ID A0A0D2AYG2_9PEZI Unreviewed; 390 AA.
AC A0A0D2AYG2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=PV09_04517 {ECO:0000313|EMBL:KIW04209.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW04209.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW04209.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW04209.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-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}.
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DR EMBL; KN847541; KIW04209.1; -; Genomic_DNA.
DR RefSeq; XP_016214078.1; XM_016357876.1.
DR AlphaFoldDB; A0A0D2AYG2; -.
DR STRING; 253628.A0A0D2AYG2; -.
DR GeneID; 27312490; -.
DR VEuPathDB; FungiDB:PV09_04517; -.
DR HOGENOM; CLU_036645_0_1_1; -.
DR InParanoid; A0A0D2AYG2; -.
DR OrthoDB; 1217184at2759; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000053259; 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 SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:KIW04209.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362100};
KW Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362100}.
FT REGION 51..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 41564 MW; FB589F7A927E1B27 CRC64;
MSRALTKSVE RASKTLVACR YSTSSLPVVH KLSAAAATAT RPQLTPIVHN GTQHQQLRHS
SHSPMGAPPA NPRKKVTLQT IQNMYKKSEP ITMLTAYDFP SAHVADHAGI DLILVGDSLA
MVSMGLEDTS EVTMEEMIFA SRAVARATKT AFIIGDLPMG SYEVNPEQAV RSSIEMIKKG
RSHSVKLEGG KEMAPTIKAI TDAGIPVLAH VGLTPQRQNA LGGFRVQGKT AASAIALLTD
ALAVQEAGAW GVVLEAIPPE IASIITAQLR IPTIGIGAGA GCSGQVLVQV DMLGNFPPGR
YMPKFAKKYG NVWGEAHRAI EQYKNEVKAR TYPSKEYTYE VKPDEVRKFE QLVAERYGSR
TRGQEQGLEG LGGTAVPEST PAAAAAAAAV
//
