ID PANB_BACCN Reviewed; 279 AA. AC A7GN76; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 02-SEP-2026, entry version 104. 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=Bcer98_1262; OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=315749; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). 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; CP000764; ABS21584.1; -; Genomic_DNA. DR RefSeq; WP_012093751.1; NC_009674.1. DR AlphaFoldDB; A7GN76; -. DR SMR; A7GN76; -. DR STRING; 315749.Bcer98_1262; -. DR PaxDb; 315749-Bcer98_1262; -. DR GeneID; 33896611; -. DR KEGG; bcy:Bcer98_1262; -. DR eggNOG; COG0413; Bacteria. DR HOGENOM; CLU_036645_1_0_9; -. DR OrthoDB; 9781789at2; -. DR UniPathway; UPA00028; UER00003. DR Proteomes; UP000002300; 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: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 Reference proteome; Transferase. FT CHAIN 1..279 FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase" FT /id="PRO_1000076815" 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; 30463 MW; 8535BCB00EA0F8AD CRC64; MKTKTDFLRM KQKGEPITML TAYDYPSAKL VEEAEVDMIL VGDSLGMVVL GYDSTVPVTV EDMIHHTKAV RRGAKDTFVV TDMPFMSYHV SLAETMHHAR RIVQEGGAHA LKVEGAGEVI STIHYLTNAG IPVVAHLGLT PQSVGILGGY KVQGKDAESA KQLIADAKKC EDAGAIALVL ECVPMQLAKI ISDELTIPTI GIGAGKDVDG QVLVYHDLIS YGVNRVPKFV KQYTAVQDEI VRGISQYVAE VKTRQFPEDQ YSFTMKEEEY VALYGGKQG //