ID A0A417HX11_9CLOT Unreviewed; 461 AA. AC A0A417HX11; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 18-SEP-2019, entry version 4. 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; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; 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 RT 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. CC {ECO:0000256|HAMAP-Rule:MF_00109}. 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 -!- 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|HAMAP-Rule:MF_00109, CC ECO:0000256|SAAS:SAAS01117062}; 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=1.1.1.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00222}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00109}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00109}; 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:SAAS00315122}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_00109, CC ECO:0000256|SAAS:SAAS01080056}. 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 ECO:0000256|SAAS:SAAS00719959}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00541574}. CC -!- SIMILARITY: Belongs to the shikimate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_00109}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}. 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: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 UniPathway; UPA00053; UER00087. DR Proteomes; UP000283242; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. 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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00464; SK; 1. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. 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 Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR Pfam; PF01202; SKI; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS01128; SHIKIMATE_KINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109, KW ECO:0000256|SAAS:SAAS00315106}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109, KW ECO:0000256|SAAS:SAAS00315132}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00109, KW ECO:0000256|SAAS:SAAS00728164}; KW Complete proteome {ECO:0000313|Proteomes:UP000283242}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109, KW ECO:0000256|SAAS:SAAS00719811}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00109, KW ECO:0000256|SAAS:SAAS00728137}; 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|HAMAP-Rule:MF_00109, KW ECO:0000256|SAAS:SAAS00728079}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222, KW ECO:0000256|SAAS:SAAS00315136}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00109, KW ECO:0000256|SAAS:SAAS00728085}. FT DOMAIN 20 101 Shikimate_dh_N. {ECO:0000259|Pfam: FT PF08501}. FT DOMAIN 128 177 Shikimate_DH. {ECO:0000259|Pfam:PF01488}. FT NP_BIND 138 142 NADP. {ECO:0000256|HAMAP-Rule:MF_00222}. FT NP_BIND 308 313 ATP. {ECO:0000256|HAMAP-Rule:MF_00109}. FT REGION 28 30 Shikimate binding. {ECO:0000256|HAMAP- FT Rule:MF_00222}. FT ACT_SITE 78 78 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00222}. FT METAL 312 312 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00109}. FT BINDING 74 74 Shikimate. {ECO:0000256|HAMAP-Rule: FT MF_00222}. FT BINDING 99 99 Shikimate. {ECO:0000256|HAMAP-Rule: FT MF_00222}. FT BINDING 114 114 Shikimate. {ECO:0000256|HAMAP-Rule: FT MF_00222}. FT BINDING 228 228 NADP; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00222}. FT BINDING 230 230 Shikimate. {ECO:0000256|HAMAP-Rule: FT MF_00222}. FT BINDING 251 251 NADP; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00222}. FT BINDING 258 258 Shikimate. {ECO:0000256|HAMAP-Rule: FT MF_00222}. FT BINDING 330 330 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00109}. FT BINDING 354 354 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00109}. FT BINDING 376 376 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00109}. FT BINDING 414 414 ATP. {ECO:0000256|HAMAP-Rule:MF_00109}. FT BINDING 433 433 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00109}. FT BINDING 449 449 ATP. {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 //