ID PANB_BACAH Reviewed; 279 AA. AC A0RBZ2; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 02-SEP-2026, entry version 96. 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=BALH_1392; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=412694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam; RX PubMed=17337577; DOI=10.1128/jb.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). 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 = 2-dehydropantoate + (6S)-5,6,7,8- CC tetrahydrofolate; 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; Evidence={ECO:0000255|HAMAP- CC 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; CP000485; ABK84735.1; -; Genomic_DNA. DR RefSeq; WP_000851103.1; NC_008600.1. DR AlphaFoldDB; A0RBZ2; -. DR SMR; A0RBZ2; -. DR GeneID; 45021534; -. DR KEGG; btl:BALH_1392; -. DR HOGENOM; CLU_036645_1_0_9; -. DR UniPathway; UPA00028; UER00003. 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:0000287; F:magnesium ion binding; IEA:TreeGrafter. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd06557; KPHMT-like; 1. DR FunFam; 3.20.20.60:FF:000003; 3-methyl-2-oxobutanoate hydroxymethyltransferase; 1. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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 NCBIfam; TIGR00222; panB; 1. DR NCBIfam; NF001452; PRK00311.1; 1. DR PANTHER; PTHR20881; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1. DR PANTHER; PTHR20881:SF0; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1. DR Pfam; PF02548; Pantoate_transf; 1. DR PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. PE 3: Inferred from homology; KW Cytoplasm; Magnesium; Metal-binding; Pantothenate biosynthesis; KW Transferase. FT CHAIN 1..279 FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase" FT /id="PRO_0000297221" FT ACT_SITE 181 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 43..44 FT /ligand="3-methyl-2-oxobutanoate" FT /ligand_id="ChEBI:CHEBI:11851" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 43 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 82 FT /ligand="3-methyl-2-oxobutanoate" FT /ligand_id="ChEBI:CHEBI:11851" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 112 FT /ligand="3-methyl-2-oxobutanoate" FT /ligand_id="ChEBI:CHEBI:11851" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 114 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" SQ SEQUENCE 279 AA; 30535 MW; BC891820D7C0D1D6 CRC64; MKTKTDFLKM KEQGEPITML TAYDYPSAKL AEEAEVDMIL VGDSLGMVVL GYDSTVPVTV EDMIHHTKAV RRGAKETFIV TDMPFMSYHV SLQDTMVNAR RIVQESGAHA LKVEGAGEVI STIHYLTNAG IPVVAHLGLT PQSVGVLGGY KVQGKDAESA KKLIEDAKKC EEAGAIALVL ECVPMQLAEL ISEQLTIPTI GIGAGQKVDG QVLVYHDLIS YGVNRVPKFV KQYTSVQEEI VRGISQYVAE VKTRQFPEEK HSFTMKEEEC LALYGGKQS //