ID A7MAT6_PHOPO Unreviewed; 154 AA.
AC A7MAT6;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|ARBA:ARBA00018836, ECO:0000256|RuleBase:RU003843};
DE Short=DHBP synthase {ECO:0000256|RuleBase:RU003843};
DE EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153, ECO:0000256|RuleBase:RU003843};
DE Flags: Fragment;
GN Name=ribB {ECO:0000313|EMBL:ABU50701.1};
OS Photobacterium phosphoreum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=659 {ECO:0000313|EMBL:ABU50701.1};
RN [1] {ECO:0000313|EMBL:ABU50701.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FS-1.1 {ECO:0000313|EMBL:ABU50701.1};
RX PubMed=16156737; DOI=10.1111/j.1462-2920.2005.00859.x;
RA Ast J.C., Dunlap P.V.;
RT "Phylogenetic resolution and habitat specificity of members of the
RT Photobacterium phosphoreum species group.";
RL Environ. Microbiol. 7:1641-1654(2005).
RN [2] {ECO:0000313|EMBL:ABU50701.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FS-1.1 {ECO:0000313|EMBL:ABU50701.1};
RA Ast J.C., Cleenwerck I., Engelbeen K., Urbanczyk H., Thompson F.L.,
RA De Vos P., Dunlap P.V.;
RT "Photobacterium kishitanii sp. nov., a luminous marine bacterium symbiotic
RT with deep-sea fishes.";
RL Int. J. Syst. Evol. Microbiol. 57:2073-2078(2007).
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|RuleBase:RU003843}.
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|RuleBase:RU003843};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU003843};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU003843};
CC Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC manganese. {ECO:0000256|RuleBase:RU003843};
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|RuleBase:RU003843}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003843}.
CC -!- SIMILARITY: Belongs to the DHBP synthase family.
CC {ECO:0000256|RuleBase:RU003843}.
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DR EMBL; AY849486; ABU50701.1; -; Genomic_DNA.
DR AlphaFoldDB; A7MAT6; -.
DR UniPathway; UPA00275; UER00399.
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 InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR000422; DHBP_synthase_RibB.
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 SUPFAM; SSF55821; YrdC/RibB; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU003843};
KW Magnesium {ECO:0000256|RuleBase:RU003843};
KW Manganese {ECO:0000256|RuleBase:RU003843};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003843};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW ECO:0000256|RuleBase:RU003843}.
FT NON_TER 154
FT /evidence="ECO:0000313|EMBL:ABU50701.1"
SQ SEQUENCE 154 AA; 16538 MW; 9F38FDFDB88D4C01 CRC64;
MTLSTAQEII EDIRQGKMVI LMDDEDRENE GDLIIASDKI TPEAINFMAT YGRGLICLTL
NKARCLQLKL PLMVKNNTDK FATPFTLSIE AASGVTTGIS VKDRARTVQA AVAAMATSED
IVMPGHIFPL MAQDGGVLTR AGHTEAGCDV ARLA
//
