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
//