P16440 (RISA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Riboflavin synthase alpha chain
EC=2.5.1.9

Gene names

Name:	ribE
Synonyms:	ribB
Ordered Locus Names:	BSU23270

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2-butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The alpha subunit catalyzes the dismutation of 6,7-dimethyl-8-lumazine to riboflavin and 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione.
Catalytic activity	2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine.
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.
Subunit structure	Oligomer that consist of 3 alpha subunits and 60 beta subunits.
Sequence similarities	Contains 2 lumazine-binding repeats.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Domain	Repeat
Molecular function	Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	oxidoreductase activity Inferred from electronic annotation. Source: InterPro riboflavin synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 215	215	Riboflavin synthase alpha chain		PRO_0000068159
Regions
	Repeat	1 – 96	96	Lumazine-binding 1
	Repeat	97 – 193	97	Lumazine-binding 2

Sequences

	Sequence		Length	Mass (Da)
	P16440 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 5B2A694C078B3600	FASTA	215	23,481
	10 20 30 40 50 60 MFTGIIEETG TIESMKKAGH AMALTIKCSK ILEDVHLGDS IAVNGICLTV TDFTKNQFTV 70 80 90 100 110 120 DVMPETVKAT SLNDLTKGSK VNLERAMAAN GRFGGHFVSG HVDGTAEITR IEEKSNAVYY 130 140 150 160 170 180 DLKMDPSLTK TLVLKGSITV DGVSLTIFGL TEDTVTISLI PHTISETIFS EKTIGSKVNI 190 200 210 ECDMIGKYMY RFLHKANENK TQQTITKAFL SENGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Riboflavin synthases of Bacillus subtilis. Purification and amino acid sequence of the alpha subunit." Schott K., Kellermann J., Lottspeich F., Bacher A. J. Biol. Chem. 265:4204-4209(1990) [PubMed: 2106516] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-202.
[2]	Mironov V.N. Thesis (1989), USSR Academy of Sciences, Russia Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / SHGW.
[3]	"The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data." Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P. Mol. Microbiol. 10:385-395(1993) [PubMed: 7934829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[4]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[5]	"Studies on the lumazine synthase/riboflavin synthase complex of Bacillus subtilis: crystal structure analysis of reconstituted, icosahedral beta-subunit capsids with bound substrate analogue inhibitor at 2.4-A resolution." Ritseert K., Huber R., Turk D., Ladenstein R., Schmidt-Baese K., Bacher A. J. Mol. Biol. 253:151-167(1995) [PubMed: 7473709] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L09228 Genomic DNA. Translation: AAA67482.1. X51510 Genomic DNA. Translation: CAA35879.1. AL009126 Genomic DNA. Translation: CAB14259.1.
PIR	A35711. S45544.
RefSeq	NP_390208.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P16440.
SMR	P16440. Positions 1-198.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002822; EBBACP00000002822; EBBACG00000002817.
GeneID	938947.
GenomeReviews	Gene locus BSU23270 in contig AL009126_GR.
KEGG	bsu:BSU23270.
NMPDR	fig|224308.1.peg.2331.
PATRIC	18976471. VBIBacSub10457_2426.
Organism-specific databases
GenoList	BSU23270. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000001264.
HOGENOM	HBG289809.
OMA	PVNLEVD.
PhylomeDB	P16440.
ProtClustDB	PRK09289.
Enzyme and pathway databases
BioCyc	BSUB:BSU23270-MONOMER. MetaCyc:MONOMER-14608.
Family and domain databases
InterPro	IPR023366. ATPase_F1/A1-cplx_a_su_N. IPR001783. Lumazine-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Gene3D	G3DSA:2.40.30.20. G3DSA:2.40.30.20. 2 hits.
KO	K00793.
PANTHER	PTHR21098. Lumazine_bd. 1 hit.
Pfam	PF00677. Lum_binding. 2 hits. [Graphical view]
PIRSF	PIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAM	SSF63380. Riboflavin_synthase_like_b-brl. 2 hits.
TIGRFAMs	TIGR00187. RibE. 1 hit.
PROSITE	PS51177. LUMAZINE_BIND. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RISA_BACSU

Accession

Primary (citable) accession number: P16440
Secondary accession number(s): P17619

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program