ID W6MWN0_9ASCO Unreviewed; 326 AA.
AC W6MWN0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 13-SEP-2023, entry version 24.
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=KUCA_T00003654001 {ECO:0000313|EMBL:CDK27675.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK27675.1};
RN [1] {ECO:0000313|EMBL:CDK27675.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK27675.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK27675.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK27675.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) 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; HG793128; CDK27675.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MWN0; -.
DR STRING; 1382522.W6MWN0; -.
DR HOGENOM; CLU_036645_0_1_1; -.
DR OrthoDB; 1217184at2759; -.
DR UniPathway; UPA00028; UER00003.
DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-EC.
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 SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362100};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362100}.
SQ SEQUENCE 326 AA; 35312 MW; DDB51BB2EF946446 CRC64;
MASKTVARAC FLGRRSFSGC LRAQSTGAQS SPYSAPETAI AKHKPSTLKE IYAKYKNGTP
ISVVTAHDYI SGKWADAAPS CDAVLIGDSL AMVAVGYPTT LEIPFDEFYY HCASVCRAVK
SKYIIADLPY GSFESSVEKC IESSMRLMKL GKICSIKIEG AYEHEESISR LIKLGIPVTG
HIGLKPQRFN GLEGFRVQGK TVDSALQILK EALFLQETGI SLLVLEGIPH EIASYITTKL
SIPTIGIGAG NGTSGQVLVQ ADLLGMHTGR GPKFVKRYED LYGKGVAAIE KYAQEVSASA
FPDNAVHTYP MKTKVLEEFL EQAEKI
//
