ID K9NS60_9PSED Unreviewed; 363 AA.
AC K9NS60;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=ribBA3 {ECO:0000313|EMBL:AFY22018.1};
GN Synonyms=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
GN ORFNames=PputUW4_04828 {ECO:0000313|EMBL:AFY22018.1};
OS Pseudomonas sp. UW4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1207075 {ECO:0000313|EMBL:AFY22018.1, ECO:0000313|Proteomes:UP000010397};
RN [1] {ECO:0000313|EMBL:AFY22018.1, ECO:0000313|Proteomes:UP000010397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UW4 {ECO:0000313|EMBL:AFY22018.1,
RC ECO:0000313|Proteomes:UP000010397};
RX PubMed=23516524;
RA Duan J., Jiang W., Cheng Z., Heikkila J.J., Glick B.R.;
RT "The Complete Genome Sequence of the Plant Growth-Promoting Bacterium
RT Pseudomonas sp. UW4.";
RL PLoS ONE 8:E58640-E58640(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, 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 -!- 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, 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; CP003880; AFY22018.1; -; Genomic_DNA.
DR RefSeq; WP_007970163.1; NC_019670.1.
DR AlphaFoldDB; K9NS60; -.
DR STRING; 1207075.PputUW4_04828; -.
DR KEGG; ppuu:PputUW4_04828; -.
DR PATRIC; fig|1207075.3.peg.4918; -.
DR eggNOG; COG0108; Bacteria.
DR eggNOG; COG0807; Bacteria.
DR HOGENOM; CLU_020273_1_2_6; -.
DR OrthoDB; 9793111at2; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000010397; Chromosome.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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:AFY22018.1};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000313|EMBL:AFY22018.1};
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};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW Rule:MF_00180}.
FT DOMAIN 208..361
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; 39387 MW; 71728EC681BA9188 CRC64;
MALNSIEELV EDIRQGKMVI LMDDEDRENE GDLIMAAECC KPEHINFMAK HARGLICMPM
SRERCELLKL PLMAPRNGSG FGTKFTVSIE AATGVTTGIS AADRARTVQA AAARDAKAED
IVSPGHIFPL MAQAGGTLAR AGHTEAACDL ARMAGFEPSG VICEVMNDDG TMSRRAELEA
FAAEHDIKIG TIADLIHYRM IHERTVQRIA EQPLDSELGQ FNLVTYRDSV EGDVHMALTL
GNVCAEEPTL VRVHNMDPLR DLLMVKQPGR WSLRAAMSAV AEAGSGVVLL LGHPLDGDVL
LAHIRETADH AAVKKPTTYS TVGAGSQILR DLGVRKMRLM SAPMKFNAIS GFDLEVVEYV
PSE
//
