ID A0A0G3ELJ9_9BACT Unreviewed; 387 AA.
AC A0A0G3ELJ9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00073, ECO:0000256|HAMAP-Rule:MF_00178};
DE Includes:
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178};
DE Short=DMRL synthase {ECO:0000256|HAMAP-Rule:MF_00178};
DE Short=LS {ECO:0000256|HAMAP-Rule:MF_00178};
DE Short=Lumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178};
DE EC=2.5.1.78 {ECO:0000256|HAMAP-Rule:MF_00178};
DE Includes:
DE RecName: Full=Transcription antitermination protein NusB {ECO:0000256|HAMAP-Rule:MF_00073};
DE AltName: Full=Antitermination factor NusB {ECO:0000256|HAMAP-Rule:MF_00073};
GN Name=ribH {ECO:0000256|HAMAP-Rule:MF_00178,
GN ECO:0000313|EMBL:AKJ65019.1};
GN Synonyms=nusB {ECO:0000256|HAMAP-Rule:MF_00073};
GN ORFNames=L21SP4_01781 {ECO:0000313|EMBL:AKJ65019.1};
OS Kiritimatiella glycovorans.
OC Bacteria; Kiritimatiellota; Kiritimatiellia; Kiritimatiellales;
OC Kiritimatiellaceae; Kiritimatiella.
OX NCBI_TaxID=1307763 {ECO:0000313|EMBL:AKJ65019.1, ECO:0000313|Proteomes:UP000035268};
RN [1] {ECO:0000313|Proteomes:UP000035268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Fru-AB {ECO:0000313|Proteomes:UP000035268};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of the first cultured
RT representative of the subdivision 5 of the Verrucomicrobia phylum.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKJ65019.1, ECO:0000313|Proteomes:UP000035268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Fru-AB {ECO:0000313|EMBL:AKJ65019.1,
RC ECO:0000313|Proteomes:UP000035268};
RX PubMed=27300277; DOI=10.1038/ismej.2016.84;
RA Spring S., Bunk B., Sproer C., Schumann P., Rohde M., Tindall B.J.,
RA Klenk H.P.;
RT "Characterization of the first cultured representative of Verrucomicrobia
RT subdivision 5 indicates the proposal of a novel phylum.";
RL ISME J. 10:2801-2816(2016).
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:0000256|HAMAP-Rule:MF_00178}.
CC -!- FUNCTION: Involved in transcription antitermination. Required for
CC transcription of ribosomal RNA (rRNA) genes. Binds specifically to the
CC boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
CC {ECO:0000256|HAMAP-Rule:MF_00073}.
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:0000256|ARBA:ARBA00001697, ECO:0000256|HAMAP-
CC Rule:MF_00178};
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. {ECO:0000256|ARBA:ARBA00004917,
CC ECO:0000256|HAMAP-Rule:MF_00178}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family.
CC {ECO:0000256|ARBA:ARBA00007424, ECO:0000256|HAMAP-Rule:MF_00178}.
CC -!- SIMILARITY: Belongs to the NusB family. {ECO:0000256|ARBA:ARBA00005952,
CC ECO:0000256|HAMAP-Rule:MF_00073}.
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DR EMBL; CP010904; AKJ65019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3ELJ9; -.
DR STRING; 1307763.L21SP4_01781; -.
DR KEGG; vbl:L21SP4_01781; -.
DR PATRIC; fig|1609981.3.peg.1848; -.
DR OrthoDB; 9809709at2; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000035268; 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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-UniRule.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-KW.
DR CDD; cd09209; Lumazine_synthase-I; 1.
DR CDD; cd00619; Terminator_NusB; 1.
DR Gene3D; 3.40.50.960; Lumazine/riboflavin synthase; 1.
DR Gene3D; 1.10.940.10; NusB-like; 1.
DR HAMAP; MF_00178; Lumazine_synth; 1.
DR HAMAP; MF_00073; NusB; 1.
DR InterPro; IPR034964; LS.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR InterPro; IPR035926; NusB-like_sf.
DR InterPro; IPR011605; NusB_fam.
DR InterPro; IPR006027; NusB_RsmB_TIM44.
DR NCBIfam; TIGR00114; lumazine-synth; 1.
DR NCBIfam; TIGR01951; nusB; 1.
DR PANTHER; PTHR21058:SF0; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE; 1.
DR PANTHER; PTHR21058; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE DMRL SYNTHASE LUMAZINE SYNTHASE; 1.
DR Pfam; PF00885; DMRL_synthase; 1.
DR Pfam; PF01029; NusB; 1.
DR SUPFAM; SSF52121; Lumazine synthase; 1.
DR SUPFAM; SSF48013; NusB-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000035268};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW Rule:MF_00178};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00073};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00073};
KW Transcription antitermination {ECO:0000256|ARBA:ARBA00022814,
KW ECO:0000256|HAMAP-Rule:MF_00073};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_00073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00178}.
FT DOMAIN 241..366
FT /note="NusB/RsmB/TIM44"
FT /evidence="ECO:0000259|Pfam:PF01029"
FT REGION 172..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 40
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 74..76
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 98..100
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 103..104
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 131
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 145
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
SQ SEQUENCE 387 AA; 42353 MW; 4D944461F544DD79 CRC64;
MNEQKGMAES FEDLPALAAQ TRDGRGGAQG LRFAIAVSRF NLALTGELAR SAVDALRGAG
ARQEDLTVCW APGAGELPGV LAALAEQSSF DALIALGAVI EGETSHARMI IRSTGFALQE
LARSTGTPVI NEIVGAPSWA HAEARCRYGE GSRGWYAAEA AVETANLYRR IRAPHPPPVS
PPPPVEPTPS PEVPETGAAE PEIWQPSARP DRGEPQPGDE PSPPPPSEEP EPESRPARGR
REARRWAVQM LYQADLNPSP IEELFASFFE DKRPVARFRT FAEKTVREVM ARRGELDARL
QSFTPNWEVE RMGCVDRNIM RVALYEMFYR DDIPPVVSIN EAIEIAKDLS SDESARFVNG
VLDKVRKSIS RPARTVRPGP VTGEEEE
//
