ID A0A2S5TBP8_9GAMM Unreviewed; 251 AA.
AC A0A2S5TBP8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000256|ARBA:ARBA00012618};
DE EC=2.1.2.11 {ECO:0000256|ARBA:ARBA00012618};
GN Name=panB {ECO:0000313|EMBL:PPE72423.1};
GN ORFNames=C3942_17915 {ECO:0000313|EMBL:PPE72423.1};
OS Solimonas fluminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Solimonas.
OX NCBI_TaxID=2086571 {ECO:0000313|EMBL:PPE72423.1, ECO:0000313|Proteomes:UP000238220};
RN [1] {ECO:0000313|EMBL:PPE72423.1, ECO:0000313|Proteomes:UP000238220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-BB {ECO:0000313|EMBL:PPE72423.1,
RC ECO:0000313|Proteomes:UP000238220};
RA Lee Y., Jeon C.O.;
RT "Genome sequencing of Solimonas sp. HR-BB.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000388-3};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000388-3};
CC -!- SUBUNIT: Homodecamer; pentamer of dimers.
CC {ECO:0000256|ARBA:ARBA00011424}.
CC -!- SIMILARITY: Belongs to the PanB family.
CC {ECO:0000256|ARBA:ARBA00008676}.
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:PPE72423.1}.
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DR EMBL; PSNW01000012; PPE72423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5TBP8; -.
DR OrthoDB; 9781789at2; -.
DR Proteomes; UP000238220; Unassembled WGS sequence.
DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-EC.
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-KW.
DR CDD; cd06557; KPHMT-like; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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 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 Magnesium {ECO:0000256|PIRSR:PIRSR000388-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000388-3};
KW Methyltransferase {ECO:0000313|EMBL:PPE72423.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000238220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PPE72423.1}.
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-1"
FT BINDING 46..47
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 85
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 113
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-3"
SQ SEQUENCE 251 AA; 26237 MW; D6E8BFEDCB553347 CRC64;
MSTAKHTAAS LRAMKAVARI PMLTAYTTPV ARALEKARVP VLLVGDTVGM VEMGFDSTRQ
VTLDHMCYHV GAVRRGAPAT HIIGDLPYET DGDPETALRS ARALITAGAD SVKLEGPKLE
VIRHLVAQGI DVVGHTGLTP QTSTNFKQVG REAPDAQRIL DEARAIAGAG AFLVVLEHIP
AALGEAVTRA IAVPTIGIGA GSGCDGQVLV INDAMGLGER WPPFSRQYAF MGQAIVDAAA
TYVGQVTGGT Y
//