004842, ECO:0000256|HAMAP-Rule:MF_00109}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00109}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000256|HAMAP-Rule:MF_00222}. CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000256|HAMAP- CC Rule:MF_00109}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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:RHT79076.1}. 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; QUJL01000001; RHT79076.1; -; Genomic_DNA. DR AlphaFoldDB; A0A417HX11; -. DR OrthoDB; 9792692at2; -. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000283242; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter. DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. 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:TreeGrafter. DR CDD; cd01065; NAD_bind_Shikimate_DH; 1. DR CDD; cd00464; SK; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. DR InterPro; IPR046346; Aminoacid_DH-like_N_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR031322; Shikimate/glucono_kinase. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR022893; Shikimate_DH_fam. DR InterPro; IPR000623; Shikimate_kinase/TSH1. DR InterPro; IPR023000; Shikimate_kinase_CS. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1. DR Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR Pfam; PF01202; SKI; 1. DR PRINTS; PR01100; SHIKIMTKNASE. DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS01128; SHIKIMATE_KINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00109}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00109}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00109}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00109}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00222}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00109}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00109}. FT DOMAIN 20..101 FT /note="Shikimate dehydrogenase substrate binding N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08501" FT DOMAIN 128..177 FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA FT reductase" FT /evidence="ECO:0000259|Pfam:PF01488" FT ACT_SITE 78 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 28..30 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 74 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 99 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 114 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 138..142 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 228 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 230 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 251 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 258 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222" FT BINDING 308..313 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 312 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 330 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 354 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 376 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 414 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 433 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 449 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" SQ SEQUENCE 461 AA; 51201 MW; 2C1A4972DF61BFC5 CRC64; MLFSMDEFRA FEPKKTTYAL FGWPLGHTMS PELHAQLFEA SGQDADYIGV AVPPEDLPEA FELAKRKLGG INCTIPHKKA VIPLLDDIDT AARDLHSVNT VRFADGKATG FNTDILGFAE SLNRDGVSLQ GKKVLLLGYG GAASVMAYHC VTQGAYLTIT GRNLEKAEAL QKQLTDAVPG ARISVFSRRH IPRDIHIVLN STPVGMYPKE NAAPLHYLPH KTEYVFDAIY NPPVTSTMKL ANPRKTKTRD GLFMLVMQAA HAQTIWTGVT FEPQACEIIL RRTYGKMAVK RLHEKHGKKN LVLCGFMGSG KTTIGRKLAR LTGLEFIDAD IYLEAKEGKK ISEIFAEKGE AYFRDRETAY IKELAQKDGI VLALGGGSVL RPENVAAVKE TGLLILLDTP FYRIMKNLSY STNRPLLDKP DKQAETRRLY NARKALYHRV ADIAVRSPRL SEVLEKVVKS V //