RISA_BACSU
ID RISA_BACSU Reviewed; 215 AA.
AC P16440; P17619;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Riboflavin synthase;
DE Short=RS;
DE EC=2.5.1.9;
DE AltName: Full=Heavy riboflavin synthase alpha subunit;
DE Short=HRS alpha subunit;
DE AltName: Full=Light riboflavin synthase;
GN Name=ribE; Synonyms=ribB; OrderedLocusNames=BSU23270;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP PROTEIN SEQUENCE OF 1-202, AND SUBUNIT.
RX PubMed=2106516; DOI=10.1016/s0021-9258(19)39547-x;
RA Schott K., Kellermann J., Lottspeich F., Bacher A.;
RT "Riboflavin synthases of Bacillus subtilis. Purification and amino acid
RT sequence of the alpha subunit.";
RL J. Biol. Chem. 265:4204-4209(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / SHGW;
RA Mironov V.N.;
RL Thesis (1989), USSR Academy of Sciences, Russia.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7934829; DOI=10.1111/j.1365-2958.1993.tb02670.x;
RA Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT "The organization of the Bacillus subtilis 168 chromosome region between
RT the spoVA and serA genetic loci, based on sequence data.";
RL Mol. Microbiol. 10:385-395(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=6766130; DOI=10.1016/s0021-9258(19)86223-3;
RA Bacher A., Baur R., Eggers U., Harders H.D., Otto M.K., Schnepple H.;
RT "Riboflavin synthases of Bacillus subtilis. Purification and properties.";
RL J. Biol. Chem. 255:632-637(1980).
RN [6]
RP SUBUNIT.
RX PubMed=3083108; DOI=10.1016/0022-2836(86)90407-9;
RA Bacher A., Ludwig H.C., Schnepple H., Ben-Shaul Y.;
RT "Heavy riboflavin synthase from Bacillus subtilis. Quaternary structure and
RT reaggregation.";
RL J. Mol. Biol. 187:75-86(1986).
CC -!- FUNCTION: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-
CC ribityllumazine, resulting in the formation of riboflavin and 5-amino-
CC 6-(D-ribitylamino)uracil. {ECO:0000269|PubMed:6766130}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-
CC ribitylamino)uracil + riboflavin; Xref=Rhea:RHEA:20772,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58201; EC=2.5.1.9; Evidence={ECO:0000269|PubMed:6766130};
CC -!- ACTIVITY REGULATION: Is activated by sulfite ions.
CC {ECO:0000269|PubMed:6766130}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for 6,7-dimethyl-8-(1-D-ribityl)lumazine
CC {ECO:0000269|PubMed:6766130};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:6766130};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 2/2.
CC -!- SUBUNIT: Homotrimer. Can interact with 6,7-dimethyl-8-ribityllumazine
CC synthase, forming a lumazine synthase/riboflavin synthase complex, also
CC designated as 'heavy riboflavin synthase complex', which consists of a
CC trimer of riboflavin synthase enclosed within an icosahedral structure
CC composed of 60 subunits of 6,7-dimethyl-8-ribityllumazine synthase.
CC {ECO:0000269|PubMed:2106516, ECO:0000269|PubMed:3083108,
CC ECO:0000269|PubMed:6766130}.
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DR EMBL; L09228; AAA67482.1; -; Genomic_DNA.
DR EMBL; X51510; CAA35879.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14259.1; -; Genomic_DNA.
DR PIR; S45544; A35711.
DR RefSeq; NP_390208.1; NC_000964.3.
DR RefSeq; WP_004398505.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P16440; -.
DR SMR; P16440; -.
DR STRING; 224308.BSU23270; -.
DR PaxDb; P16440; -.
DR PRIDE; P16440; -.
DR EnsemblBacteria; CAB14259; CAB14259; BSU_23270.
DR GeneID; 938947; -.
DR KEGG; bsu:BSU23270; -.
DR PATRIC; fig|224308.179.peg.2534; -.
DR eggNOG; COG0307; Bacteria.
DR InParanoid; P16440; -.
DR OMA; HFVTGHV; -.
DR PhylomeDB; P16440; -.
DR BioCyc; BSUB:BSU23270-MON; -.
DR BioCyc; MetaCyc:MON-14608; -.
DR SABIO-RK; P16440; -.
DR UniPathway; UPA00275; UER00405.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004746; F:riboflavin synthase activity; IBA:GO_Central.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
DR CDD; cd00402; Riboflavin_synthase_like; 1.
DR Gene3D; 2.40.30.20; -; 2.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR001783; Lumazine-bd.
DR InterPro; IPR026017; Lumazine-bd_dom.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR21098; PTHR21098; 1.
DR Pfam; PF00677; Lum_binding; 2.
DR PIRSF; PIRSF000498; Riboflavin_syn_A; 1.
DR SUPFAM; SSF63380; SSF63380; 2.
DR TIGRFAMs; TIGR00187; ribE; 1.
DR PROSITE; PS51177; LUMAZINE_BIND; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Repeat;
KW Riboflavin biosynthesis; Transferase.
FT CHAIN 1..215
FT /note="Riboflavin synthase"
FT /id="PRO_0000068159"
FT REPEAT 1..96
FT /note="Lumazine-binding 1"
FT REPEAT 97..193
FT /note="Lumazine-binding 2"
FT BINDING 4..6
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 47..49
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 61..66
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0AFU8"
FT BINDING 100..102
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 135
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 144..146
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 158..163
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
SQ SEQUENCE 215 AA; 23481 MW; 5B2A694C078B3600 CRC64;
MFTGIIEETG TIESMKKAGH AMALTIKCSK ILEDVHLGDS IAVNGICLTV TDFTKNQFTV
DVMPETVKAT SLNDLTKGSK VNLERAMAAN GRFGGHFVSG HVDGTAEITR IEEKSNAVYY
DLKMDPSLTK TLVLKGSITV DGVSLTIFGL TEDTVTISLI PHTISETIFS EKTIGSKVNI
ECDMIGKYMY RFLHKANENK TQQTITKAFL SENGF
