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Database: UniProt
Entry: V9V378_9PSED
LinkDB: V9V378_9PSED
Original site: V9V378_9PSED 
ID   V9V378_9PSED            Unreviewed;       266 AA.
AC   V9V378;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
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   ORFNames=X970_22040 {ECO:0000313|EMBL:AHC89959.1};
OS   Pseudomonas monteilii SB3101.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1435058 {ECO:0000313|EMBL:AHC89959.1, ECO:0000313|Proteomes:UP000018660};
RN   [1] {ECO:0000313|EMBL:AHC89959.1, ECO:0000313|Proteomes:UP000018660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB3101 {ECO:0000313|EMBL:AHC89959.1,
RC   ECO:0000313|Proteomes:UP000018660};
RA   Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D., Nilsen P.H.,
RA   Nielsen J.L.;
RT   "Complete Genomes of Pseudomonas monteilii SB3078 and SB3101, two Benzene,
RT   Toluene and Ethylbenzene Degrading Bacteria used for Bioaugmentation.";
RL   Submitted (DEC-2013) 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; CP006979; AHC89959.1; -; Genomic_DNA.
DR   RefSeq; WP_023661348.1; NC_023076.1.
DR   AlphaFoldDB; V9V378; -.
DR   KEGG; pmot:X970_22040; -.
DR   PATRIC; fig|1435058.3.peg.4280; -.
DR   HOGENOM; CLU_036645_1_0_6; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000018660; 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:AHC89959.1};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW   ECO:0000256|HAMAP-Rule:MF_00156};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00156}.
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT                   ECO:0000256|PIRSR:PIRSR000388-1"
FT   BINDING         45..46
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         45
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         84
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         84
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         112
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         114
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   266 AA;  27751 MW;  E17ACCC81A43F7D0 CRC64;
     MPEVTLTTLN GLKAKGEKIT MLTCYDATFA KAASQAGVEV LLVGDSLGMV LQGHDSTLPV
     TTADMAYHTA SVKRGNDGAL ILADLPFMAH ATPELAFANS ATLMQAGAHM IKIEGAAWLA
     ETIRLLAERG VPVCAHMGLT PQTVNVMGGY KVQGRQEAQA RQMRADAIAL EQAGAAMLLL
     ECVPSELAAE ITSAVSIPVI GIGAGNGTDG QVLVLHDMLG LSLSGRVPKF VKNFMQGQPD
     IHSALVAYVE AVKQVSFPGS EHGFSA
//
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