(data stored in SCRATCH zone)

SWISSPROT: C8U1K4_ECO10

ID   C8U1K4_ECO10            Unreviewed;       264 AA.
AC   C8U1K4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00156};
DE            EC=2.1.2.11 {ECO:0000256|HAMAP-Rule:MF_00156};
DE   AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00156};
DE            Short=KPHMT {ECO:0000256|HAMAP-Rule:MF_00156};
GN   Name=panB {ECO:0000256|HAMAP-Rule:MF_00156,
GN   ECO:0000313|EMBL:BAI29012.1};
GN   OrderedLocusNames=ECO103_0134 {ECO:0000313|EMBL:BAI29012.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29012.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29012.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|HAMAP-
CC       Rule:MF_00156, ECO:0000256|SAAS:SAAS00843518}.
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:0000256|HAMAP-
CC         Rule:MF_00156, ECO:0000256|SAAS:SAAS01125081};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00156, ECO:0000256|PIRSR:PIRSR000388-3};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00156, ECO:0000256|PIRSR:PIRSR000388-3};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS00771269}.
CC   -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00156, ECO:0000256|SAAS:SAAS00771257}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156,
CC       ECO:0000256|SAAS:SAAS00771239}.
CC   -!- SIMILARITY: Belongs to the PanB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00156, ECO:0000256|SAAS:SAAS00771235}.
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DR   EMBL; AP010958; BAI29012.1; -; Genomic_DNA.
DR   RefSeq; WP_000805455.1; NC_013353.1.
DR   SMR; C8U1K4; -.
DR   EnsemblBacteria; BAI29012; BAI29012; ECO103_0134.
DR   KEGG; eoh:ECO103_0134; -.
DR   HOGENOM; HOG000078427; -.
DR   KO; K00606; -.
DR   OMA; GHIGLMP; -.
DR   BioCyc; ECOL585395:ECO103_RS00685-MONOMER; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000000959; 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:0008168; F:methyltransferase activity; 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; C8U1K4.
DR   SWISS-2DPAGE; C8U1K4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|SAAS:SAAS00771250};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|PIRSR:PIRSR000388-3, ECO:0000256|SAAS:SAAS00771249};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|PIRSR:PIRSR000388-3, ECO:0000256|SAAS:SAAS00771262};
KW   Methyltransferase {ECO:0000313|EMBL:BAI29012.1};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|SAAS:SAAS00771245};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|SAAS:SAAS00771224, ECO:0000313|EMBL:BAI29012.1}.
FT   REGION       45     46       Alpha-ketoisovalerate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00156,
FT                                ECO:0000256|PIRSR:PIRSR000388-2}.
FT   ACT_SITE    181    181       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                1}.
FT   METAL        45     45       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                3}.
FT   METAL        84     84       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                3}.
FT   METAL       114    114       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                3}.
FT   BINDING      84     84       Alpha-ketoisovalerate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00156,
FT                                ECO:0000256|PIRSR:PIRSR000388-2}.
FT   BINDING     112    112       Alpha-ketoisovalerate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00156,
FT                                ECO:0000256|PIRSR:PIRSR000388-2}.
SQ   SEQUENCE   264 AA;  28179 MW;  0EB08E5780F74B5D CRC64;
     MKPTTIASLQ KCKQDKKRFA TITAYDYSFA KLFADEGLNV MLVGDSLGMT VQGHDSTLPV
     TVEDIAYHTA AVRRGAPNCL LLADLPFMAY ATPEQAFENA ATVMRAGANM VKIEGGEWLV
     ETVKMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRGDEAG DQLLSDALAL EAAGAQLLVL
     ECVPVELAKR ITEALAIPVI GIGAGNVTDG QILVMHDAFG ITGGHIPKFA KNFLAETGDI
     RAAVRQYMAE VESGVYPGEE HSFH
//

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