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RIBB_VIBHA
ID   RIBB_VIBHA              Reviewed;         230 AA.
AC   P16448;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 87.
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};
DE   AltName: Full=LUXH protein;
GN   Name=ribB {ECO:0000255|HAMAP-Rule:MF_00180}; Synonyms=luxH;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2303459; DOI=10.1016/s0021-9258(19)39798-4;
RA   Swartzman E., Miyamoto C., Graham A., Meighen E.;
RT   "Delineation of the transcriptional boundaries of the lux operon of Vibrio
RT   harveyi demonstrates the presence of two new lux genes.";
RL   J. Biol. Chem. 265:3513-3517(1990).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate. {ECO:0000255|HAMAP-
CC       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:0000255|HAMAP-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-hydroxy-3-
CC       oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00180}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00180}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00180}.
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DR   EMBL; M27139; AAA27538.1; -; Genomic_DNA.
DR   PIR; C35081; C35081.
DR   RefSeq; WP_038897477.1; NZ_UAVF01000022.1.
DR   AlphaFoldDB; P16448; -.
DR   SMR; P16448; -.
DR   PRIDE; P16448; -.
DR   GeneID; 57823099; -.
DR   PATRIC; fig|669.65.peg.3623; -.
DR   UniPathway; UPA00275; UER00399.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
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   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;
KW   Lyase; Magnesium; Manganese; Metal-binding; Riboflavin biosynthesis.
FT   CHAIN           1..230
FT                   /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT                   /id="PRO_0000151815"
FT   BINDING         38..39
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         43
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         151..155
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   BINDING         175
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   SITE            137
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
FT   SITE            175
FT                   /note="Essential for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00180"
SQ   SEQUENCE   230 AA;  25328 MW;  665EF0DC266B0174 CRC64;
     MSSTSLLDEF GTPVQRVERA IEALKNGLGV LLMDDEDREN EGDLIFSAQH LTEAQMALMI
     REGSGIVCLC LTEERANWLD LPPMVKDNCS KNQTAFTVSI EAKEGVTTGV SAKDRVTTVK
     TATYFDAQPE DLARPGHVFP LVAKTNGVLA RRGHTEGTID LMYLANLVPS GILCELTNPD
     GTMAKLPETI EFARRHGMPV LTIEDIVDYR TGIDLRNEYK SGLVREVSWS
 
 
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