ID A0A0D6EWI4_9PROT Unreviewed; 251 AA.
AC A0A0D6EWI4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:CEZ19987.1};
GN ORFNames=BN1208_1106 {ECO:0000313|EMBL:CEZ19987.1};
OS Candidatus Methylopumilus planktonicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylopumilus.
OX NCBI_TaxID=1581557 {ECO:0000313|EMBL:CEZ19987.1, ECO:0000313|Proteomes:UP000064007};
RN [1] {ECO:0000313|Proteomes:UP000064007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000064007};
RA Salcher M.M.;
RL Submitted (DEC-2014) 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 ---------------------------------------------------------------------------
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; LN827929; CEZ19987.1; -; Genomic_DNA.
DR RefSeq; WP_046488656.1; NZ_LN827929.1.
DR AlphaFoldDB; A0A0D6EWI4; -.
DR STRING; 1581557.BN1208_1106; -.
DR KEGG; mbat:BN1208_1106; -.
DR HOGENOM; CLU_036645_1_0_4; -.
DR OrthoDB; 9781789at2; -.
DR Proteomes; UP000064007; Chromosome 1.
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 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:CEZ19987.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000064007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEZ19987.1}.
FT BINDING 42..43
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 81
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 109
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-3"
SQ SEQUENCE 251 AA; 27382 MW; B40FDB9B04AA71DE CRC64;
MNLTSLKSMK KSGKKITILT CYDASFARLL ESIEVDAILV GDSLGMFIKG EANTHDVSLN
DMIYHTKSVS RGAQSSFIIS DLPIHTYETN DLAYKNALAL IEAGAHMVKL EGGASLTSIV
THLKTKDIKV CGHIGYMPQS IKNMNSNEIQ HALQKTLGTI IEDAKALEKS GADMLVLSSV
PEDIAKHITQ EISIPTIGFH SGGTCDGEVF ILYDLLMNSN TSQDLYLDNT ASSNKNTDIK
NLLLEFIKNR S
//