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 22-SEP-2009, entry version 16. DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase; DE EC=2.1.2.11; DE AltName: Full=Ketopantoate hydroxymethyltransferase; DE Short=KPHMT; GN Name=panB; OrderedLocusNames=Teth514_0427; OS Thermoanaerobacter sp. (strain X514). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=399726; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., RA Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., RA 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 tranferred onto CC alpha-ketoisovalerate to form ketopantoate (By similarity). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + 3-methyl-2- CC oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. CC -!- SUBUNIT: Homodecamer; pentamer of dimers (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the panB family. 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; YP_001662073.1; -. DR GeneID; 5877019; -. DR GenomeReviews; CP000923_GR; Teth514_0427. DR KEGG; tex:Teth514_0427; -. DR OMA; B0K365; YATPEQT. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransf...; IEA:HAMAP. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00156; -; 1. DR InterPro; IPR003700; Pantoate_hydroxy_MeTrfase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase_cat. DR Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1. DR PANTHER; PTHR20881; Pantoate_transf; 1. DR Pfam; PF02548; Pantoate_transf; 1. DR PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1. DR TIGRFAMs; TIGR00222; panB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Methyltransferase; Pantothenate biosynthesis; Transferase. FT CHAIN 1 274 3-methyl-2-oxobutanoate FT hydroxymethyltransferase. FT /FTId=PRO_1000097014. FT REGION 46 47 Alpha-ketoisovalerate binding (By FT similarity). FT ACT_SITE 184 184 Proton acceptor (By similarity). FT METAL 46 46 Magnesium (By similarity). FT METAL 85 85 Magnesium (By similarity). FT METAL 117 117 Magnesium (By similarity). FT BINDING 85 85 Alpha-ketoisovalerate (By similarity). FT BINDING 115 115 Alpha-ketoisovalerate (By similarity). 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 //