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Database: UniProt
Entry: E9DYP3_METAQ
LinkDB: E9DYP3_METAQ
Original site: E9DYP3_METAQ 
ID   E9DYP3_METAQ            Unreviewed;       299 AA.
AC   E9DYP3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000256|ARBA:ARBA00012618, ECO:0000256|RuleBase:RU362100};
DE            EC=2.1.2.11 {ECO:0000256|ARBA:ARBA00012618, ECO:0000256|RuleBase:RU362100};
GN   ORFNames=MAC_02740 {ECO:0000313|EMBL:EFY91313.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY91313.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY91313.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
CC   -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl
CC       group from 5,10-methylenetetrahydrofolate is transferred onto alpha-
CC       ketoisovalerate to form ketopantoate. {ECO:0000256|RuleBase:RU362100}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-
CC         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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000344,
CC         ECO:0000256|RuleBase:RU362100};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005033, ECO:0000256|RuleBase:RU362100}.
CC   -!- SIMILARITY: Belongs to the PanB family. {ECO:0000256|ARBA:ARBA00008676,
CC       ECO:0000256|RuleBase:RU362100}.
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DR   EMBL; GL698483; EFY91313.1; -; Genomic_DNA.
DR   RefSeq; XP_007809080.1; XM_007810889.1.
DR   AlphaFoldDB; E9DYP3; -.
DR   STRING; 655827.E9DYP3; -.
DR   GeneID; 19247051; -.
DR   KEGG; maw:MAC_02740; -.
DR   eggNOG; KOG2949; Eukaryota.
DR   HOGENOM; CLU_036645_0_1_1; -.
DR   InParanoid; E9DYP3; -.
DR   OMA; VLVWTDM; -.
DR   OrthoDB; 1217184at2759; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000002499; 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-UniPathway.
DR   CDD; cd06557; KPHMT-like; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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   NCBIfam; TIGR00222; panB; 1.
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   PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:EFY91313.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362100};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362100}.
SQ   SEQUENCE   299 AA;  31791 MW;  BA34D92CF61A2081 CRC64;
     MGAAPANQRK KVTLGTLRSL HRKGEPITMM TAHDFPSAHV ADHAGMDVIL VGDSLAMVSL
     GMEDTSEVLV EEMLLHCRSV ARATKSAFTV GDLPMGSYEI APEQALATAI RFIKEGRVQG
     IKLEGGKEMV PTIEKITTAG IPVLGHVGLT PQRQNSLGGF RVQGKTSSSA MSLLEDALGV
     QAAGCFAVVL EAVPAEVAAL VTQKLSIPTI GIGAGAGCSG QVLVQTDMTG NFPPGRYLPK
     FVKKYGDVWG EAKKAIEAYR DDVKAREYPA KEHTYPMPQE EFAAFEKGVK ALENEANQA
//
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