ID A0A174VLJ7_9BACE Unreviewed; 273 AA.
AC A0A174VLJ7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:CUQ31899.1};
GN ORFNames=DW190_05180 {ECO:0000313|EMBL:RHH94067.1}, DW794_13355
GN {ECO:0000313|EMBL:RHD46715.1}, DWY26_10845
GN {ECO:0000313|EMBL:RGR71014.1}, DXA49_13045
GN {ECO:0000313|EMBL:RGY24669.1}, ERS852494_01542
GN {ECO:0000313|EMBL:CUP11935.1}, ERS852558_02600
GN {ECO:0000313|EMBL:CUQ31899.1}, F2Y31_11230
GN {ECO:0000313|EMBL:KAA5498511.1}, F2Y35_12985
GN {ECO:0000313|EMBL:KAA5490952.1}, F2Y36_00565
GN {ECO:0000313|EMBL:KAA5466383.1}, F2Y39_17695
GN {ECO:0000313|EMBL:KAA5473514.1}, NXW23_14045
GN {ECO:0000313|EMBL:UVQ95488.1};
OS Bacteroides caccae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=47678 {ECO:0000313|EMBL:CUQ31899.1, ECO:0000313|Proteomes:UP000095725};
RN [1] {ECO:0000313|Proteomes:UP000095657, ECO:0000313|Proteomes:UP000095725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834880 {ECO:0000313|EMBL:CUP11935.1,
RC ECO:0000313|Proteomes:UP000095657}, and 2789STDY5834946
RC {ECO:0000313|EMBL:CUQ31899.1, ECO:0000313|Proteomes:UP000095725};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000283512, ECO:0000313|Proteomes:UP000284205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF24-29LB {ECO:0000313|EMBL:RGR71014.1,
RC ECO:0000313|Proteomes:UP000284205}, AM16-49B
RC {ECO:0000313|EMBL:RHH94067.1, ECO:0000313|Proteomes:UP000283512},
RC AM31-16AC {ECO:0000313|EMBL:RHD46715.1,
RC ECO:0000313|Proteomes:UP000284689}, and OF02-6LB
RC {ECO:0000313|EMBL:RGY24669.1, ECO:0000313|Proteomes:UP000284431};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000368418, ECO:0000313|Proteomes:UP000427825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A19 {ECO:0000313|EMBL:KAA5498511.1,
RC ECO:0000313|Proteomes:UP000368418}, BIOML-A21
RC {ECO:0000313|EMBL:KAA5490952.1, ECO:0000313|Proteomes:UP000491168},
RC BIOML-A25 {ECO:0000313|EMBL:KAA5473514.1,
RC ECO:0000313|Proteomes:UP000427825}, and BIOML-A31
RC {ECO:0000313|EMBL:KAA5466383.1, ECO:0000313|Proteomes:UP000475905};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
RN [4] {ECO:0000313|EMBL:UVQ95488.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BFG-474 {ECO:0000313|EMBL:UVQ95488.1};
RA Tisza M.J., Smith D., Dekker J.P.;
RT "Genome Sequencing of Bacteroides fragilis Group Isolates with Nanopore
RT Technology.";
RL Submitted (AUG-2022) 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; CZAI01000003; CUP11935.1; -; Genomic_DNA.
DR EMBL; CZBL01000010; CUQ31899.1; -; Genomic_DNA.
DR EMBL; VVYP01000001; KAA5466383.1; -; Genomic_DNA.
DR EMBL; VVYJ01000011; KAA5473514.1; -; Genomic_DNA.
DR EMBL; VVYF01000012; KAA5490952.1; -; Genomic_DNA.
DR EMBL; VVYD01000009; KAA5498511.1; -; Genomic_DNA.
DR EMBL; QRUO01000009; RGR71014.1; -; Genomic_DNA.
DR EMBL; QSCS01000020; RGY24669.1; -; Genomic_DNA.
DR EMBL; QSJD01000021; RHD46715.1; -; Genomic_DNA.
DR EMBL; QRKD01000002; RHH94067.1; -; Genomic_DNA.
DR EMBL; CP103166; UVQ95488.1; -; Genomic_DNA.
DR RefSeq; WP_005676105.1; NZ_VVYQ01000001.1.
DR STRING; 47678.ERS852494_01542; -.
DR GeneID; 75114340; -.
DR KEGG; bcac:CGC64_12560; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000095657; Unassembled WGS sequence.
DR Proteomes; UP000095725; Unassembled WGS sequence.
DR Proteomes; UP000283512; Unassembled WGS sequence.
DR Proteomes; UP000284205; Unassembled WGS sequence.
DR Proteomes; UP000284431; Unassembled WGS sequence.
DR Proteomes; UP000284689; Unassembled WGS sequence.
DR Proteomes; UP000368418; Unassembled WGS sequence.
DR Proteomes; UP000427825; Unassembled WGS sequence.
DR Proteomes; UP000475905; Unassembled WGS sequence.
DR Proteomes; UP000491168; Unassembled WGS sequence.
DR Proteomes; UP001060260; Chromosome.
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:CUQ31899.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|HAMAP-Rule:MF_00156};
KW Reference proteome {ECO:0000313|Proteomes:UP000095657};
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; 29969 MW; 552A18752E48FC61 CRC64;
MAGYISDDTR KVTTHRLVEM KQRGEKISML TAYDYTMAQI VDGAGMDVIL VGDSASNVMA
GNVTTLPITL DQMIYHAKSV VRGVKRAMVV VDMPFGSYQG NEMEGLASAI RIMKESHADA
LKLEGGEEII DTVKRIISAG IPVMGHLGLM PQSINKYGTY TVRAKDDAEA DKLIRDAHLL
EEAGCFAIVL EKIPATLAER VAAELTIPII GIGAGGHVDG QVLVIQDMLG MNNGFRPRFL
RRYADLYTVM TDAISRYVSD VKNCYFPNEK EQY
//
