ID A0A1C7H170_9BACE Unreviewed; 273 AA.
AC A0A1C7H170; A0A4S2D2F8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ECO:0000313|EMBL:NDO59821.1};
GN ORFNames=A4V03_09255 {ECO:0000313|EMBL:ANU57736.1}, E5353_09610
GN {ECO:0000313|EMBL:TGY35152.1}, FMM78_08830
GN {ECO:0000313|EMBL:NDO59821.1};
OS Bacteroides caecimuris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1796613 {ECO:0000313|EMBL:ANU57736.1, ECO:0000313|Proteomes:UP000092631};
RN [1] {ECO:0000313|Proteomes:UP000092631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I48 {ECO:0000313|Proteomes:UP000092631};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANU57736.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I48 {ECO:0000313|EMBL:ANU57736.1};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TGY35152.1, ECO:0000313|Proteomes:UP000309566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM63_1-25 {ECO:0000313|EMBL:TGY35152.1,
RC ECO:0000313|Proteomes:UP000309566};
RA Navarre W., Wong E., Huang K., Tropini C., Ng K., Yu B.;
RT "Microbes associate with the intestines of laboratory mice.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:NDO59821.1, ECO:0000313|Proteomes:UP000589339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD237 {ECO:0000313|EMBL:NDO59821.1,
RC ECO:0000313|Proteomes:UP000589339};
RA Elie C., Mathieu A., Saliou A., Darnaud M., Leulier F., Tamellini A.;
RT "Draft genome sequences of 15 bacterial species constituting the stable
RT defined intestinal microbiota of the GM15 gnotobiotic mouse model.";
RL Submitted (JUN-2019) 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}.
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DR EMBL; CP015401; ANU57736.1; -; Genomic_DNA.
DR EMBL; VIRD01000036; NDO59821.1; -; Genomic_DNA.
DR EMBL; SRYX01000030; TGY35152.1; -; Genomic_DNA.
DR RefSeq; WP_065538707.1; NZ_VIRD01000036.1.
DR AlphaFoldDB; A0A1C7H170; -.
DR STRING; 1796613.A4V03_09255; -.
DR GeneID; 82187324; -.
DR KEGG; bcae:A4V03_09255; -.
DR OrthoDB; 9781789at2; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000092631; Chromosome.
DR Proteomes; UP000309566; Unassembled WGS sequence.
DR Proteomes; UP000589339; 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; Phosphoenolpyruvate-binding domains; 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 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 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:ANU57736.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|HAMAP-Rule:MF_00156};
KW Reference proteome {ECO:0000313|Proteomes:UP000092631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00156}.
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-1"
FT BINDING 53..54
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 92
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 122
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-3"
SQ SEQUENCE 273 AA; 29987 MW; 16F050FDEA0DE9A1 CRC64;
MAGYISDDTR KVTTHRLVEM KQRGEKISML TAYDYTMAQI VDGAGMDVIL VGDSASNVMA
GNVTTLPITL DQMIYHAKSV VRGVKRAMVV VDMPFGSYQG NEMEGLASAI RIMKESHADA
LKLEGGEEII DTVKRIVCAG IPVMGHLGLM PQSINKYGTY TVRAKDEAEA DKLIRDAHLL
EEAGCFAIVL EKIPATLAER VASELTIPII GIGAGGHVDG QVLVVQDMLG MNNGFRPRFL
RRYADLYTVM TDAISRYVSD VKNCYFPNEK EQY
//
