Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q818X6 (RIBBA_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Riboflavin biosynthesis protein ribBA

Including the following 2 domains:

  1. 3,4-dihydroxy-2-butanone 4-phosphate synthase
    Short name=DHBP synthase
    EC=4.1.99.12
  2. GTP cyclohydrolase-2
    EC=3.5.4.25
    Alternative name(s):
    GTP cyclohydrolase II
Gene names
Name:ribBA
Ordered Locus Names:BC_4111
OrganismBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceInferred 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-phospho-D-ribosylamino)pyrimidine + diphosphate. HAMAP MF_01283

Cofactor

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_1000067417

Regions

Nucleotide binding250 – 2545GTP By similarity
Nucleotide binding293 – 2953GTP By similarity
Region1 – 199199DHBP synthase HAMAP MF_01283
Region26 – 272D-ribulose 5-phosphate binding By similarity
Region138 – 1425D-ribulose 5-phosphate binding By similarity
Region200 – 397198GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3271Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3291Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding271Magnesium or manganese 1 By similarity
Metal binding271Magnesium or manganese 2 By similarity
Metal binding1411Magnesium or manganese 2 By similarity
Metal binding2551Zinc; catalytic By similarity
Metal binding2661Zinc; catalytic By similarity
Metal binding2681Zinc; catalytic By similarity
Binding site311D-ribulose 5-phosphate By similarity
Binding site1621D-ribulose 5-phosphate By similarity
Binding site2711GTP By similarity
Binding site3151GTP By similarity
Binding site3501GTP By similarity
Binding site3551GTP By similarity
Site1241Essential for DHBP synthase activity By similarity
Site1621Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q818X6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3B4071B7519E54A6

FASTA39743,886
        10         20         30         40         50         60 
MFHRIEEALE DLKKGKVVIV CDDENRENEG DFIALAEYIT PETINFMITH GRGLVCVPIT 

        70         80         90        100        110        120 
EGYAERLQLE PMVSHNTDSH HTAFTVSIDH VSTTTGISAH ERATTIQELL NPASKGADFN 

       130        140        150        160        170        180 
RPGHIFPLIA KEGGVLRRAG HTEAAVDLAK LCGAEPAGVI CEIINEDGTM ARVPDLIECA 

       190        200        210        220        230        240 
KQFDIKMITI EDLIAYRRHH ETLVTREAEI TLPTDFGTFH AIGYSNSLDT KEHIALVKGD 

       250        260        270        280        290        300 
ISTGEPVLVR VHSECLTGDV FGSHRCDCGP QLHAALAQIE REGKGVLLYM RQEGRGIGLL 

       310        320        330        340        350        360 
NKLRAYKLQE EGFDTVEANE KLGFPADLRD YGIGAQILKD LGLQSLRLLT NNPRKIAGLQ 

       370        380        390 
GYDLEVVERV PLQMPAKEEN KSYLQTKVNK LGHLLNL

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016877 Genomic DNA. Translation: AAP11030.1.
RefSeqNP_833829.1. NC_004722.1.

3D structure databases

HSSPHSSP built from PDB template 2BZ0 based on UniProtKB P0A7I7.
ProteinModelPortalQ818X6.
SMRQ818X6. Positions 204-373.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ818X6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000033401; EBBACP00000032607; EBBACG00000033392.
GeneID1206456.
GenomeReviewsGene locus BC_4111 in contig AE016877_GR.
KEGGbce:BC4111.
PATRIC32604288. VBIBacCer54481_4247.

Phylogenomic databases

eggNOGCOG0108.
GeneTreeEBGT00050000001077.
HOGENOMHBG735778.
OMARCDCRMQ.
PhylomeDBQ818X6.
ProtClustDBPRK09311.

Enzyme and pathway databases

BioCycBCER226900:BC_4111-MONOMER.

Family and domain databases

HAMAPMF_01283. RibBA.
[Tree]
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlaseII_RibA.
IPR016299. Riboflavin_synth_RibBA.
[Graphical view]
Gene3DG3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
KOK14652.
PfamPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFPIRSF001259. RibA. 1 hit.
SUPFAMSSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit.
TIGRFAMsTIGR00505. RibA. 1 hit.
TIGR00506. RibB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBBA_BACCR
AccessionPrimary (citable) accession number: Q818X6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents