Reviewed, UniProtKB/Swiss-Prot Q7W2M1 (RIBB_BORPA)

Names and origin

Protein names

Recommended name:
    3,4-dihydroxy-2-butanone 4-phosphate synthase
      Short name=DHBP synthase
    EC=4.1.99.12

Gene names

Name:	ribB
Ordered Locus Names:	BPP4385

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	230 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate By similarity.
Catalytic activity	D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP MF_00180
Cofactor	Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_00180
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the DHBP synthase family.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	Magnesium Manganese Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 230	230	3,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180		PRO_0000151789
Regions
	Region	42 – 43	2	Substrate binding By similarity
	Region	155 – 159	5	Substrate binding By similarity
Sites
	Metal binding	43	1	Magnesium or manganese 1 By similarity
	Metal binding	43	1	Magnesium or manganese 2 By similarity
	Metal binding	158	1	Magnesium or manganese 2 By similarity
	Binding site	47	1	Substrate By similarity
	Binding site	179	1	Substrate By similarity
	Site	141	1	Essential for catalytic activity By similarity
	Site	179	1	Essential for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7W2M1-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 976E0451584FDB42	FASTA	230	24,125
	10 20 30 40 50 60 MSNVVPTPVS PLFAQPFATR LERALQHLRI GRPVILMDDF DRENEADLIV AADKLTVPVM 70 80 90 100 110 120 AQLIRDGSGI VCLCLPGETL DRLELPPMVD SNRSRYSTAF TVSIEAREGV TTGVSAVDRV 130 140 150 160 170 180 TTIRAAIAPG ARSGDVVSPG HVFPLRAQPG GVLTRRGHTE GSVDLAALAG LRPAGVLCEL 190 200 210 220 230 MNADGTMMRG ASLERYAAKE GLVALAIDEL AAHLQARGAT GAPAELAVAA

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640436 Genomic DNA. Translation: CAE39664.1.
RefSeq	NP_886511.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1667144.
GenomeReviews	Gene locus BPP4385 in contig BX470249_GR.
KEGG	bpa:BPP4385.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7W2M1.
OMA	YGSGIVC.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP4385-MON.
BRENDA	4.1.99.12. 263123.
Family and domain databases
HAMAP	MF_00180. [Tree]
InterPro	IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR000422. DHBP_synthase_RibB. [Graphical view]
Gene3D	G3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
Pfam	PF00926. DHBP_synthase. 1 hit. [Graphical view]
ProDom	PD003034. DHBP_synthase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00506. ribB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RIBB_BORPA

Accession

Primary (citable) accession number: Q7W2M1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)