ID PANB_THEPX Reviewed; 274 AA. AC B0K365; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 1. DT 07-OCT-2020, entry version 76. DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156}; DE EC=2.1.2.11 {ECO:0000255|HAMAP-Rule:MF_00156}; DE AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156}; DE Short=KPHMT {ECO:0000255|HAMAP-Rule:MF_00156}; GN Name=panB {ECO:0000255|HAMAP-Rule:MF_00156}; GN OrderedLocusNames=Teth514_0427; OS Thermoanaerobacter sp. (strain X514). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter; OC unclassified Thermoanaerobacter. OX NCBI_TaxID=399726; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X514; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.; RT "Complete sequence of Thermoanaerobacter sp. X514."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl CC group from 5,10-methylenetetrahydrofolate is transferred onto alpha- CC ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP- CC Rule:MF_00156}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2- CC oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2- CC dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561, CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, CC ChEBI:CHEBI:57453; EC=2.1.2.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00156}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00156}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00156}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)- CC pantoate from 3-methyl-2-oxobutanoate: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_00156}. CC -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00156}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00156}. CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000255|HAMAP- CC Rule:MF_00156}. 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; CP000923; ABY91737.1; -; Genomic_DNA. DR RefSeq; WP_009051762.1; NC_010320.1. DR SMR; B0K365; -. DR EnsemblBacteria; ABY91737; ABY91737; Teth514_0427. DR KEGG; tex:Teth514_0427; -. DR HOGENOM; CLU_036645_1_0_9; -. DR KO; K00606; -. DR OMA; GHIGLMP; -. DR UniPathway; UPA00028; UER00003. DR Proteomes; UP000002155; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd06557; KPHMT-like; 1. DR Gene3D; 3.20.20.60; -; 1. DR HAMAP; MF_00156; PanB; 1. DR InterPro; IPR003700; Pantoate_hydroxy_MeTrfase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf. DR PANTHER; PTHR20881; PTHR20881; 1. DR Pfam; PF02548; Pantoate_transf; 1. DR PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR TIGRFAMs; TIGR00222; panB; 1. PE 3: Inferred from homology; KW Cytoplasm; Magnesium; Metal-binding; Pantothenate biosynthesis; KW Transferase. FT CHAIN 1..274 FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase" FT /id="PRO_1000097014" FT REGION 46..47 FT /note="Alpha-ketoisovalerate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT ACT_SITE 184 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT METAL 46 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT METAL 85 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT METAL 117 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 85 FT /note="Alpha-ketoisovalerate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 115 FT /note="Alpha-ketoisovalerate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" SQ SEQUENCE 274 AA; 29988 MW; 758752D0F4E653B8 CRC64; MEEKVSTLTL RKFKKEGRKI TALTAYDFPT AKILDNCGID MILVGDSLGM VVLGYESTIP VTMEDMIHHT KAVSRAVNRA FIVADMPFMS YHISKEQAMT NAARLIAEGG AHAVKLEGGE EIASIVKAIV DAGIPVVGHL GLTPQSVHQL GGYKVQGKEK EQAKKIFNDA KVLEQAGICA LVLESIPMEL AKNITENISV PTIGIGAGPY CDGQILVTHD MLGITQGHRP KFVKQYADIE KIMIDGINAY IKEVQQVLFP DEEHSFTLEK RENK //