PANB_BURTA
ID PANB_BURTA Reviewed; 271 AA.
AC Q2SYZ1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=BTH_I1311;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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=ABC38840.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000086; ABC38840.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_025369782.1; NZ_CP008785.1.
DR PDB; 3VAV; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=1-271.
DR PDBsum; 3VAV; -.
DR AlphaFoldDB; Q2SYZ1; -.
DR SMR; Q2SYZ1; -.
DR PRIDE; Q2SYZ1; -.
DR EnsemblBacteria; ABC38840; ABC38840; BTH_I1311.
DR KEGG; bte:BTH_I1311; -.
DR HOGENOM; CLU_036645_1_0_4; -.
DR OrthoDB; 916845at2; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000001930; Chromosome I.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Magnesium; Metal-binding;
KW Pantothenate biosynthesis; Transferase.
FT CHAIN 1..271
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT /id="PRO_0000297237"
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"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:3VAV"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:3VAV"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:3VAV"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:3VAV"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:3VAV"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3VAV"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:3VAV"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:3VAV"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:3VAV"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:3VAV"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3VAV"
SQ SEQUENCE 271 AA; 28726 MW; A3D42CB528EFFC99 CRC64;
MTYLQESSRP AVTVPKLQAM REAGEKIAML TCYDASFAAL LDRANVDVQL IGDSLGNVLQ
GQTTTLPVTL DDIAYHTACV ARAQPRALIV ADLPFGTYGT PADAFASAVK LMRAGAQMVK
FEGGEWLAET VRFLVERAVP VCAHVGLTPQ SVHAFGGFKV QGKTEAGAAQ LLRDARAVEE
AGAQLIVLEA VPTLVAAEVT RELSIPTIGI GAGAECSGQV LVLHDMLGVF PGKRPRFVKD
FMQGQPSIFA AVEAYVRAVK DGSFPGPEHS F
