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Reviewed, UniProtKB/Swiss-Prot B1H0I0 (RIBBA_UNCTG)

Last modified November 3, 2009. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: TGRD_529
OrganismUncultured termite group 1 bacterium phylotype Rs-D17 [Complete proteome] [HAMAP]
Taxonomic identifier471821 [NCBI]
Taxonomic lineageBacteriaElusimicrobiaenvironmental samples

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity.

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.

Binds 1 zinc ion per subunit By similarity.

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 – 403403Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_1000140369

Regions

Nucleotide binding255 – 2595GTP By similarity
Nucleotide binding298 – 3003GTP By similarity
Region1 – 204204DHBP synthase HAMAP MF_01283
Region30 – 312D-ribulose 5-phosphate binding By similarity
Region143 – 1475D-ribulose 5-phosphate binding By similarity
Region205 – 403199GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3321Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3341Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding311Magnesium or manganese 1 By similarity
Metal binding311Magnesium or manganese 2 By similarity
Metal binding1461Magnesium or manganese 2 By similarity
Metal binding2601Zinc; catalytic By similarity
Metal binding2711Zinc; catalytic By similarity
Metal binding2731Zinc; catalytic By similarity
Binding site351D-ribulose 5-phosphate By similarity
Binding site1671D-ribulose 5-phosphate By similarity
Binding site2761GTP By similarity
Binding site3201GTP By similarity
Binding site3551GTP By similarity
Binding site3601GTP By similarity
Site1291Essential for DHBP synthase activity By similarity
Site1671Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B1H0I0-1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 9FF1E288DA7226B2

FASTA40344,853
        10         20         30         40         50         60 
MKNKVFASIG DAVKDIKVGR MVIVVDDPGR ENEGDLICAA EKASPEVINF MTKYARGLIC 

        70         80         90        100        110        120 
VPMKHERLKE LEIENMVEKP TEKKGCSFTV SVDYKIGTTT GISAYDRSVT VRKLIDKTAK 

       130        140        150        160        170        180 
HEDFARPGHI FPLRCKEGGV LARTGHTEAA VDLVRLAGFY PAGIICEIMN NDGTMARMSD 

       190        200        210        220        230        240 
LIKFAKKHDL HIITIGELVN YRRRTEKFIS EIVNVDLPTR YGDFKLVLFE DLITKDSHIA 

       250        260        270        280        290        300 
VVKGVVKNRQ NVLVRVHSSC ETGDIFHSLR CDCGDQLETA LKAVGEAEQG VVLYIHQEGR 

       310        320        330        340        350        360 
GIGLANKLKA YRLQEKGMDT VEANKALGFD PDLRDYGIGA QMLSELGIKS INLMTNNPGK 

       370        380        390        400 
INGLESYGLK ITKRVPLEIS PSKSNEKYLK TKKEKMGHML KKV 

« Hide

References

[1]"Complete genome of the uncultured termite group 1 bacteria in a single host protist cell."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008) [PubMed: 18391199] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP009510 Genomic DNA. Translation: BAG14012.1.
RefSeqYP_001956473.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6373331.
GenomeReviewsGene locus TGRD_529 in contig AP009510_GR.
KEGGrsd:TGRD_529.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAHTEASLE.

Family and domain databases

HAMAPMF_01283.
[Tree]
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlase_II.
IPR016299. Riboflavin_synth_RibA.
[Graphical view]
Gene3DG3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
PfamPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFPIRSF001259. RibA. 1 hit.
ProDomPD003034. DHBP_synthase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBBA_UNCTG
AccessionPrimary (citable) accession number: B1H0I0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: November 3, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents