PANB_SULIM
ID PANB_SULIM Reviewed; 267 AA.
AC C3MU48;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=M1425_0191;
OS Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.14.25 / Kamchatka #1;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-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; CP001400; ACP37082.1; -; Genomic_DNA.
DR RefSeq; WP_012710369.1; NC_012588.1.
DR AlphaFoldDB; C3MU48; -.
DR SMR; C3MU48; -.
DR EnsemblBacteria; ACP37082; ACP37082; M1425_0191.
DR GeneID; 7813884; -.
DR GeneID; 7940076; -.
DR KEGG; sia:M1425_0191; -.
DR HOGENOM; CLU_036645_1_0_2; -.
DR OMA; VLVWTDM; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000001350; 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:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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 Coenzyme A biosynthesis; Cytoplasm; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..267
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT /id="PRO_1000203480"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 45..46
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 84
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 113
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
SQ SEQUENCE 267 AA; 29502 MW; 39725AD41540B0E7 CRC64;
MKKVTIRDFI KKKSTKEKIT ILTAYDYPTA KIISNTGLDS ILVGDSLGMV VLGYANTLNV
TMRDMISHTR AVARANPPQL IVADMPFLSY EIDTKSAVKN AGLLVKAGSD AIKLEGGEEM
KDTVKAIVKA GIPVMGHIGL TPQRFLRLGG FRTIGKTKQE EDQLIKDSLE LEDAGVFSLV
IENTYVDIAK RITEKLNIPT ICIGAGPYCD GQVLVINDLL GLSEFTPYFA KSYVNLKEII
SNAINQYIID VKNNKFPEKQ HYKEKES
