Skip Header

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

O66679 (RIBBA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. 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
Synonyms:ribA
Ordered Locus Names:aq_350
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length406 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 – 406406Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_0000151719

Regions

Nucleotide binding260 – 2645GTP By similarity
Nucleotide binding304 – 3063GTP By similarity
Region1 – 209209DHBP synthase HAMAP MF_01283
Region33 – 342D-ribulose 5-phosphate binding By similarity
Region148 – 1525D-ribulose 5-phosphate binding By similarity
Region210 – 406197GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3381Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3401Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding341Magnesium or manganese 1 By similarity
Metal binding341Magnesium or manganese 2 By similarity
Metal binding1511Magnesium or manganese 2 By similarity
Metal binding2651Zinc; catalytic By similarity
Metal binding2761Zinc; catalytic By similarity
Metal binding2781Zinc; catalytic By similarity
Binding site381D-ribulose 5-phosphate By similarity
Binding site1721D-ribulose 5-phosphate By similarity
Binding site2811GTP By similarity
Binding site3261GTP By similarity
Binding site3611GTP By similarity
Binding site3661GTP By similarity
Site1341Essential for DHBP synthase activity By similarity
Site1721Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
O66679 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 9C5B54539B1C2645

FASTA40645,577
        10         20         30         40         50         60 
MSEREEFKFN TVEEAIEDIR QGKMVIVVDD PDRENEGDLV MAAEKVTPEA INFMAKYGRG 

        70         80         90        100        110        120 
LICLSLTPER CEQLDLHPMT PMNTDPKGTY FCVSIDAHPK HGTTTGISAY DRALTIKLAI 

       130        140        150        160        170        180 
SPDAKPSDFV RPGHVFPLKA RPGGVLERAG HTEASVDLAR LAGLYPAGVI CEIMKDDGTM 

       190        200        210        220        230        240 
ARVPDLMEFA KKHNLKIITI ADLIKYRLRR ETLVEKVASA HLPTPWGVFK IHAYRHKLTG 

       250        260        270        280        290        300 
EEQVALTMGE WKEDEPVLVR VHSECLTGDV FRSFRCDCRP QLEKALEMIA KEGKGVLVYI 

       310        320        330        340        350        360 
LGHEGRGIGI ANKIKAYELQ EKGYDTVEAN EKLGYPPDLR DYGIGAQILR DLGVRKMKLM 

       370        380        390        400 
TNNPRKIVAL EGFGLEVVER VPIKIEPNPY NKIYLQVKKD KLGHMF

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC06638.1.
PIRC70331.
RefSeqNP_213239.1. NC_000918.1.

3D structure databases

ProteinModelPortalO66679.
SMRO66679. Positions 8-211.
ModBaseSearch...

Proteomic databases

PRIDEO66679.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193005.
GenomeReviewsGene locus aq_350 in contig AE000657_GR.
KEGGaae:aq_350.
NMPDRfig|224324.1.peg.254.
PATRIC20958294. VBIAquAeo85532_0283.

Phylogenomic databases

HOGENOMHBG735778.
OMARCDCRMQ.
PhylomeDBO66679.
ProtClustDBCLSK2299371.

Enzyme and pathway databases

BioCycAAEO224324:AQ_350-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_AQUAE
AccessionPrimary (citable) accession number: O66679
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 81 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