(data stored in ACNUC7421 zone)

SWISSPROT: RIBB_EDWI9

ID   RIBB_EDWI9              Reviewed;         219 AA.
AC   C5BHH8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00180};
DE            Short=DHBP synthase {ECO:0000255|HAMAP-Rule:MF_00180};
DE            EC=4.1.99.12 {ECO:0000255|HAMAP-Rule:MF_00180};
GN   Name=ribB {ECO:0000255|HAMAP-Rule:MF_00180};
GN   OrderedLocusNames=NT01EI_0545;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
CC       formate and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00180}.
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
CC       dihydroxybutan-2-one 4-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00180}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00180};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00180};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000255|HAMAP-Rule:MF_00180};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
CC       hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_00180}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00180}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00180}.
DR   EMBL; CP001600; ACR67777.1; -; Genomic_DNA.
DR   RefSeq; WP_015869977.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0545; -.
DR   EnsemblBacteria; ACR67777; ACR67777; NT01EI_0545.
DR   GeneID; 7961569; -.
DR   KEGG; eic:NT01EI_0545; -.
DR   PATRIC; fig|634503.3.peg.494; -.
DR   eggNOG; ENOG4105C66; Bacteria.
DR   eggNOG; COG0108; LUCA.
DR   HOGENOM; HOG000115444; -.
DR   KO; K02858; -.
DR   OMA; VVCEMLD; -.
DR   OrthoDB; POG091H008U; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000001485; 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; -; 1.
DR   HAMAP; MF_00180; RibB; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00506; ribB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHH8.
DR   SWISS-2DPAGE; C5BHH8.
KW   Complete proteome; Lyase; Magnesium; Manganese; Metal-binding;
KW   Reference proteome; Riboflavin biosynthesis.
FT   CHAIN         1    219       3,4-dihydroxy-2-butanone 4-phosphate
FT                                synthase.
FT                                /FTId=PRO_1000203820.
FT   REGION       37     38       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00180}.
FT   REGION      150    154       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00180}.
FT   METAL        38     38       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00180}.
FT   METAL        38     38       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00180}.
FT   METAL       153    153       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00180}.
FT   BINDING      42     42       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00180}.
FT   BINDING     174    174       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00180}.
FT   SITE        136    136       Essential for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00180}.
FT   SITE        174    174       Essential for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00180}.
SQ   SEQUENCE   219 AA;  23898 MW;  CAE61191C20B8E97 CRC64;
     MNQILLSDFG TPMERVERAL SALRDGRGVM VLDDENRENE GDMIFAAEKM TVEQMALTIR
     HGSGIVCLCI TEARRQQLDL PMMVSNNTSH YGTAFTVTIE AAEGVTTGVS AQDRLTTVRA
     AIADDAKPGD LHRPGHVFPL RARPGGVLAR RGHTEATIDL VSLAGFRPAG VLCELTNDDG
     TMARAPQVMA FARQHEMPVV TIEDLVAYRQ AREPQEQAD
//

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