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Entry: A0A1B9G522_9TREE
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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
//
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