ID A0A1E1UVI7_9HYPH Unreviewed; 271 AA. AC A0A1E1UVI7; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 25-MAY-2022, entry version 20. DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00156}; DE EC=2.1.2.11 {ECO:0000256|HAMAP-Rule:MF_00156}; DE AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00156}; DE Short=KPHMT {ECO:0000256|HAMAP-Rule:MF_00156}; GN Name=panB {ECO:0000256|HAMAP-Rule:MF_00156}; GN ORFNames=BIWAKO_00187 {ECO:0000313|EMBL:GAU80301.1}; OS Bosea sp. BIWAKO-01. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; Boseaceae; OC Bosea. OX NCBI_TaxID=506668 {ECO:0000313|EMBL:GAU80301.1, ECO:0000313|Proteomes:UP000095193}; RN [1] {ECO:0000313|Proteomes:UP000095193} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIWAKO-01 {ECO:0000313|Proteomes:UP000095193}; RA Okano K.; RT "Whole Genome Sequence of Mn Oxiding Bacterium Bosea sp. Strain RT BIWAKO-01."; RL Submitted (JAN-2016) 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:0000256|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:0000256|HAMAP- CC Rule:MF_00156}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00156, CC ECO:0000256|PIRSR:PIRSR000388-3}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00156, CC ECO:0000256|PIRSR:PIRSR000388-3}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)- CC pantoate from 3-methyl-2-oxobutanoate: step 1/2. {ECO:0000256|HAMAP- CC Rule:MF_00156}. CC -!- SUBUNIT: Homodecamer; pentamer of dimers. CC {ECO:0000256|ARBA:ARBA00011424, ECO:0000256|HAMAP-Rule:MF_00156}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156}. CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000256|ARBA:ARBA00008676, CC ECO:0000256|HAMAP-Rule:MF_00156}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GAU80301.1}. 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; BCQA01000001; GAU80301.1; -; Genomic_DNA. DR RefSeq; WP_069876931.1; NZ_BCQA01000001.1. DR STRING; 506668.BIWAKO_00187; -. DR EnsemblBacteria; GAU80301; GAU80301; BIWAKO_00187. DR UniPathway; UPA00028; UER00003. DR Proteomes; UP000095193; Unassembled WGS sequence. 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; 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 {ECO:0000256|HAMAP-Rule:MF_00156}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|PIRSR:PIRSR000388- KW 3}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00156, KW ECO:0000256|PIRSR:PIRSR000388-3}; KW Methyltransferase {ECO:0000313|EMBL:GAU80301.1}; KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655, KW ECO:0000256|HAMAP-Rule:MF_00156}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00156}. FT REGION 51..52 FT /note="Alpha-ketoisovalerate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-2" FT ACT_SITE 188 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-1" FT METAL 51 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-3" FT METAL 90 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-3" FT METAL 121 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-3" FT BINDING 90 FT /note="Alpha-ketoisovalerate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-2" FT BINDING 119 FT /note="Alpha-ketoisovalerate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-2" SQ SEQUENCE 271 AA; 28643 MW; BB724B20856D98CB CRC64; MAYLSDARTL TLADFARMKT AGEKVAMMTC YDSSFASLLE SCGVEILLIG DSMGNVLQGH ATTLPVTMEQ MVYHTACVAR GARRAFIMAD MPFGSYQEGP AQAMHNAARL MAAGAHMVKL EGSDYAVEAV RFLVERGVPV CGHLGLTPQS VHQLGGYRVQ GKSADAATKL KADAAALEQA GARFLVLEMV PSTLAAEIGE TSDAMLTIGI GAGVHCNGQV LVLHDAIGVY PGKRPRFSKD FMVGAGSIPE AIQAYVAAVK SQEFPGPEHS Y //