ID A0A1E1UVI7_9BRAD Unreviewed; 271 AA. AC A0A1E1UVI7; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 05-DEC-2018, entry version 11. 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; Rhizobiales; OC Bradyrhizobiaceae; 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 CC alpha-ketoisovalerate to form ketopantoate. {ECO:0000256|HAMAP- CC Rule:MF_00156, ECO:0000256|SAAS:SAAS00843518}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl- CC 2-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, ECO:0000256|SAAS:SAAS00771259}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00156, ECO:0000256|PIRSR:PIRSR000388-3}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00156, ECO:0000256|PIRSR:PIRSR000388-3}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS00771269}. CC -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000256|HAMAP- CC Rule:MF_00156, ECO:0000256|SAAS:SAAS00771257}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156, CC ECO:0000256|SAAS:SAAS00771239}. CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000256|HAMAP- CC Rule:MF_00156, ECO:0000256|SAAS:SAAS00771235}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd06557; KPHMT-like; 1. DR HAMAP; MF_00156; PanB; 1. DR InterPro; IPR003700; Pantoate_hydroxy_MeTrfase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. 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 Complete proteome {ECO:0000313|Proteomes:UP000095193}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156, KW ECO:0000256|SAAS:SAAS00771250}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00156, KW ECO:0000256|PIRSR:PIRSR000388-3, ECO:0000256|SAAS:SAAS00771249}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00156, KW ECO:0000256|PIRSR:PIRSR000388-3, ECO:0000256|SAAS:SAAS00771262}; KW Methyltransferase {ECO:0000313|EMBL:GAU80301.1}; KW Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00156, KW ECO:0000256|SAAS:SAAS00771245}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00156, KW ECO:0000256|SAAS:SAAS00771224, ECO:0000313|EMBL:GAU80301.1}. FT REGION 51 52 Alpha-ketoisovalerate binding. FT {ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-2}. FT ACT_SITE 188 188 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00156, ECO:0000256|PIRSR:PIRSR000388- FT 1}. FT METAL 51 51 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00156, ECO:0000256|PIRSR:PIRSR000388- FT 3}. FT METAL 90 90 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00156, ECO:0000256|PIRSR:PIRSR000388- FT 3}. FT METAL 121 121 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00156, ECO:0000256|PIRSR:PIRSR000388- FT 3}. FT BINDING 90 90 Alpha-ketoisovalerate. FT {ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-2}. FT BINDING 119 119 Alpha-ketoisovalerate. FT {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 //