GenomeNet

Database: UniProt
Entry: A0A3M7BJY2_HORWE
LinkDB: A0A3M7BJY2_HORWE
Original site: A0A3M7BJY2_HORWE 
ID   A0A3M7BJY2_HORWE        Unreviewed;       720 AA.
AC   A0A3M7BJY2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   28-JAN-2026, 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=D0866_01689 {ECO:0000313|EMBL:RMY39810.1};
OS   Hortaea werneckii (Black yeast) (Cladosporium werneckii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=91943 {ECO:0000313|EMBL:RMY39810.1, ECO:0000313|Proteomes:UP000276864};
RN   [1] {ECO:0000313|EMBL:RMY39810.1, ECO:0000313|Proteomes:UP000276864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-6651 {ECO:0000313|EMBL:RMY39810.1,
RC   ECO:0000313|Proteomes:UP000276864};
RX   PubMed=29764372; DOI=10.1186/s12864-018-4751-5;
RA   Gostincar C., Stajich J.E., Zupancic J., Zalar P., Gunde-Cimerman N.;
RT   "Genomic evidence for intraspecific hybridization in a clonal and extremely
RT   halotolerant yeast.";
RL   BMC Genomics 19:364-364(2018).
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 = 2-dehydropantoate + (6S)-5,6,7,8-
CC         tetrahydrofolate; 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:ARBA00049172,
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMY39810.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QWIM01000100; RMY39810.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M7BJY2; -.
DR   VEuPathDB; FungiDB:BTJ68_10693; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000276864; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-ARBA.
DR   GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06557; KPHMT-like; 1.
DR   FunFam; 3.20.20.60:FF:000003; 3-methyl-2-oxobutanoate hydroxymethyltransferase; 1.
DR   FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR   Gene3D; 6.10.250.3410; DBF zinc finger; 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; IPR013939; Regulatory_Dfp1/Him1.
DR   InterPro; IPR006572; Znf_DBF.
DR   InterPro; IPR038545; Znf_DBF_sf.
DR   NCBIfam; TIGR00222; panB; 1.
DR   NCBIfam; NF001452; PRK00311.1; 1.
DR   PANTHER; PTHR20881; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR20881:SF0; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1.
DR   Pfam; PF08630; Dfp1_Him1_M; 1.
DR   Pfam; PF02548; Pantoate_transf; 1.
DR   Pfam; PF07535; zf-DBF; 1.
DR   SMART; SM00586; ZnF_DBF; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362100};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362100};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          342..391
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..188
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..339
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..430
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   720 AA;  78669 MW;  740C07E745769C6A CRC64;
     MLSTILDTDA GDQGTGHDTR SHVTNGRTTS KAGRNADLEQ LLRNEKLTGP TDRDMSVAGQ
     DMATFRGCYL YVHDMDEKTK PVMVRDYPKP GARETGKWPQ FRLSGPGRCP FVEDPSYQKR
     QAQEASAAKA QEELTTQRRL RAASAQETAA SRQTQDRPLT ERHANLRRSP RKIDAPAKPL
     DPPKPPPANK QISAENVPLF GSTQQSLRGL PRMIGGEPVA SGVQASNVTS AIRSQYVSSA
     AISSTAPGAN HRVGDSKEVS ALKRKVLERG NSINSNNSVL SSHMNDMRAA LNGDNEPPPR
     AAKRKAQETL GVVNEDEEDY DRGKRPSKQR KPAPRRRKPV ERDPKPGYCE NCRDKFDDFD
     EHIQSRKHRK FAMTQDNWKE LDELLGKLKR PHKVEQHVAR LANGTHKAVS YPSLSNSSIR
     HSSHSPLGSS APTRKKVTIP TLNAMHKRGE PITMLTAHDF PSAHVADQAG MDMVLVGDSL
     AMVSMGLEDT SEVLLEEMIL HCRSVARGAK SAFIVGDLPM GTYEVSPEQA LQSAIRMVKE
     GRVHGIKLEG GAEMAPAIEK ITTAGIPVLA HVGLTPQRQN ALGGFRVQGK TTAGALKFMA
     DAIAVQEAGA FAVVVEAVPA EVAGLVTKKL RIPTIGIGAG NGCSGQVLVQ VDMSGNFPPG
     RFLPKFVKKF GDVWGEAQRA IQTYRTEVKD RSYPAPEHTY PIPKEEYAEF ERMIEASNRA
//
DBGET integrated database retrieval system