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Database: UniProt
Entry: W2RQA0_9EURO
LinkDB: W2RQA0_9EURO
Original site: W2RQA0_9EURO 
ID   W2RQA0_9EURO            Unreviewed;       314 AA.
AC   W2RQA0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   13-SEP-2023, entry version 27.
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=HMPREF1541_06694 {ECO:0000313|EMBL:ETN38657.1};
OS   Cyphellophora europaea CBS 101466.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX   NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN38657.1, ECO:0000313|Proteomes:UP000030752};
RN   [1] {ECO:0000313|EMBL:ETN38657.1, ECO:0000313|Proteomes:UP000030752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN38657.1,
RC   ECO:0000313|Proteomes:UP000030752};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phialophora europaea CBS 101466.";
RL   Submitted (MAR-2013) 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}.
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DR   EMBL; KB822722; ETN38657.1; -; Genomic_DNA.
DR   RefSeq; XP_008719246.1; XM_008721024.1.
DR   AlphaFoldDB; W2RQA0; -.
DR   STRING; 1220924.W2RQA0; -.
DR   GeneID; 19974033; -.
DR   VEuPathDB; FungiDB:HMPREF1541_06694; -.
DR   eggNOG; KOG2949; Eukaryota.
DR   HOGENOM; CLU_036645_0_1_1; -.
DR   InParanoid; W2RQA0; -.
DR   OrthoDB; 1217184at2759; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000030752; 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   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:ETN38657.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362100};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362100}.
SQ   SEQUENCE   314 AA;  33212 MW;  F4CE52F0800776B9 CRC64;
     MAAVKKFYAA CEAGPAVCLT AWDYPTGLLA KDAGMDLILI GDSLAITALG LPSTTSITLD
     ELIYHARAVS RAAKAGPFLL GDLPLGSYEI TPEQAVASAL RLVKEGDVDG VKLEGGKEMA
     PQVAAITKAG VPVVGHIGLT PQRALATLHT EGIEGLSGAG EARLSFGSTL DSAEMVLDDA
     LALQKAGAVA IVMEAVAAPT ARMITEVLKV PTIGIGCGGG TSAQIAVQSE VLGYQRTFLQ
     RWHTKYAEVG DVSLQALRKY KEETRGKQFP TEQQGYVMKN GEEKVLVDLK KRAKEMSLYE
     NMGRERRGSK SSSY
//
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