PANB_BURMA
ID PANB_BURMA Reviewed; 271 AA.
AC Q62HD8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
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}; OrderedLocusNames=BMA2323;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU49787.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000010; AAU49787.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004194137.1; NC_006348.1.
DR RefSeq; YP_103882.1; NC_006348.1.
DR AlphaFoldDB; Q62HD8; -.
DR SMR; Q62HD8; -.
DR STRING; 243160.BMA2323; -.
DR EnsemblBacteria; AAU49787; AAU49787; BMA2323.
DR GeneID; 56594687; -.
DR KEGG; bma:BMA2323; -.
DR PATRIC; fig|243160.12.peg.2390; -.
DR eggNOG; COG0413; Bacteria.
DR HOGENOM; CLU_036645_1_0_4; -.
DR OMA; VLVWTDM; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000006693; Chromosome 1.
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..271
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT /id="PRO_0000184830"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 53..54
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 92
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 120
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
SQ SEQUENCE 271 AA; 28618 MW; E279FF169C23C041 CRC64;
MTYLQESSRP AVTVPKLQAM REAGEKIAML TSYDASFAAL LDRANVDVQL IGDSLGNVLQ
GQATTLPVTL DDIAYHTACV ARAQPRGLVV ADLPFGTYGT PADAFASAVK LMRAGAQMVK
LEGGEWLAET VRFLVERAVP VCAHVGLTPQ SVHAFGGFKV QGKTEAGAAQ LLRDARAVEE
AGAQLIVLEA VPTLVAAEVT RELSIPTIGI GAGAECSGQV LVLHDMLGVF PGKRPRFVKD
FMQGQPSIFA AVEAYVRAVK DGSFPGPEHS F
