(data stored in ACNUC29543 zone)

SWISSPROT: PANB_SYNR3

ID   PANB_SYNR3              Reviewed;         270 AA.
AC   A5GRJ3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 78.
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=SynRCC307_0599;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT978603; CAK27502.1; -; Genomic_DNA.
DR   RefSeq; WP_011935017.1; NC_009482.1.
DR   SMR; A5GRJ3; -.
DR   STRING; 316278.SynRCC307_0599; -.
DR   PRIDE; A5GRJ3; -.
DR   EnsemblBacteria; CAK27502; CAK27502; SynRCC307_0599.
DR   KEGG; syr:SynRCC307_0599; -.
DR   eggNOG; ENOG4105CCG; Bacteria.
DR   eggNOG; COG0413; LUCA.
DR   HOGENOM; HOG000078427; -.
DR   KO; K00606; -.
DR   OMA; GHIGLMP; -.
DR   OrthoDB; 916845at2; -.
DR   BioCyc; SSP316278:G1GJL-585-MONOMER; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000001115; 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; A5GRJ3.
DR   SWISS-2DPAGE; A5GRJ3.
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Pantothenate biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    270       3-methyl-2-oxobutanoate
FT                                hydroxymethyltransferase.
FT                                /FTId=PRO_1000071533.
FT   REGION       48     49       Alpha-ketoisovalerate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00156}.
FT   ACT_SITE    186    186       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   METAL        48     48       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   METAL        87     87       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   METAL       119    119       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   BINDING      87     87       Alpha-ketoisovalerate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00156}.
FT   BINDING     117    117       Alpha-ketoisovalerate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00156}.
SQ   SEQUENCE   270 AA;  28789 MW;  2AF71F3A052FDA68 CRC64;
     MSLTPRQLGE QLRQRKQRRQ PIAVLTAWDA LSASWAEAAG VDLVLVGDSL AMVALGHATT
     LPVTLEAMVQ HTAAVERGLR HTPIVSDLPF LSYQCGPDQA VAAAGRFLKE TGCAGVKLEG
     GEPETIAVID RLVRSGIPVM GHLGLTPQSV HQLGYRRQAT DPVAQERLWQ RALELQQTGC
     FALVLEHVPA ELATRLSAEL SVPVIGIGAG EGCDGQVRVS ADLLGLTPQQ PPFSPALLDG
     RELFSQALRQ WVQGVQSAPV PPANHSAPHC
//

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