PANB_ECOLI
ID PANB_ECOLI Reviewed; 264 AA.
AC P31057;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase;
DE EC=2.1.2.11 {ECO:0000269|PubMed:6463, ECO:0000269|PubMed:776976};
DE AltName: Full=Ketopantoate hydroxymethyltransferase;
DE Short=KPHMT;
GN Name=panB; OrderedLocusNames=b0134, JW0130;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Merkel W.K., Nichols B.P.;
RT "Nucleotide sequence of the Escherichia coli panBCD gene cluster.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RC STRAIN=K12;
RX PubMed=8096212; DOI=10.1128/jb.175.7.2125-2130.1993;
RA Jones C.E., Brook J.M., Buck D., Abell C., Smith A.G.;
RT "Cloning and sequencing of the Escherichia coli panB gene, which encodes
RT ketopantoate hydroxymethyltransferase, and overexpression of the enzyme.";
RL J. Bacteriol. 175:2125-2130(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=776976; DOI=10.1016/s0021-9258(17)33412-9;
RA Teller J.H., Powers S.G., Snell E.E.;
RT "Ketopantoate hydroxymethyltransferase. I. Purification and role in
RT pantothenate biosynthesis.";
RL J. Biol. Chem. 251:3780-3785(1976).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, COFACTOR, SUBUNIT, AND PATHWAY.
RX PubMed=6463; DOI=10.1016/s0021-9258(17)33413-0;
RA Powers S.G., Snell E.E.;
RT "Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and
RT regulatory properties.";
RL J. Biol. Chem. 251:3786-3793(1976).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ITS PRODUCT AND
RP MAGNESIUM IONS, REACTION MECHANISM, MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=12906829; DOI=10.1016/s0969-2126(03)00158-8;
RA von Delft F., Inoue T., Saldanha S.A., Ottenhof H.H., Schmitzberger F.,
RA Birch L.M., Dhanaraj V., Witty M., Smith A.G., Blundell T.L., Abell C.;
RT "Structure of E. coli ketopantoate hydroxymethyl transferase complexed with
RT ketopantoate and Mg2+, solved by locating 160 selenomethionine sites.";
RL Structure 11:985-996(2003).
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:0000269|PubMed:6463,
CC ECO:0000269|PubMed:776976}.
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:0000269|PubMed:6463,
CC ECO:0000269|PubMed:776976};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11825;
CC Evidence={ECO:0000269|PubMed:6463, ECO:0000269|PubMed:776976};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11826;
CC Evidence={ECO:0000269|PubMed:6463, ECO:0000269|PubMed:776976};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:6463};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:6463};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:6463};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:6463};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also use Mn(2+), Co(2+) and
CC Zn(2+) to a lesser extent. {ECO:0000269|PubMed:6463};
CC -!- ACTIVITY REGULATION: Inhibited by isovalerate, pyruvate, 3-methyl-2-
CC butanone, and valine. Partially inhibited by formaldehyde and
CC tetrahydrofolate below or near the KM value. Also inhibited by later
CC intermediates pantoate, pantothenate and coenzyme A.
CC {ECO:0000269|PubMed:6463}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for ketopantoate {ECO:0000269|PubMed:6463};
CC KM=0.18 mM for L-tetrahydrofolate {ECO:0000269|PubMed:6463};
CC KM=1.0 mM for alpha-ketoisovalerate (at 37 degrees Celsius and pH
CC 6.8) {ECO:0000269|PubMed:6463};
CC KM=2.9 mM for alpha-ketobutyrate (at 37 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:6463};
CC KM=5.9 mM for formaldehyde {ECO:0000269|PubMed:6463};
CC KM=5.9 mM for alpha-keto-beta-methylvalerate (at 37 degrees Celsius
CC and pH 6.8) {ECO:0000269|PubMed:6463};
CC KM=25 mM for alpha-ketovalerate (at 37 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:6463};
CC Vmax=8.25 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:6463};
CC Vmax=7.3 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:6463};
CC Vmax=4 umol/min/mg enzyme with alpha-ketobutyrate as substrate (at 37
CC degrees Celsius and pH 6.8) {ECO:0000269|PubMed:6463};
CC Vmax=2.8 umol/min/mg enzyme with alpha-ketoisovalerate as substrate
CC (at 37 degrees Celsius and pH 6.8) {ECO:0000269|PubMed:6463};
CC Vmax=2 umol/min/mg enzyme with alpha-ketovalerate as substrate (at 37
CC degrees Celsius and pH 6.8) {ECO:0000269|PubMed:6463};
CC Vmax=0.43 umol/min/mg enzyme with alpha-keto-beta-methylvalerate as
CC substrate (at 37 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:6463};
CC pH dependence:
CC Optimum pH is 7.0-7.6. Stable from pH 5.0 to 10.0. Rapidly
CC inactivated below pH 4.5. {ECO:0000269|PubMed:6463};
CC Temperature dependence:
CC Optimum temperature is 70-80 degrees Celsius.
CC {ECO:0000269|PubMed:6463};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC {ECO:0000305|PubMed:6463, ECO:0000305|PubMed:776976}.
CC -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000269|PubMed:12906829,
CC ECO:0000269|PubMed:6463}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=28234; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12906829};
CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000305}.
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DR EMBL; L17086; AAA24271.1; -; Genomic_DNA.
DR EMBL; X65538; CAA46505.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73245.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96711.1; -; Genomic_DNA.
DR PIR; F64736; F64736.
DR RefSeq; NP_414676.1; NC_000913.3.
DR RefSeq; WP_000805497.1; NZ_STEB01000010.1.
DR PDB; 1M3U; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=1-264.
DR PDBsum; 1M3U; -.
DR AlphaFoldDB; P31057; -.
DR SMR; P31057; -.
DR BioGRID; 4261383; 256.
DR DIP; DIP-10436N; -.
DR IntAct; P31057; 8.
DR STRING; 511145.b0134; -.
DR DrugBank; DB03795; 2-Dehydropantoate.
DR jPOST; P31057; -.
DR PaxDb; P31057; -.
DR PRIDE; P31057; -.
DR EnsemblBacteria; AAC73245; AAC73245; b0134.
DR EnsemblBacteria; BAB96711; BAB96711; BAB96711.
DR GeneID; 944839; -.
DR KEGG; ecj:JW0130; -.
DR KEGG; eco:b0134; -.
DR PATRIC; fig|1411691.4.peg.2147; -.
DR EchoBASE; EB1626; -.
DR eggNOG; COG0413; Bacteria.
DR HOGENOM; CLU_036645_1_0_6; -.
DR InParanoid; P31057; -.
DR OMA; VLVWTDM; -.
DR PhylomeDB; P31057; -.
DR BioCyc; EcoCyc:3-CH3-2-OXOBUTANOATE-OH-CH3-XFER-MON; -.
DR BioCyc; MetaCyc:3-CH3-2-OXOBUTANOATE-OH-CH3-XFER-MON; -.
DR BRENDA; 2.1.2.11; 2026.
DR SABIO-RK; P31057; -.
DR UniPathway; UPA00028; UER00003.
DR EvolutionaryTrace; P31057; -.
DR PRO; PR:P31057; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Magnesium;
KW Metal-binding; Pantothenate biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..264
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT /id="PRO_0000184841"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT BINDING 45..46
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 84
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 112
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 7..8
FT /note="SL -> AS (in Ref. 2; CAA46505)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="Y -> C (in Ref. 2; CAA46505)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="E -> D (in Ref. 2; CAA46505)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="A -> E (in Ref. 2; CAA46505)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="Q -> K (in Ref. 2; CAA46505)"
FT /evidence="ECO:0000305"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 157..173
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1M3U"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:1M3U"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:1M3U"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1M3U"
SQ SEQUENCE 264 AA; 28237 MW; 0437D6BB9EBF817B CRC64;
MKPTTISLLQ KYKQEKKRFA TITAYDYSFA KLFADEGLNV MLVGDSLGMT VQGHDSTLPV
TVADIAYHTA AVRRGAPNCL LLADLPFMAY ATPEQAFENA ATVMRAGANM VKIEGGEWLV
ETVQMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRGDEAG DQLLSDALAL EAAGAQLLVL
ECVPVELAKR ITEALAIPVI GIGAGNVTDG QILVMHDAFG ITGGHIPKFA KNFLAETGDI
RAAVRQYMAE VESGVYPGEE HSFH
