ID W6QH74_PENRF Unreviewed; 359 AA.
AC W6QH74;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 13-SEP-2023, entry version 29.
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=PROQFM164_S04g000187 {ECO:0000313|EMBL:CDM35306.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM35306.1};
RN [1] {ECO:0000313|EMBL:CDM35306.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM35306.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792018; CDM35306.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QH74; -.
DR STRING; 1365484.W6QH74; -.
DR OMA; VLVWTDM; -.
DR OrthoDB; 1217184at2759; -.
DR UniPathway; UPA00028; UER00003.
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:CDM35306.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362100};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362100}.
SQ SEQUENCE 359 AA; 38998 MW; 4DBA31DD78C166BD CRC64;
MAAPGSVLQR TALISSSMLR TRVISATRTQ ATHTLRTGRC SALSSHIPTH PLFQTRHSSY
SAPTLRENEK ARKKVTIQTL QNMHKKGEPI TMLTAHDFPS AHVADASGMD MVLVGDSLGM
VALGLENTTE VVMEEMILHC RSVARATKAA FIVGDLPMGS YEVCAEQAIE SSLRLVKEGR
VHAVKLEGSQ ELAPTIKRIT QAGVPVVGHV GLTPQRQNAL GGFRVQGKTA VSAVRMLHDA
LAMQEAGAFM LVLEAIPSEV ASIITQKLRI PTIGIGAGNG CSGQVLVQVD MTGNFQPGRF
VPKFVKQYAD VWDEASRGIS LYRDEVKSRA FPSEEYTYPI AKDELAEFQK TVDEVFRES
//
