RIBB_PSEAE
ID RIBB_PSEAE Reviewed; 365 AA.
AC Q9HWX4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase;
DE Short=DHBP synthase;
DE EC=4.1.99.12;
GN Name=ribB; OrderedLocusNames=PA4054;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC and 3,4-dihydroxy-2-butanone 4-phosphate. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC manganese. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC cyclohydrolase II family. {ECO:0000305}.
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DR EMBL; AE004091; AAG07441.1; -; Genomic_DNA.
DR PIR; F83137; F83137.
DR RefSeq; NP_252743.1; NC_002516.2.
DR RefSeq; WP_003093313.1; NZ_QZGE01000013.1.
DR AlphaFoldDB; Q9HWX4; -.
DR SMR; Q9HWX4; -.
DR STRING; 287.DR97_3813; -.
DR PaxDb; Q9HWX4; -.
DR PRIDE; Q9HWX4; -.
DR EnsemblBacteria; AAG07441; AAG07441; PA4054.
DR GeneID; 878914; -.
DR KEGG; pae:PA4054; -.
DR PATRIC; fig|208964.12.peg.4245; -.
DR PseudoCAP; PA4054; -.
DR HOGENOM; CLU_020273_1_2_6; -.
DR InParanoid; Q9HWX4; -.
DR OMA; ECRGLIC; -.
DR PhylomeDB; Q9HWX4; -.
DR BioCyc; PAER208964:G1FZ6-4127-MON; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IBA:GO_Central.
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; IBA:GO_Central.
DR Gene3D; 3.40.50.10990; -; 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 Pfam; PF00926; DHBP_synthase; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR SUPFAM; SSF142695; SSF142695; 1.
DR SUPFAM; SSF55821; SSF55821; 1.
DR TIGRFAMs; TIGR00506; ribB; 1.
PE 3: Inferred from homology;
KW Lyase; Magnesium; Manganese; Metal-binding; Reference proteome;
KW Riboflavin biosynthesis.
FT CHAIN 1..365
FT /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT /id="PRO_0000151731"
FT REGION 1..201
FT /note="DHBP synthase"
FT REGION 202..365
FT /note="GTP cyclohydrolase II-like"
FT BINDING 27..28
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250"
FT BINDING 140..144
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250"
FT SITE 126
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 164
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 39438 MW; 9D2CE0B6366DAEB8 CRC64;
MALNTIDELI EDIRQGKMVI LMDDEDRENE GDLIMAAECV RTEDINFMVK HARGLVCMPM
TRERCERLGL PLMVQRNGSG FGTKFTVSIE AAEGVTTGIS AADRARTVQA AAAKNAVAAD
IVSPGHIFPL MAQPGGTLAR AGHTEAACDL ARMAGFEPSG VICEVMNDDG SMARRPELEA
FAAEHGIKIG TIADLIHYRL IHERTVERIA EQPLDSELGH FNLITYRDSV EGDVHLALTL
GKVCAEEPTL VRVHNMDPLR DLLQVNQPGR WSLRAAMTKV AEAGSGVVLL LGHQIGGDDL
LAHVREIASA PAPAPKATTT YSTVGAGSQI LRDLGVRKMR LLSAPMRFNA ISGFDLEVVE
YLPAE
