Reviewed, UniProtKB/Swiss-Prot P57167 (RIBB_BUCAI)

Names and origin

Protein names

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

Gene names

Name:	ribB
Ordered Locus Names:	BU059

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	215 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.
Cofactor	Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 3,4-dihydroxy-2-butanone 4-phosphate from D-ribulose 5-phosphate: step 1/1.
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
Molecule processing
	Chain	1 – 215	215	3,4-dihydroxy-2-butanone 4-phosphate synthase
Regions
	Region	37 – 38	2	Substrate binding By similarity
	Region	150 – 154	5	Substrate binding By similarity
Sites
	Metal binding	38	1	Magnesium or manganese 1 By similarity
	Metal binding	38	1	Magnesium or manganese 2 By similarity
	Metal binding	153	1	Magnesium or manganese 2 By similarity
	Binding site	42	1	Substrate By similarity
	Binding site	174	1	Substrate By similarity
	Site	136	1	Essential for catalytic activity By similarity
	Site	174	1	Essential for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57167-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 39F8437670FEA531	FASTA	215	23,574
	10 20 30 40 50 60 MNQTLLSKFG KPIERIKNAI LALKSGQGVI ILDDEERENE GDLVFACENM TVEQMALSIR 70 80 90 100 110 120 YGSGIVCLCI TESKRKQLNL PMMVKKNTSA YRTGFTVTIE ASKGISTGVS AKDRLTTIKT 130 140 150 160 170 180 AIADDAKPSD LNRPGHVFPL RAHKGGVLSR PGHTEAAIEI VSLAGFKPAG VICELTNKDG 190 200 210 TMARTPEIIK FSENKKMQVL TIQDLIFYIK NINHL

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB12782.1.
RefSeq	NP_239896.1.
3D structure databases
HSSP	HSSP built from PDB template 1G58 based on UniProtKB P24199.
ModBase	Search...
Genome annotation databases
GeneID	1109466.
GenomeReviews	Gene locus BU059 in contig BA000003_GR.
KEGG	buc:BU059.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57167.
Enzyme and pathway databases
BioCyc	BSP107806:BU059-MON.
Family and domain databases
HAMAP	MF_00180. [Tree]
InterPro	IPR000422. DHBP_synthase. [Graphical view]
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.
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

RIBB_BUCAI

Accession

Primary (citable) accession number: P57167

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	July 22, 2008
This is version 35 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)