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RISB1_RHILO
ID   RISB1_RHILO             Reviewed;         164 AA.
AC   Q983B0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=6,7-dimethyl-8-ribityllumazine synthase 1;
DE            Short=DMRL synthase 1;
DE            Short=LS 1;
DE            Short=Lumazine synthase 1;
DE            EC=2.5.1.78;
DE   AltName: Full=Type I lumazine synthase;
GN   Name=ribH1; Synonyms=ribH; OrderedLocusNames=mlr8409;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
RN   [2]
RP   GENE NAME.
RX   PubMed=16923880; DOI=10.1128/jb.00207-06;
RA   Zylberman V., Klinke S., Haase I., Bacher A., Fischer M., Goldbaum F.A.;
RT   "Evolution of vitamin B2 biosynthesis: 6,7-dimethyl-8-ribityllumazine
RT   synthases of Brucella.";
RL   J. Bacteriol. 188:6135-6142(2006).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND SUBUNIT.
RX   PubMed=17854827; DOI=10.1016/j.jmb.2007.08.021;
RA   Klinke S., Zylberman V., Bonomi H.R., Haase I., Guimaraes B.G.,
RA   Braden B.C., Bacher A., Fischer M., Goldbaum F.A.;
RT   "Structural and kinetic properties of lumazine synthase isoenzymes in the
RT   order Rhizobiales.";
RL   J. Mol. Biol. 373:664-680(2007).
CC   -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by
CC       condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-
CC       butanone 4-phosphate. This is the penultimate step in the biosynthesis
CC       of riboflavin. {ECO:0000269|PubMed:17854827}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-
CC         ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2
CC         H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;
CC         Evidence={ECO:0000269|PubMed:17854827};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.5 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius
CC         and pH 7.0) {ECO:0000269|PubMed:17854827};
CC         KM=15 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees
CC         Celsius and pH 7.0) {ECO:0000269|PubMed:17854827};
CC         Note=kcat is 0.040 sec(-1) (at 37 degrees Celsius and pH 7.0).;
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC       from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC       ribitylamino)uracil: step 1/2.
CC   -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:17854827}.
CC   -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
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DR   EMBL; BA000012; BAB54296.1; -; Genomic_DNA.
DR   RefSeq; WP_010915596.1; NC_002678.2.
DR   AlphaFoldDB; Q983B0; -.
DR   SMR; Q983B0; -.
DR   STRING; 266835.14027703; -.
DR   EnsemblBacteria; BAB54296; BAB54296; BAB54296.
DR   KEGG; mlo:mlr8409; -.
DR   PATRIC; fig|266835.9.peg.6724; -.
DR   eggNOG; COG0054; Bacteria.
DR   HOGENOM; CLU_089358_1_2_5; -.
DR   OMA; CQGVTQG; -.
DR   OrthoDB; 1680292at2; -.
DR   BRENDA; 2.5.1.78; 3243.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR   GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd09209; Lumazine_synthase-I; 1.
DR   Gene3D; 3.40.50.960; -; 1.
DR   HAMAP; MF_00178; Lumazine_synth; 1.
DR   InterPro; IPR034964; LS.
DR   InterPro; IPR002180; LS/RS.
DR   InterPro; IPR036467; LS/RS_sf.
DR   PANTHER; PTHR21058; PTHR21058; 1.
DR   Pfam; PF00885; DMRL_synthase; 1.
DR   SUPFAM; SSF52121; SSF52121; 1.
DR   TIGRFAMs; TIGR00114; lumazine-synth; 1.
PE   1: Evidence at protein level;
KW   Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..164
FT                   /note="6,7-dimethyl-8-ribityllumazine synthase 1"
FT                   /id="PRO_0000134793"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         27
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000250"
FT   BINDING         58..60
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000250"
FT   BINDING         87..89
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000250"
FT   BINDING         92..93
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   164 AA;  17196 MW;  9C9A7FADE8DC7C3C CRC64;
     MAGISQHGKA FIRPKAKAHL LIVEARFHDD LADALLDGAT SALEEAGATY DVVTVPGSLE
     IPAVITFALD GAAEGGTNYD GFVALGTIIR GDTYHFDIVA NESSRALMDM SVQDSVCIGN
     GILTTENDAQ AWTRAKRSEG DKGGFAARAA LTMIALKEQL GARS
 
 
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