O66529 (RISB_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Riboflavin synthase beta chain

Gene names

Name:	ribH
Ordered Locus Names:	aq_132

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	154 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. 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
Subunit structure	Oligomer of 60 beta subunits forming an icosahedral capsid.
Sequence similarities	Belongs to the DMRL synthase family.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference 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 – 154

154

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

PRO_0000134708

Secondary structure

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154

Helix Strand Turn

Details...

Beta strand

2 – 4

3

Beta strand

15 – 20

6

Helix

24 – 40

17

Helix

45 – 47

3

Beta strand

48 – 55

8

Helix

56 – 58

3

Helix

59 – 67

9

Beta strand

74 – 82

9

Helix

88 – 107

20

Beta strand

111 – 120

10

Helix

121 – 127

7

Beta strand

128 – 130

3

Helix

135 – 153

19

Sequences

	Sequence		Length	Mass (Da)
	O66529 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: A189410A16454AB7	FASTA	154	16,705
	10 20 30 40 50 60 MQIYEGKLTA EGLRFGIVAS RFNHALVDRL VEGAIDCIVR HGGREEDITL VRVPGSWEIP 70 80 90 100 110 120 VAAGELARKE DIDAVIAIGV LIRGATPHFD YIASEVSKGL ANLSLELRKP ITFGVITADT 130 140 150 LEQAIERAGT KHGNKGWEAA LSAIEMANLF KSLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
[2]	"X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: determinants of thermostability revealed from structural comparisons." Zhang X., Meining W., Fischer M., Bacher A., Ladenstein R. J. Mol. Biol. 306:1099-1114(2001) [PubMed: 11237620] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000657 Genomic DNA. Translation: AAC06489.1.

PIR

F70312.

RefSeq

NP_213089.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HQK	X-ray	1.60	A/B/C/D/E	1-154	[»]
1NQU	X-ray	1.75	A/B/C/D/E	1-154	[»]
1NQV	X-ray	2.05	A/B/C/D/E	1-154	[»]
1NQW	X-ray	2.20	A/B/C/D/E	1-154	[»]
1NQX	X-ray	1.82	A/B/C/D/E	1-154	[»]

ProteinModelPortal

O66529.

SMR

O66529. Positions 1-154.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1192672.

GenomeReviews

Gene locus aq_132 in contig AE000657_GR.

KEGG

aae:aq_132.

NMPDR

fig|224324.1.peg.104.

PATRIC

20957942. VBIAquAeo85532_0111.

Phylogenomic databases

HOGENOM

HBG311126.

OMA

DYVCNEA.

PhylomeDB

O66529.

ProtClustDB

PRK00061.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_132-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.

TIGRFAMs

TIGR00114. Lumazine-synth. 1 hit.

ProtoNet

Search...

Entry information

Entry name

RISB_AQUAE

Accession

Primary (citable) accession number: O66529

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program