Reviewed, UniProtKB/Swiss-Prot A7GSD5 (RIBBA_BACCN)

Names and origin

Protein names

Recommended name:
    Riboflavin biosynthesis protein ribBA
Including the following 2 domains:
    1- Recommended name:
            3,4-dihydroxy-2-butanone 4-phosphate synthase
                Short name=DHBP synthase
              EC=4.1.99.12
    2- Recommended name:
            GTP cyclohydrolase-2
              EC=3.5.4.25
        Alternative name(s):
            GTP cyclohydrolase II

Gene names

Name:	ribBA
Ordered Locus Names:	Bcer98_2810

Organism

Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]

Taxonomic identifier

315749 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	397 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_01283 Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity. HAMAP MF_01283
Catalytic activity	D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP MF_01283 GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate. HAMAP MF_01283
Cofactor	Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity. HAMAP MF_01283 Binds 1 zinc ion per subunit By similarity. HAMAP MF_01283
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_01283 Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. HAMAP MF_01283
Sequence similarities	In the N-terminal section; belongs to the DHBP synthase family. In the C-terminal section; belongs to the GTP cyclohydrolase II family.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	GTP-binding Magnesium Manganese Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Lyase
Technical term	Complete proteome Multifunctional enzyme
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 GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase II 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 zinc 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 – 397	397	Riboflavin biosynthesis protein ribBA HAMAP MF_01283		PRO_1000085897
Regions
	Nucleotide binding	250 – 254	5	GTP By similarity
	Nucleotide binding	293 – 295	3	GTP By similarity
	Region	1 – 199	199	DHBP synthase HAMAP MF_01283
	Region	26 – 27	2	D-ribulose 5-phosphate binding By similarity
	Region	138 – 142	5	D-ribulose 5-phosphate binding By similarity
	Region	200 – 397	198	GTP cyclohydrolase II HAMAP MF_01283
Sites
	Active site	327	1	Proton acceptor; for GTP cyclohydrolase activity Potential
	Active site	329	1	Nucleophile; for GTP cyclohydrolase activity By similarity
	Metal binding	27	1	Magnesium or manganese 1 By similarity
	Metal binding	27	1	Magnesium or manganese 2 By similarity
	Metal binding	141	1	Magnesium or manganese 2 By similarity
	Metal binding	255	1	Zinc; catalytic By similarity
	Metal binding	266	1	Zinc; catalytic By similarity
	Metal binding	268	1	Zinc; catalytic By similarity
	Binding site	31	1	D-ribulose 5-phosphate By similarity
	Binding site	162	1	D-ribulose 5-phosphate By similarity
	Binding site	271	1	GTP By similarity
	Binding site	315	1	GTP By similarity
	Binding site	350	1	GTP By similarity
	Binding site	355	1	GTP By similarity
	Site	124	1	Essential for DHBP synthase activity By similarity
	Site	162	1	Essential for DHBP synthase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7GSD5-1 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: A4B48A68EC6A685F	FASTA	397	44,315
	10 20 30 40 50 60 MFHRIEEALE DLKQGKVIIV CDDKNRENEG DFLALAEYIT PETINFMITH GRGLVCVPLP 70 80 90 100 110 120 EHYAKRLQLE PMVSQNTDSH HTAFTVSIDH ISTTTGISAH ERATTVRELL NPSSKGSDFN 130 140 150 160 170 180 RPGHIFPLIA KDGGVLRRAG HTEAAVDLAK LCGTEPVGVI CEIIKEDGTM ARVPDLIQVA 190 200 210 220 230 240 KQFDIKMITI EDLIAYRRHH ETFVTKEVEI TLPTEFGTFH AIGYTNSLDQ KEHIALIKGD 250 260 270 280 290 300 VSTDEPVLVR VHSECLTGDV FGSCRCDCGP QLHAALTQIE REGRGVLLYM RQEGRGIGLL 310 320 330 340 350 360 NKLRAYKLQE EGLDTVEANE KLGFPADLRD YGIGAQILKD LGLQKLRLLT NNPRKIAGLQ 370 380 390 GYELEIVERV PLQMPTKQEN KTYLQTKVTK LGHLLNL

References

[1]

"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000764 Genomic DNA. Translation: ABS23043.1.
RefSeq	YP_001376038.1.
3D structure databases
SMR	A7GSD5. Positions 1-199, 204-373.
ModBase	Search...
Protein-protein interaction databases
STRING	A7GSD5.
Genome annotation databases
GeneID	5343864.
GenomeReviews	Gene locus Bcer98_2810 in contig CP000764_GR.
KEGG	bcy:Bcer98_2810.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0108.
HOGENOM	HBG735778.
OMA	LRCDCRM.
Family and domain databases
HAMAP	MF_01283. RibBA. [Tree]
InterPro	IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR000422. DHBP_synthase_RibB. IPR000926. GTP_CycHdrlase_II. IPR016299. Riboflavin_synth_RibA. [Graphical view]
Gene3D	G3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
Pfam	PF00926. DHBP_synthase. 1 hit. PF00925. GTP_cyclohydro2. 1 hit. [Graphical view]
PIRSF	PIRSF001259. RibA. 1 hit.
TIGRFAMs	TIGR00505. ribA. 1 hit. TIGR00506. ribB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RIBBA_BACCN

Accession

Primary (citable) accession number: A7GSD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 11, 2007
Last modified:	February 9, 2010
This is version 23 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)