P61711 (RISB2_BRUAB) 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
Synonyms:	ribH, ribH-2
Ordered Locus Names:	BruAb2_0535

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	158 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 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. Ref.3
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
Subunit structure	Homopentamer Probable.
Sequence similarities	Belongs to the DMRL synthase family.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Molecular function	Transferase
Technical term	3D-structure 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 – 158

158

6,7-dimethyl-8-ribityllumazine synthase 2 HAMAP MF_00178

PRO_0000134725

Secondary structure

1

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158

Helix Strand Turn

Details...

Beta strand

11 – 18

8

Helix

22 – 40

19

Beta strand

43 – 53

11

Helix

54 – 56

3

Helix

57 – 66

10

Beta strand

71 – 78

8

Beta strand

83 – 85

3

Helix

88 – 105

18

Beta strand

109 – 114

6

Beta strand

116 – 118

3

Helix

123 – 153

31

Sequences

	Sequence		Length	Mass (Da)
	P61711 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: EE59C2C815E53A2B	FASTA	158	17,356
	10 20 30 40 50 60 MNQSCPNKTS FKIAFIQARW HADIVDEARK SFVAELAAKT GGSVEVEIFD VPGAYEIPLH 70 80 90 100 110 120 AKTLARTGRY AAIVGAAFVI DGGIYRHDFV ATAVINGMMQ VQLETEVPVL SVVLTPHHFH 130 140 150 ESKEHHDFFH AHFKVKGVEA AHAALQIVSE RSRIAALV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of a newly identified Brucella abortus gene and serological evaluation of the 17-kilodalton antigen that it encodes." Hemmen F., Weynants V., Scarcez T., Letesson J.-J., Saman E. Clin. Diagn. Lab. Immunol. 2:263-267(1995) [PubMed: 7664168] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.
[3]	"The 18-kDa cytoplasmic protein of Brucella species -- an antigen useful for diagnosis -- is a lumazine synthase." Goldbaum F.A., Velikovsky C.A., Baldi P.C., Moertl S., Bacher A., Fossati C.A. J. Med. Microbiol. 48:833-839(1999) [PubMed: 10482294] [Abstract] Cited for: FUNCTION.
[4]	"Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus." Braden B.C., Velikovsky C.A., Cauerhff A.A., Polikarpov I., Goldbaum F.A. J. Mol. Biol. 297:1031-1036(2000) [PubMed: 10764570] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z46864 Genomic DNA. Translation: CAA86936.1.
AE017224 Genomic DNA. Translation: AAX75953.1.

PIR

S49918.

RefSeq

YP_223314.1. NC_006933.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DI0	X-ray	2.70	A/B/C/D/E	1-158	[»]
1T13	X-ray	2.90	A/B/C/D/E	1-158	[»]
1XN1	X-ray	3.05	A/B/C/D/E/F/G/H/I/J	1-158	[»]

ProteinModelPortal

P61711.

SMR

P61711. Positions 8-157.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3341228.

GenomeReviews

Gene locus BruAb2_0535 in contig AE017224_GR.

KEGG

bmb:BruAb2_0535.

PATRIC

17827340. VBIBruAbo15061_2848.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG311126.

OMA

RRYTAIV.

PhylomeDB

P61711.

ProtClustDB

PRK12419.

Enzyme and pathway databases

BioCyc

BABO262698:BRUAB2_0535-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_BRUAB

Accession

Primary (citable) accession number: P61711
Secondary accession number(s): Q44668, Q578I1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program