PANB_TRIL1
ID PANB_TRIL1 Reviewed; 266 AA.
AC B3E5K9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Glov_0957;
OS Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter
OS lovleyi).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Trichlorobacter.
OX NCBI_TaxID=398767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E.,
RA Ritalahti K.M., Loeffler F.E., Richardson P.;
RT "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001089; ACD94680.1; -; Genomic_DNA.
DR RefSeq; WP_012469030.1; NC_010814.1.
DR AlphaFoldDB; B3E5K9; -.
DR SMR; B3E5K9; -.
DR STRING; 398767.Glov_0957; -.
DR EnsemblBacteria; ACD94680; ACD94680; Glov_0957.
DR KEGG; glo:Glov_0957; -.
DR eggNOG; COG0413; Bacteria.
DR HOGENOM; CLU_036645_1_0_7; -.
DR OMA; VLVWTDM; -.
DR OrthoDB; 916845at2; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000002420; 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 Reference proteome; Transferase.
FT CHAIN 1..266
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT /id="PRO_1000096968"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 46..47
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 85
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 115
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"
SQ SEQUENCE 266 AA; 28639 MW; 8AE6F50180C50AB9 CRC64;
MRKKITIPEI LLMKQEGRKV TVLTAYDYPT ARLVDAGGVD AILVGDSAGV VFSGHENTLP
VTMDEMLYHV KAVVRARPKA LVVADMPFMA CQSGEIEALK NCGRMLQEGG AEAVKIEGGS
NMAPIIRAVT EMDIPVMGHV GLTPQSVHRM GGYKVQGRKD QAERILEDAH AVQEAGAFAV
VLEGIPAKLA ARITEMLEIP TIGIGAGPAC DGQVLVIHDI LGLCEKYSPK FVKRYADLAP
LITEAARQYV SEVKDGTFPT EEHSFS
