ID A0A1B9G522_9TREE Unreviewed; 1053 AA.
AC A0A1B9G522;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=I302_03811 {ECO:0000313|EMBL:OCF26134.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF26134.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF26134.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF26134.1,
RC ECO:0000313|Proteomes:UP000092730};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-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; KI894020; OCF26134.1; -; Genomic_DNA.
DR RefSeq; XP_019047204.1; XM_019190456.1.
DR AlphaFoldDB; A0A1B9G522; -.
DR STRING; 1296100.A0A1B9G522; -.
DR GeneID; 30208210; -.
DR VEuPathDB; FungiDB:I302_03811; -.
DR OrthoDB; 1217184at2759; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000092730; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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 GO; GO:0006412; P:translation; IEA:InterPro.
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 InterPro; IPR015324; Ribosomal_Rsm22-like.
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 Pfam; PF09243; Rsm22; 2.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:OCF26134.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362100};
KW Reference proteome {ECO:0000313|Proteomes:UP000092730};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362100};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT REGION 57..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 115272 MW; 0FABD4354D84C2B5 CRC64;
MLPRPARLIH QQKTLLCRTS RKFTSTSIVH PQGQVVHHIP STSIDESFND LIREDDMGMG
MGPSRSIKPG KSKGKGRMHD LEVVDHDHSS PSGNLDFHKF GVIQHEPPSH QYRLGDDEGE
GEYLHERREE RRSPAAVLGS KRIGVVVLPE ALKNGIQRQI DLLDNPRTLR QSYLDLPSSP
SQKTREEKVD HRSSKPRKTV ESELAKAAGI LPGEYGVIRN ILEEMDRRLG TGWLERVTQE
GEITEVVEFS GGLGAGLWAT VETLKDTSSA ENLRIQLVHS SRHGLDLAKK ITEDIPEQAA
EILYNRKHHS YPSPPALALS TFLLSTLPTQ PSQQSHLLQL LSLNSPYIIL VDRSTPAGWQ
AISHARSFLL DQSTPENPLH VIAPCPHDGV CPLASTDDKC SFSQRLQRPS FVRKTKHSSR
GEEDTGYCYV VLARGERPVS GLSDEVQLQG MLKSALGRMG GVGKEEAEKA RLKKAGRSVL
REIEGHEGIL EVVNLPEYDG SHHQHVPASS NAADKEDLQK VLTNEAYSWP RLVAPPMKRS
GHVTMDACCP DGNIQRLTFS KSHSKQGYHD ARKSSWGDIF PHTPKATPVV RTRGVRRLSK
PVNDDQVLHD LTAALREEGS ELDNSVLEDD LVELEKLGIN IPRAEVVQEA EGDYPVSGNK
SNSGENGPFG SAGQRRHFAS MSVRRPIVQA VGLSPSLQSR HMSARPPPRA KVTLSTLEKL
SMAKTPITVL TAYDFPTALL SESCGVDMTL VGDSLSQVCL GHTSTTEITL DEIIHHAKAV
TKGAKTPFVF ADLPFGSFEV SLEDGVRNVI RLVKESGIDG VKIEGGLEII PLVKRLSEIG
IPVMPHLGLQ PQRATYLSGY LVQGRTSQSA YEICNTAKAM QDAGAFAVLL EAIPDKVARR
ITEDLDIITI GIGAGNGTNG QVLVITDVLG TYAEEPQEEI DIVEPATQLA LNDVSIPSTP
SVASDLTTTT SATNVNGAPE KGGDDIAMLE PPKKSLNSPK FVRHFGNIGE LSRRVIKSYL
KAVREGDFPN ASESYGMKKD QWEGFLRLLE GNK
//