P66034 (RISB_MYCTU) 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:	Rv1416, MT1459
ORF Names:	MTCY21B4.34

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	160 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 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
Miscellaneous	Was identified as a high-confidence drug target. HAMAP MF_00178
Sequence similarities	Belongs to the DMRL synthase family.
Sequence caution	The sequence CAB02164.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	growth Inferred from mutant phenotype. Source: MTBBASE 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 – 160

160

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

PRO_0000134772

Secondary structure

1

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160

Helix Strand Turn

Details...

Beta strand

20 – 24

5

Helix

29 – 45

17

Beta strand

52 – 55

4

Helix

59 – 61

3

Helix

62 – 69

8

Beta strand

74 – 83

10

Helix

89 – 108

20

Beta strand

112 – 121

10

Helix

122 – 126

5

Helix

138 – 156

19

Sequences

	Sequence		Length	Mass (Da)
	P66034 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 20E837C273312E83	FASTA	160	16,371
	10 20 30 40 50 60 MKGGAGVPDL PSLDASGVRL AIVASSWHGK ICDALLDGAR KVAAGCGLDD PTVVRVLGAI 70 80 90 100 110 120 EIPVVAQELA RNHDAVVALG VVIRGQTPHF DYVCDAVTQG LTRVSLDSST PIANGVLTTN 130 140 150 160 TEEQALDRAG LPTSAEDKGA QATVAALATA LTLRELRAHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Experimental determination of translational starts using peptide mass mapping and tandem mass spectrometry within the proteome of Mycobacterium tuberculosis." Rison S.C., Mattow J., Jungblut P.R., Stoker N.G. Microbiology 153:521-528(2007) [PubMed: 17259624] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, DETERMINATION OF TRANSLATIONAL START SITE. Strain: ATCC 25618 / H37Rv.
[4]	"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis." Raman K., Yeturu K., Chandra N. BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842576 Genomic DNA. Translation: CAB02164.1. Different initiation.
AE000516 Genomic DNA. Translation: AAK45724.1.

PIR

E70902.

RefSeq

NP_215932.1. NC_000962.2.
NP_335910.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W19	X-ray	2.00	A/B/C/D/E	1-160	[»]
1W29	X-ray	2.30	A/B/C/D/E	1-160	[»]
2C92	X-ray	1.60	A/B/C/D/E	1-160	[»]
2C94	X-ray	1.90	A/B/C/D/E	1-160	[»]
2C97	X-ray	2.00	A/B/C/D/E	1-160	[»]
2C9B	X-ray	2.75	A/B/C/D/E/F/G/H/I/J	1-160	[»]
2C9D	X-ray	2.80	A/B/C/D/E/F/G/H/I/J	1-160	[»]
2VI5	X-ray	2.30	A/B/C/D/E/F/G/H/I/J	1-160	[»]

ProteinModelPortal

P66034.

SMR

P66034. Positions 10-160.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000003301; EBMYCP00000003301; EBMYCG00000003299.
EBMYCT00000072146; EBMYCP00000070205; EBMYCG00000072141.

GeneID

886681.
924512.

GenomeReviews

Gene locus MT1459 in contig AE000516_GR.
Gene locus Rv1416 in contig AL123456_GR.

KEGG

mtc:MT1459.
mtu:Rv1416.

PATRIC

18124978. VBIMycTub22151_1603.

TIGR

MT1459.

Organism-specific databases

TubercuList

Rv1416.

Phylogenomic databases

GeneTree

EBGT00050000016935.

HOGENOM

HBG311126.

OMA

SSRALMD.

PhylomeDB

P66034.

ProtClustDB

PRK00061.

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_MYCTU

Accession

Primary (citable) accession number: P66034
Secondary accession number(s): P71685

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program