Q92NI1 (RISB2_RHIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6,7-dimethyl-8-ribityllumazine synthase 2
Short name=DMRL synthase 2
Short name=Lumazine synthase 2
EC=2.5.1.9

Alternative name(s):
Riboflavin synthase 2 beta chain

Gene names

Name:	ribH2
Ordered Locus Names:	R02221
ORF Names:	SMc01609

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 beta subunit catalyzes the condensation of 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate yielding 6,7-dimethyl-8-lumazine By similarity. HAMAP MF_00178
Catalytic activity	2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. HAMAP MF_00178
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2. HAMAP MF_00178
Sequence similarities	Belongs to the DMRL synthase family.
Sequence caution	The sequence CAC46800.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	riboflavin synthase complex Inferred from electronic annotation. Source: InterPro
Molecular function	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 – 157	157	6,7-dimethyl-8-ribityllumazine synthase 2 HAMAP MF_00178		PRO_0000134795

Sequences

	Sequence		Length	Mass (Da)
	Q92NI1 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 90FA9171C982C039	FASTA	157	16,935
	10 20 30 40 50 60 MTILSHPSAK IAIVRARWHA DIVDRCVDAF VAQWTKLGGS AADVEIFDVP GALEIPLHAQ 70 80 90 100 110 120 ALARTGRYAA ILGTAFVVNG GIYRHDFVSG TVLDGMMRVQ LDTDVPVLSA VLTPHNFQES 130 140 150 EPLIAFFRDH FVVKGEEAAN ACAQILDARA KLALVDA

References

[1]	"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[2]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed: 11474104] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591688 Genomic DNA. Translation: CAC46800.1. Different initiation.
RefSeq	NP_386327.1. NC_003047.1.
3D structure databases
ProteinModelPortal	Q92NI1.
SMR	Q92NI1. Positions 6-152.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1233887.
GenomeReviews	Gene locus R02221 in contig AL591688_GR.
KEGG	sme:SMc01609.
NMPDR	fig|266834.1.peg.3515.
PATRIC	23633905. VBISinMel96828_3690.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG311126.
ProtClustDB	PRK12419.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC01609-MONOMER.
Family and domain databases
HAMAP	MF_00178. Lumazine_synth. [Tree]
InterPro	IPR002180. DMRL_synthase. [Graphical view]
Gene3D	G3DSA:3.40.50.960. DMRL_synthase. 1 hit.
KO	K00794.
PANTHER	PTHR21058. DMRL_synthase. 1 hit.
Pfam	PF00885. DMRL_synthase. 1 hit. [Graphical view]
SUPFAM	SSF52121. DMRL_synthase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RISB2_RHIME

Accession

Primary (citable) accession number: Q92NI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	January 23, 2002
Last modified:	January 25, 2012
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program