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Database: UniProt
Entry: G7W9M1_DESOD
LinkDB: G7W9M1_DESOD
Original site: G7W9M1_DESOD 
ID   G7W9M1_DESOD            Unreviewed;       215 AA.
AC   G7W9M1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843};
DE            Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843};
DE            EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843};
GN   Name=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
GN   OrderedLocusNames=Desor_4532 {ECO:0000313|EMBL:AET69938.1};
OS   Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / VKM
OS   B-1628 / Singapore I) (Desulfotomaculum orientis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768706 {ECO:0000313|EMBL:AET69938.1, ECO:0000313|Proteomes:UP000006346};
RN   [1] {ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Pester M.,
RA   Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA   Woyke T.;
RT   "Complete sequence of Desulfosporosinus orientis DSM 765.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AET69938.1, ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000256|ARBA:ARBA00002284, ECO:0000256|HAMAP-Rule:MF_00180,
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|HAMAP-Rule:MF_00180,
CC         ECO:0000256|RuleBase:RU003843};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00180,
CC         ECO:0000256|RuleBase:RU003843};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00180,
CC         ECO:0000256|RuleBase:RU003843};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|HAMAP-Rule:MF_00180,
CC       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|HAMAP-Rule:MF_00180,
CC       ECO:0000256|RuleBase:RU003843}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180,
CC       ECO:0000256|RuleBase:RU003843}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00180, ECO:0000256|RuleBase:RU003843}.
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DR   EMBL; CP003108; AET69938.1; -; Genomic_DNA.
DR   RefSeq; WP_014186745.1; NC_016584.1.
DR   AlphaFoldDB; G7W9M1; -.
DR   STRING; 768706.Desor_4532; -.
DR   KEGG; dor:Desor_4532; -.
DR   PATRIC; fig|768706.3.peg.4606; -.
DR   eggNOG; COG0108; Bacteria.
DR   HOGENOM; CLU_020273_3_0_9; -.
DR   OrthoDB; 9793111at2; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000006346; Chromosome.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.870.10; DHBP synthase; 1.
DR   HAMAP; MF_00180; RibB; 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:SF38; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00180};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00180};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00180}; Reference proteome {ECO:0000313|Proteomes:UP000006346};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW   Rule:MF_00180}.
FT   BINDING         37..38
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         42
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         150..154
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   SITE            136
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   SITE            174
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
SQ   SEQUENCE   215 AA;  23777 MW;  8B922089CCB4521D CRC64;
     MNQTLLKRFG TPFERVEKAL DSLRRGRGVL VTDDEQRENE GDIFFAAQYL TIEQMAMLIR
     EGSGIVCLCL PEEKVQELGL PMMVENNTSS YQTPFTVSIE AAIGVTTGVS AADRVTTVKA
     AIADKARPED LRRPGHMFPL KAKPLGVLER PGHTEANVDL MKLAGLKPYG VLCELTNPDG
     TMARLPEIVA FAEKNEMPVV TVDDIISYRK AREQK
//
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