(data stored in ACNUC7421 zone)

SWISSPROT: PANB_ECODH

ID   PANB_ECODH              Reviewed;         264 AA.
AC   B1XCA9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 62.
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=ECDH10B_0114;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB01313.1; -; Genomic_DNA.
DR   RefSeq; WP_000805497.1; NC_010473.1.
DR   ProteinModelPortal; B1XCA9; -.
DR   SMR; B1XCA9; -.
DR   EnsemblBacteria; ACB01313; ACB01313; ECDH10B_0114.
DR   KEGG; ecd:ECDH10B_0114; -.
DR   eggNOG; ENOG4105CCG; Bacteria.
DR   eggNOG; COG0413; LUCA.
DR   HOGENOM; HOG000078427; -.
DR   KO; K00606; -.
DR   OMA; GHIGLMP; -.
DR   UniPathway; UPA00028; UER00003.
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; B1XCA9.
DR   SWISS-2DPAGE; B1XCA9.
KW   Cytoplasm; Magnesium; Metal-binding; Pantothenate biosynthesis;
KW   Transferase.
FT   CHAIN         1    264       3-methyl-2-oxobutanoate
FT                                hydroxymethyltransferase.
FT                                /FTId=PRO_1000096962.
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;  28237 MW;  0437D6BB9EBF817B CRC64;
     MKPTTISLLQ KYKQEKKRFA TITAYDYSFA KLFADEGLNV MLVGDSLGMT VQGHDSTLPV
     TVADIAYHTA AVRRGAPNCL LLADLPFMAY ATPEQAFENA ATVMRAGANM VKIEGGEWLV
     ETVQMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRGDEAG DQLLSDALAL EAAGAQLLVL
     ECVPVELAKR ITEALAIPVI GIGAGNVTDG QILVMHDAFG ITGGHIPKFA KNFLAETGDI
     RAAVRQYMAE VESGVYPGEE HSFH
//

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