A5I603 (RIBB_CLOBH) Reviewed, UniProtKB/Swiss-Prot

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:	CBO2921, CLC_2815

Organism

Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)

Taxonomic identifier

441771 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
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. HAMAP MF_00180
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. HAMAP MF_00180
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 Reference proteome
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 213	213	3,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180		PRO_1000040599
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)
	A5I603 [UniParc]. Last modified June 26, 2007. Version 1. Checksum: D4E8EEC15DFC805E	FASTA	213	23,266
	10 20 30 40 50 60 MNESLLTQFG NSLTRVEKAL ENLKNGKGVL LVDDENRENE GDLIFPAETI TVPQMVMLIR 70 80 90 100 110 120 ECSGIVCLCL TDKKVKKLGL TQMVHNNTCT YETAFTISIE AKEGVTTGVS AADRVTTILT 130 140 150 160 170 180 AVKDDCKPED LCHPGHVFPL RARAGGVLTR PGHTEGTVDL MRLAGYNPAG ILCELTNPDG 190 200 210 TMARLPQIIN FAKKHNLAVL SIEDIIKYKK ITT

References

[1]

"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes." Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J. Genome Res. 17:1082-1092(2007) [PubMed: 17519437] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

[2]

"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids." Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S. PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000727 Genomic DNA. Translation: ABS38196.1. AM412317 Genomic DNA. Translation: CAL84483.1.
RefSeq	YP_001255415.1. NC_009495.1. YP_001388650.1. NC_009698.1.
3D structure databases
ProteinModelPortal	A5I603.
SMR	A5I603. Positions 1-210.
ModBase	Search...
Protein-protein interaction databases
STRING	A5I603.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5187176. 5399861.
GenomeReviews	Gene locus CBO2921 in contig AM412317_GR. Gene locus CLC_2815 in contig CP000727_GR.
KEGG	cbh:CLC_2815. cbo:CBO2921.
PATRIC	19367913. VBICloBot22612_2899.
Phylogenomic databases
eggNOG	COG0108.
HOGENOM	HBG735778.
OMA	GDMIFAA.
ProtClustDB	CLSK941046.
Enzyme and pathway databases
BioCyc	CBOT36826:CBO2921-MONOMER. CBOT441771:CLC_2815-MONOMER.
Family and domain databases
HAMAP	MF_00180. RibB. [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.
KO	K02858.
Pfam	PF00926. DHBP_synthase. 1 hit. [Graphical view]
SUPFAM	SSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit.
TIGRFAMs	TIGR00506. RibB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RIBB_CLOBH

Accession

Primary (citable) accession number: A5I603
Secondary accession number(s): A7G785

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 26, 2007
Last modified:	December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program