ID PANB_BRUSU Reviewed; 275 AA. AC P65655; G0K686; Q8YFD0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 107. 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=BR0330, BS1330_I0331; OS Brucella suis biovar 1 (strain 1330). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella; OC Brucella melitensis group. OX NCBI_TaxID=204722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between animal RT and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=22038969; DOI=10.1128/jb.06181-11; RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.; RT "Revised genome sequence of Brucella suis 1330."; RL J. Bacteriol. 193:6410-6410(2011). 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; AE014291; AAN29279.1; -; Genomic_DNA. DR EMBL; CP002997; AEM17692.1; -; Genomic_DNA. DR RefSeq; WP_002963495.1; NC_004310.3. DR AlphaFoldDB; P65655; -. DR SMR; P65655; -. DR GeneID; 93017205; -. DR GeneID; 99644440; -. DR KEGG; bms:BR0330; -. DR KEGG; bsi:BS1330_I0331; -. DR PATRIC; fig|204722.21.peg.2490; -. DR HOGENOM; CLU_036645_1_0_5; -. DR PhylomeDB; P65655; -. DR UniPathway; UPA00028; UER00003. DR Proteomes; UP000007104; Chromosome I. 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..275 FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase" FT /id="PRO_0000184827" FT ACT_SITE 187 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 49..50 FT /ligand="3-methyl-2-oxobutanoate" FT /ligand_id="ChEBI:CHEBI:11851" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 49 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 88 FT /ligand="3-methyl-2-oxobutanoate" FT /ligand_id="ChEBI:CHEBI:11851" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 88 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 118 FT /ligand="3-methyl-2-oxobutanoate" FT /ligand_id="ChEBI:CHEBI:11851" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" FT BINDING 120 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156" SQ SEQUENCE 275 AA; 29418 MW; F73117B84258FE26 CRC64; MSAPVTRKRL TPKVIQAMKG ECPIVSLTAY TTPVARLLDP HCDLLLVGDS LGMVLYGMES TLAVTLDMMI MHGQAVMRGT SHACVIVDMP FGSYQESKEQ AFRNAARVMQ ETGCDGVKLE GGEEMAETVA FLVRRGIPVF GHVGLMPQQV NTVGGFRSLG RGDDEAGKIR RDAQAIAQAG AFAVVIEGTV EPLAREITAL IDIPTVGIGA SSACDGQVLV SDDMLGLFQD FTPRFVKRFA HLAPQVSQAA EAYAEEVRAR RFPGPEHVFG AKPGA //