PANB_MYCUA
ID PANB_MYCUA Reviewed; 297 AA.
AC A0PNG6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=MUL_1330;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL03885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0PNG6; -.
DR SMR; A0PNG6; -.
DR STRING; 362242.MUL_1330; -.
DR EnsemblBacteria; ABL03885; ABL03885; MUL_1330.
DR KEGG; mul:MUL_1330; -.
DR eggNOG; COG0413; Bacteria.
DR HOGENOM; CLU_036645_1_0_11; -.
DR OMA; VLVWTDM; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000000765; 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..297
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT /id="PRO_0000297303"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 78..79
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 117
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 147
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
SQ SEQUENCE 297 AA; 30933 MW; 0DB00D971D529F1A CRC64;
MSEQISEQSE QNVYGACPPV PAGESSPSAA SAPRTKVRTH HLQKWKAEGH KWAMLTVYDY
STARAFDDAG IPVLLVGDSA ANVVYGYDTT VPISIDELIP LVRGVVRGAP HALVVADLPF
GSYESGPSAA LAAATRFMKE AGAHAVKLEG GERVAEQIAC LTAAGIPVMA HIGFTPQSVN
TLGGFRVQGR GDAAEQTIAD AIAVAEAGAF SVVMEMVPAE LATQITGKLT IPTIGIGAGP
SCDGQVLVWQ DMAGLSSGKA PRFVKRYADV GGELRRAAVQ YAQDVAGGVF PAEEHCF
