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Entry: A0A160N2V2_9GAMM
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ID   A0A160N2V2_9GAMM        Unreviewed;       363 AA.
AC   A0A160N2V2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|ARBA:ARBA00018836, ECO:0000256|HAMAP-Rule:MF_00180};
DE            Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_00180};
DE            EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153, ECO:0000256|HAMAP-Rule:MF_00180};
GN   Name=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
GN   ORFNames=ATSB10_21880 {ECO:0000313|EMBL:AND69642.1};
OS   Dyella thiooxydans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=445710 {ECO:0000313|EMBL:AND69642.1, ECO:0000313|Proteomes:UP000077255};
RN   [1] {ECO:0000313|EMBL:AND69642.1, ECO:0000313|Proteomes:UP000077255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATSB10 {ECO:0000313|EMBL:AND69642.1,
RC   ECO:0000313|Proteomes:UP000077255};
RA   Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y.,
RA   Madhaiyan M.;
RT   "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans
RT   isolated from rhizosphere soil of sunflower (Helianthus annuus L.).";
RL   Submitted (FEB-2016) 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|ARBA:ARBA00002284, ECO:0000256|HAMAP-Rule:MF_00180}.
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|ARBA:ARBA00000141,
CC         ECO:0000256|HAMAP-Rule:MF_00180};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00180};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00180};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|HAMAP-Rule:MF_00180};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00180}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC       cyclohydrolase II family. {ECO:0000256|ARBA:ARBA00008976}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC       family. {ECO:0000256|ARBA:ARBA00005520}.
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DR   EMBL; CP014841; AND69642.1; -; Genomic_DNA.
DR   RefSeq; WP_063672688.1; NZ_CP014841.1.
DR   AlphaFoldDB; A0A160N2V2; -.
DR   STRING; 445710.ATSB10_21880; -.
DR   KEGG; dtx:ATSB10_21880; -.
DR   PATRIC; fig|445710.3.peg.2186; -.
DR   OrthoDB; 9793111at2; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000077255; 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   Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR   HAMAP; MF_00180; RibB; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR036144; RibA-like_sf.
DR   NCBIfam; TIGR00506; ribB; 1.
DR   PANTHER; PTHR21327:SF34; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   PIRSF; PIRSF001259; RibA; 1.
DR   SUPFAM; SSF142695; RibA-like; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000313|EMBL:AND69642.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00180};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00180};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00180}; Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077255};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW   Rule:MF_00180}; Transferase {ECO:0000256|ARBA:ARBA00022695}.
FT   DOMAIN          208..363
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   BINDING         27..28
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         28
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         28
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         32
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         140..144
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   SITE            126
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
FT   SITE            164
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00180"
SQ   SEQUENCE   363 AA;  39641 MW;  793332BDF8A3EA71 CRC64;
     MSFNTIPEIL EDIRAGRMVV ILDDEDRENE GDIVMAAQMV RPEDVNFMVR EARGLLCLTL
     TEQRTRQLGL KPMVSDNTSP YHTNFTVSIE AAEGVTTGIS AHDRARTIQV AVKSDAKPQD
     LSQPGHVFPL TAQPGGVLTR AGHTEAGCDL AALAGLEPAS VLIEILHEDG SMARRPELEV
     FAQKHGLKIG TIADLIRYRL ETEKTVERVH EEDVDTEFGA FRLIAYRDAI RRGLHFALVK
     GTVDDGAPVL SRVHVRNTLS DVLHLTRDDL GLTVTAALRR IGDEGRGVLL VLSGEDTPEA
     LLARLKGQPA TISAEDAQHN QWRQLGLGAQ IMADLGVHRL RVIGTPRKLV GLGGFGLEVV
     EYV
//
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