ID A0A0W7VR62_9HYPO Unreviewed; 232 AA.
AC A0A0W7VR62;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|RuleBase:RU003843};
DE Short=DHBP synthase {ECO:0000256|RuleBase:RU003843};
DE EC=4.1.99.12 {ECO:0000256|RuleBase:RU003843};
GN ORFNames=TGAM01_v202623 {ECO:0000313|EMBL:PON28776.1}, TGAMA5MH_07273
GN {ECO:0000313|EMBL:PNP40833.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PON28776.1, ECO:0000313|Proteomes:UP000054821};
RN [1] {ECO:0000313|EMBL:PON28776.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON28776.1,
RC ECO:0000313|Proteomes:UP000054821};
RX PubMed=26893428;
RA Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL Genome Announc. 4:e01747-15(2016).
RN [2] {ECO:0000313|EMBL:PNP40833.1, ECO:0000313|Proteomes:UP000236546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5MH {ECO:0000313|EMBL:PNP40833.1,
RC ECO:0000313|Proteomes:UP000236546};
RA Gardiner D., Kazan K., Vos C., Harvey P.;
RT "Genomes of Trichoderma spp. with biocontrol activity.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PON28776.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T6085 {ECO:0000313|EMBL:PON28776.1};
RA Baroncelli R.;
RT "Trichoderma gamsii strain T6085, whole genome shotgun sequencing
RT project.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC and 3,4-dihydroxy-2-butanone 4-phosphate.
CC {ECO:0000256|RuleBase:RU003843}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate +
CC formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830;
CC EC=4.1.99.12; Evidence={ECO:0000256|RuleBase:RU003843};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU003843};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU003843};
CC Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC manganese. {ECO:0000256|RuleBase:RU003843};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004904, ECO:0000256|RuleBase:RU003843}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003843}.
CC -!- SIMILARITY: Belongs to the DHBP synthase family.
CC {ECO:0000256|RuleBase:RU003843}.
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:PON28776.1}.
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DR EMBL; MTYH01000060; PNP40833.1; -; Genomic_DNA.
DR EMBL; JPDN02000006; PON28776.1; -; Genomic_DNA.
DR RefSeq; XP_018661790.1; XM_018805066.1.
DR AlphaFoldDB; A0A0W7VR62; -.
DR STRING; 398673.A0A0W7VR62; -.
DR GeneID; 29985149; -.
DR OrthoDB; 5489599at2759; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000054821; Unassembled WGS sequence.
DR Proteomes; UP000236546; Unassembled WGS sequence.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.870.10; DHBP synthase; 1.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR000422; DHBP_synthase_RibB.
DR NCBIfam; TIGR00506; ribB; 1.
DR PANTHER; PTHR21327:SF18; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR Pfam; PF00926; DHBP_synthase; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU003843};
KW Magnesium {ECO:0000256|RuleBase:RU003843};
KW Manganese {ECO:0000256|RuleBase:RU003843};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003843};
KW Reference proteome {ECO:0000313|Proteomes:UP000054821};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW ECO:0000256|RuleBase:RU003843}.
SQ SEQUENCE 232 AA; 24644 MW; 998E81E45834F1C5 CRC64;
MPSTTLDQSL FDSIPDSIEA FRRGEFLVVL DDPSRENEAD LIIAAEAVTT EQMAWMVRHS
SGYICAPITH ARADALGLPP MVQRSEDPRG TAYTVSVDAA DPSVTTGISA HDRALVCRVL
ADPASSASSL RRPGHVLPLR AAPGGVRARN GHTEAATEFC RLAGKAEAGV ICEIVDDGEV
VPGRAVHNNP GMLRGEACIA FARKWGLKVC TIADLVTYVE KTEGKLPVNG SN
//
