ID A0A3B0CH83_9BACL Unreviewed; 276 AA.
AC A0A3B0CH83;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:RKN84490.1};
GN ORFNames=D7M11_13510 {ECO:0000313|EMBL:RKN84490.1};
OS Paenibacillus ginsengarvi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=400777 {ECO:0000313|EMBL:RKN84490.1, ECO:0000313|Proteomes:UP000282311};
RN [1] {ECO:0000313|EMBL:RKN84490.1, ECO:0000313|Proteomes:UP000282311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13059 {ECO:0000313|EMBL:RKN84490.1,
RC ECO:0000313|Proteomes:UP000282311};
RX PubMed=17684262; DOI=10.1099/ijs.0.64906-0;
RA Yoon M.H., Ten L.N., Im W.T.;
RT "Paenibacillus ginsengarvi sp. nov., isolated from soil from ginseng
RT cultivation.";
RL Int. J. Syst. Evol. Microbiol. 57:1810-1814(2007).
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:RKN84490.1}.
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DR EMBL; RBAH01000008; RKN84490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0CH83; -.
DR OrthoDB; 9781789at2; -.
DR Proteomes; UP000282311; 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|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000388-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000388-3};
KW Methyltransferase {ECO:0000313|EMBL:RKN84490.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000282311};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RKN84490.1}.
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-1"
FT BINDING 44..45
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 83
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 111
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000388-3"
SQ SEQUENCE 276 AA; 30411 MW; A82A6843BA4A2B36 CRC64;
MTTTMQELHR KKQMSRKITM LTCYDYPTAV LQDKAGLDVI FVGDSLGTNE LGYERETSVT
LGEIVHHLKA VRRGVQEAYL LADLPYKTYD DPGMAMITAR ELLSHGADGV KLEGMQEAVI
SHLAGSGIEV CAHLGYNPQF HEKAAVKGKT YDAARALLES AVSLQNAGAS MIVLELIPEE
LGKAITETLT IPTIGIGAGR YTDGQVLIVH DMLGLTPHPL RHAKNYANAG EWMLQAFRAY
AEEVTNGQFP QPANARTMID SERERFMGWY SGKDRK
//
