ID Q0K3J5_CUPNH Unreviewed; 365 AA.
AC Q0K3J5;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|ARBA:ARBA00018836};
DE EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153};
GN OrderedLocusNames=H16_B0632 {ECO:0000313|EMBL:CAJ95429.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ95429.1, ECO:0000313|Proteomes:UP000008210};
RN [1] {ECO:0000313|EMBL:CAJ95429.1, ECO:0000313|Proteomes:UP000008210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC 337 {ECO:0000313|Proteomes:UP000008210};
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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}.
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; AM260480; CAJ95429.1; -; Genomic_DNA.
DR RefSeq; WP_011616714.1; NZ_CP039288.1.
DR AlphaFoldDB; Q0K3J5; -.
DR STRING; 381666.H16_B0632; -.
DR GeneID; 57646521; -.
DR KEGG; reh:H16_B0632; -.
DR eggNOG; COG0108; Bacteria.
DR eggNOG; COG0807; Bacteria.
DR HOGENOM; CLU_020273_1_2_4; -.
DR OrthoDB; 8957175at2; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000008210; Chromosome 2.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 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 PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR PANTHER; PTHR21327:SF48; RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBBA; 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 Hydrolase {ECO:0000313|EMBL:CAJ95429.1};
KW Lyase {ECO:0000313|EMBL:CAJ95429.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008210};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 211..363
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
SQ SEQUENCE 365 AA; 38576 MW; 06BA78E75CD9E685 CRC64;
MSATTLPPMA DVLAALAAGQ RVLVIEDETD EATGCVLVAA ERASEADVNF MAAEARGLVC
MAITEARRAL LQLPPMAANH RQRERYTVSI EAASGVSTGI SAADRALTLR VAAAARAQPH
DLVQPGHIFP VVAQPDGVLR RAGFAEACSD LPALAGRVAA GAYAMLLDDD GDLLRGPALL
AFARHHGLPA VSISGLIHHR LLTESALCRT HSTELATPYG CFTVHAYHDA PVDALHLALV
LGQPDPQRPV LTRVQAVEMQ RDVLGFGAPA LPAWNLERSL ARIGAEGCGV LVLLDERESP
QQRLERLAAP AAATPAPAFA QRALGVGAQI LRDVGAHRLR LLSHPVPYRA VTGFDLEVTE
FVPPC
//
