ID   PANB_SALNS              Reviewed;         263 AA.
AC   B4SUA8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156};
DE            EC=2.1.2.11 {ECO:0000255|HAMAP-Rule:MF_00156};
DE   AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156};
DE            Short=KPHMT {ECO:0000255|HAMAP-Rule:MF_00156};
GN   Name=panB {ECO:0000255|HAMAP-Rule:MF_00156};
GN   OrderedLocusNames=SNSL254_A0199;
OS   Salmonella newport (strain SL254).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=423368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL254;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00156};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00156};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00156};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00156}.
CC   -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_00156}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00156}.
CC   -!- SIMILARITY: Belongs to the PanB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00156}.
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DR   EMBL; CP001113; ACF61163.1; -; Genomic_DNA.
DR   RefSeq; WP_000805487.1; NZ_CCMR01000003.1.
DR   AlphaFoldDB; B4SUA8; -.
DR   SMR; B4SUA8; -.
DR   EnsemblBacteria; ACF61163; ACF61163; SNSL254_A0199.
DR   KEGG; see:SNSL254_A0199; -.
DR   HOGENOM; CLU_036645_1_0_6; -.
DR   OMA; VLVWTDM; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000008824; 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:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06557; KPHMT-like; 1.
DR   Gene3D; 3.20.20.60; -; 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   PANTHER; PTHR20881; PTHR20881; 1.
DR   Pfam; PF02548; Pantoate_transf; 1.
DR   PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR00222; panB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Magnesium; Metal-binding; Pantothenate biosynthesis;
KW   Transferase.
FT   CHAIN           1..263
FT                   /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT                   /id="PRO_1000097005"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         45..46
FT                   /ligand="3-methyl-2-oxobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:11851"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         84
FT                   /ligand="3-methyl-2-oxobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:11851"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         112
FT                   /ligand="3-methyl-2-oxobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:11851"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
SQ   SEQUENCE   263 AA;  28105 MW;  D4913FBDB5577603 CRC64;
     MKPTTISLLQ KCKQEKKRFA TITAYDYSFA KLFADEGINV MLVGDSLGMT IQGHDSTLPV
     TVEDIAYHTR AVRRGAPNCL LLSDLPFMAY ATPEQACENA AIVMRAGANM VKIEGGAWLV
     DTVKMLTERA VPVCGHLGLT PQSVNIFGGY KIQGRGDAGQ VLLDDALALE AAGAQLLVLE
     CVPVELAKRV TEALSIPVIG IGAGNVTDGQ ILVMHDAFGI TGGHIPKFAK NFLAEAGDMR
     AAVQQYMAEV ESGVYPGEEH SFH