(data stored in ACNUC7421 zone)

SWISSPROT: PANB_ECO57

ID   PANB_ECO57              Reviewed;         264 AA.
AC   Q8X929;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 101.
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=Z0145, ECs0138;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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: 5,10-methylenetetrahydrofolate + 3-methyl-2-
CC       oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate.
CC       {ECO:0000255|HAMAP-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; AE005174; AAG54438.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33561.1; -; Genomic_DNA.
DR   PIR; B85497; B85497.
DR   PIR; B90646; B90646.
DR   RefSeq; NP_308165.1; NC_002695.1.
DR   RefSeq; WP_000805473.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; Q8X929; -.
DR   SMR; Q8X929; -.
DR   STRING; 155864.Z0145; -.
DR   EnsemblBacteria; AAG54438; AAG54438; Z0145.
DR   EnsemblBacteria; BAB33561; BAB33561; BAB33561.
DR   GeneID; 913736; -.
DR   KEGG; ece:Z0145; -.
DR   KEGG; ecs:ECs0138; -.
DR   PATRIC; fig|386585.9.peg.238; -.
DR   eggNOG; ENOG4105CCG; Bacteria.
DR   eggNOG; COG0413; LUCA.
DR   HOGENOM; HOG000078427; -.
DR   KO; K00606; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06557; KPHMT-like; 1.
DR   HAMAP; MF_00156; PanB; 1.
DR   InterPro; IPR003700; Pantoate_hydroxy_MeTrfase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
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; Q8X929.
DR   SWISS-2DPAGE; Q8X929.
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Pantothenate biosynthesis; Transferase.
FT   CHAIN         1    264       3-methyl-2-oxobutanoate
FT                                hydroxymethyltransferase.
FT                                /FTId=PRO_0000184843.
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;  28310 MW;  D93FF23EBEF8D090 CRC64;
     MKPTTIASLQ KCKQEKKRFA TITAYDYSFA KLFAEEGLNV MLVGDSLGMT VQGHESTLPV
     TVEDIAYHTT AVRRGAPNCL LLADLPFMAY ATPEQAFENA ATVMRAGANM VKIEGGEWLV
     ETVKMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRGDEAS DRLLSDALAL EAAGAQLLVL
     ECVPVELAKR ITEALAIPVI GIGAGNVTDG QILVMHDAFG ITGGHIPKFA KNFLAETGDI
     RAAVRQYMAE VESGVYPGEE HSFH
//

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