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Database: UniProt
Entry: A0A0G2DSU5_9EURO
LinkDB: A0A0G2DSU5_9EURO
Original site: A0A0G2DSU5_9EURO 
ID   A0A0G2DSU5_9EURO        Unreviewed;       274 AA.
AC   A0A0G2DSU5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 23.
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=UCRPC4_g06874 {ECO:0000313|EMBL:KKY14047.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY14047.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY14047.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY14047.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY14047.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY14047.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KKY14047.1}.
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DR   EMBL; LCWF01000240; KKY14047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2DSU5; -.
DR   OrthoDB; 1217184at2759; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000053317; 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:KKY14047.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362100};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362100}.
FT   REGION          239..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   274 AA;  29512 MW;  FB388486E4778A36 CRC64;
     MLTAHDFPSA SVADAAGMEM ILVGDSLAMV ALGMSDTSEV TLDEMIVHCR SVSRATQSAF
     TIGDLPMGSY EVSLEQALAS AIRIIKEGRM QGVKLEGGKE MAPTIQKITT AGIPVVAHIG
     LTPQRQNALG GFRVQGKSKA SAFRLLEDAL SVQSAGAFMV VLEAVPPEVA QWVTSKLSIP
     TIGIGAGEGC SGQVLVQVDM SGNYPPGRFL PKFVKRYGDV WSESFKAIRQ YRDEVKSRSY
     PAKEHTYPMS KEGLANFQEA VSQISRDDRN EEPQ
//
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