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Database: UniProt
Entry: A0A163M8G7_DIDRA
LinkDB: A0A163M8G7_DIDRA
Original site: A0A163M8G7_DIDRA 
ID   A0A163M8G7_DIDRA        Unreviewed;       270 AA.
AC   A0A163M8G7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=EKO05_0005976 {ECO:0000313|EMBL:UPX15532.1}, EKO05_004790
GN   {ECO:0000313|EMBL:KAF9708713.1}, ST47_g343
GN   {ECO:0000313|EMBL:KZM28492.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM28492.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM28492.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM28492.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
RN   [2] {ECO:0000313|EMBL:KAF9708713.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9708713.1};
RA   Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF9708713.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9708713.1};
RX   PubMed=32345704; DOI=10.1534/g3.120.401265;
RA   Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA   Debler J.W., Oliver R.P., Lee R.C.;
RT   "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT   ArME14.";
RL   G3 (Bethesda) 10:2131-2140(2020).
RN   [4] {ECO:0000313|EMBL:KAF9708713.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9708713.1};
RA   Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA   Debler J.W., Oliver R.P., Lee R.C.;
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:UPX15532.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:UPX15532.1};
RA   Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL   Submitted (MAR-2022) 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}.
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DR   EMBL; RYYQ01000008; KAF9708713.1; -; Genomic_DNA.
DR   EMBL; JYNV01000015; KZM28492.1; -; Genomic_DNA.
DR   EMBL; CP095296; UPX15532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163M8G7; -.
DR   STRING; 5454.A0A163M8G7; -.
DR   OrthoDB; 5489599at2759; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   Proteomes; UP000617380; Chromosome 9.
DR   Proteomes; UP000617380; 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:UP000076837};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW   ECO:0000256|RuleBase:RU003843}.
SQ   SEQUENCE   270 AA;  28621 MW;  809D8ED24CF3D6EF CRC64;
     MATMPAETNG IAVNGLAVNG LAANELAASR PAEGIIHPTH ELSNPPPADS AFDSIPDVVA
     AFANDEFVIV LDSPDRENEG DLIIAAESLT PEKAAFMIRY SSGYMCAPLP VSRAAALHLP
     QMVADNADPN RTAYAISIDA NDDSVSTGIS AHDRSLTCRL LADPNAKASH FRRPGHILPL
     QARDGGVRVR RGHTEAAVDL CRLAGKQPVG VICEMINDGE SVDGKPALLG SGMMRTDECL
     AFGKKWGIKV CTIEDMVTYI EQNEGKLPVP
//
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