ID M1M105_9PROT Unreviewed; 377 AA.
AC M1M105;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 ORFNames=ST1E_0570 {ECO:0000313|EMBL:AGF48979.1};
OS Candidatus Kinetoplastibacterium galatii TCC219.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208921 {ECO:0000313|EMBL:AGF48979.1, ECO:0000313|Proteomes:UP000011658};
RN [1] {ECO:0000313|EMBL:AGF48979.1, ECO:0000313|Proteomes:UP000011658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC219 {ECO:0000313|EMBL:AGF48979.1,
RC ECO:0000313|Proteomes:UP000011658};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(2013).
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; CP003806; AGF48979.1; -; Genomic_DNA.
DR AlphaFoldDB; M1M105; -.
DR STRING; 1208921.ST1E_0570; -.
DR KEGG; kga:ST1E_0570; -.
DR PATRIC; fig|1208921.3.peg.258; -.
DR eggNOG; COG0108; Bacteria.
DR HOGENOM; CLU_020273_1_2_4; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000011658; Chromosome.
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 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 NCBIfam; TIGR00506; ribB; 1.
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 Lyase {ECO:0000313|EMBL:AGF48979.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 242..374
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
SQ SEQUENCE 377 AA; 41944 MW; FC2B981CC9C0650B CRC64;
MVFINNISRS HFIVLLSNHT IYLNRKRDEM SLHISSTVEI IHELRSGRMI ILVDEEDREN
EGDLLIASEF VSADAINFMV KYGRGLVCLT LTNEYCNKLG LTMMSDRNRS RYGTNFTQSI
EAACGIDTGI STADRAHTIK VAISSDTTPD DIVQPGHIFP VRSVPGGVLV RAGHTEAGCD
LTSIAGLIPS SVICEILNDD GTMARLPDLI SFSQKHNIKI GTIYDLVQYR IKNESIISRI
GHRNIKTLQG TFKLVFYKDL FHDKSLHIAL ISGDPRETHE TLVYIYKSIS IVDIMDVNEK
PLSFNNALKN ISNSLSGVLV LINCQSIDNN NISEQINKIL NSEDANNVNI NSLDSYSCGI
SDQILRDIGV KNMKNII
//
