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Database: UniProt
Entry: A0A0C1XRX8_9ACTN
LinkDB: A0A0C1XRX8_9ACTN
Original site: A0A0C1XRX8_9ACTN 
ID   A0A0C1XRX8_9ACTN        Unreviewed;       282 AA.
AC   A0A0C1XRX8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000256|ARBA:ARBA00012618};
DE            EC=2.1.2.11 {ECO:0000256|ARBA:ARBA00012618};
GN   ORFNames=QR77_33625 {ECO:0000313|EMBL:KIF77458.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF77458.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF77458.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF77458.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT   150.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homodecamer; pentamer of dimers.
CC       {ECO:0000256|ARBA:ARBA00011424}.
CC   -!- SIMILARITY: Belongs to the PanB family.
CC       {ECO:0000256|ARBA:ARBA00008676}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIF77458.1}.
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DR   EMBL; JTHL01000001; KIF77458.1; -; Genomic_DNA.
DR   RefSeq; WP_040025815.1; NZ_JTHL01000001.1.
DR   AlphaFoldDB; A0A0C1XRX8; -.
DR   STRING; 1576605.QR77_33625; -.
DR   OrthoDB; 7822473at2; -.
DR   Proteomes; UP000031584; Unassembled WGS sequence.
DR   GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR20881:SF0; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1.
DR   Pfam; PF02548; Pantoate_transf; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:KIF77458.1};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031584};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KIF77458.1}.
SQ   SEQUENCE   282 AA;  29766 MW;  AE77716FAAE18570 CRC64;
     MGNTSDKVSL RSLQRMKDEG TKIVGVVAWD YQIARIVDRA GVDIVSVGDT VGMNLWGQSN
     PFEVTMEQML VVTQAVRRGV RRALVSADFP FGPLQEGTDS AVRAAVRFVK EAGVDMVKLD
     GASDFPDAVT AVTRAGIPVF AQFGITPQTA LRYGVEYNAI PSAADQIPEA MKDALVEEAK
     RLEEAGAALL NFTNSGPVVG EAVARAVSIP VVGGFGGGPW LDGRMRMAHA AIGYSAAAID
     NPPDTYANVA RITLDAMTAY ADDVRAARQI PGGIPVPPRP AP
//
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