(data stored in ACNUC7421 zone)

HOGENOM: DICZE_1_PE1007

ID   DICZE_1_PE1007                       STANDARD;      PRT;   264 AA.
AC   DICZE_1_PE1007; C6CNH9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase; EC=2.1.2
DE   11;AltName: Full=Ketopantoate hydroxymethyltransferase; (DICZE_1.PE1007).
GN   Name=panB; OrderedLocusNames=Dd1591_1028;
OS   DICKEYA ZEAE ECH1591.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Dickeya.
OX   NCBI_TaxID=561229;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DICZE_1.PE1007.
CC       Dickeya zeae Ech1591 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6CNH9_DICZE
CC   -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl
CC       group from 5,10-methylenetetrahydrofolate is tranferred onto
CC       alpha-ketoisovalerate to form ketopantoate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + 3-methyl-2-
CC       oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC   -!- SUBUNIT: Homodecamer; pentamer of dimers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the panB family.
CC   -!- GENE_FAMILY: HOG000078427 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6CNH9; -.
DR   EMBL; CP001655; ACT05901.1; -; Genomic_DNA.
DR   RefSeq; YP_003003380.1; NC_012912.1.
DR   STRING; C6CNH9; -.
DR   GeneID; 8120301; -.
DR   GenomeReviews; CP001655_GR; Dd1591_1028.
DR   KEGG; dze:Dd1591_1028; -.
DR   OMA; SCAAAVK; -.
DR   ProtClustDB; CLSK2549600; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:HAMAP.
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:HAMAP.
DR   HAMAP; MF_00156; PanB; 1; -.
DR   InterPro; IPR003700; Pantoate_hydroxy_MeTrfase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   PANTHER; PTHR20881; Pantoate_transf; 1.
DR   Pfam; PF02548; Pantoate_transf; 1.
DR   PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1.
DR   SUPFAM; SSF51621; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   TIGRFAMs; TIGR00222; PanB; 1.
DR   HOGENOMDNA; DICZE_1.PE1007; -.
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Methyltransferase; Pantothenate biosynthesis; Transferase.
SQ   SEQUENCE   264 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKATTISHLR QWKQEQKKFA TLTAYDASFA QLFYEQGIRV MLVGDSLGMP VQGHDSTLPV
     TIDDMVYHTR CVRRGAPHCL LLSDLPFMGA ATPEQACQQA AALMRAGANM VKIEGGSWLV
     PTVRMLTERA VPVCGHLGLT PQSVNIFGGY KVQGRDEAAA SQLLEDALAL EQAGAQLLVL
     ECVPVSLAQR VTEALSIPVI GIGAGNVTDG QILVMHDALG VTGGHTPKFA RNFMAEAADI
     RAAVRLYVQE VEQGTFPDEK YSFA
//

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