(data stored in ACNUC7421 zone)

SWISSPROT: PANB_SHISS

ID   PANB_SHISS              Reviewed;         264 AA.
AC   Q3Z5M6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 86.
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};
GN   OrderedLocusNames=SSON_0142;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl
CC       group from 5,10-methylenetetrahydrofolate is transferred onto
CC       alpha-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-
CC         2-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-
CC       Rule:MF_00156};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
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}.
DR   EMBL; CP000038; AAZ86936.1; -; Genomic_DNA.
DR   SMR; Q3Z5M6; -.
DR   EnsemblBacteria; AAZ86936; AAZ86936; SSON_0142.
DR   KEGG; ssn:SSON_0142; -.
DR   HOGENOM; HOG000078427; -.
DR   KO; K00606; -.
DR   OMA; GHIGLMP; -.
DR   BioCyc; SSON300269:G1GL2-160-MONOMER; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000002529; 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;
DR   PRODOM; Q3Z5M6.
DR   SWISS-2DPAGE; Q3Z5M6.
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Pantothenate biosynthesis; Transferase.
FT   CHAIN         1    264       3-methyl-2-oxobutanoate
FT                                hydroxymethyltransferase.
FT                                /FTId=PRO_0000297378.
FT   REGION       45     46       Alpha-ketoisovalerate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00156}.
FT   ACT_SITE    181    181       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   METAL        45     45       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   METAL        84     84       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   METAL       114    114       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   BINDING      84     84       Alpha-ketoisovalerate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00156}.
FT   BINDING     112    112       Alpha-ketoisovalerate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00156}.
SQ   SEQUENCE   264 AA;  28151 MW;  E5B75695EE5C55F1 CRC64;
     MKPTTIASLQ KCKQDKKRFA TITAYDYSFA KLFADEGLNV MLVGDSLGMT VQGHDSTLPV
     TVADIAYHTA SVRRGAPNCL LLADLPFMAY ATPEQAFENA ATVMRAGANM VKIEGGEWLV
     ETVKMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRGDEAG DQLLSDALAL EAAGAQLLVL
     ECVPIELAKR ITEALAIPVI GIGAGNVTDG QILVMHDAFG ITGGHIPKFA KNFLAETGDI
     RAAVRQYMAE VESGVYPGEE HSFH
//

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