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Reviewed, UniProtKB/Swiss-Prot P47924 (RIBBA_ARATH)

Last modified November 3, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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, chloroplastic
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
Synonyms: RIBA
Ordered Locus Names: At5g64300
ORF Names: MSJ1.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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.

GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate.

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.

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.

Subcellular location

Plastidchloroplast Potential.

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

Transit peptide1 – 5656Chloroplast Potential
Chain57 – 543487Riboflavin biosynthesis protein ribBA, chloroplastic
PRO_0000030436

Regions

Nucleotide binding379 – 3835GTP By similarity
Nucleotide binding423 – 4253GTP By similarity
Region57 – 328272DHBP synthase
Region152 – 1532D-ribulose 5-phosphate binding By similarity
Region267 – 2715D-ribulose 5-phosphate binding By similarity
Region329 – 543215GTP cyclohydrolase II

Sites

Active site4571Proton acceptor; for GTP cyclohydrolase activity Potential
Active site4591Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding1531Magnesium or manganese 1 By similarity
Metal binding1531Magnesium or manganese 2 By similarity
Metal binding2701Magnesium or manganese 2 By similarity
Metal binding3841Zinc; catalytic By similarity
Metal binding3951Zinc; catalytic By similarity
Metal binding3971Zinc; catalytic By similarity
Binding site1571D-ribulose 5-phosphate By similarity
Binding site2911D-ribulose 5-phosphate By similarity
Binding site4001GTP By similarity
Binding site4451GTP By similarity
Binding site4801GTP By similarity
Binding site4851GTP By similarity
Site2531Essential for DHBP synthase activity By similarity
Site2911Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P47924-1 [UniParc].

Last modified January 10, 2003. Version 2.
Checksum: 31D89A500E42BF81

FASTA54359,056
        10         20         30         40         50         60 
MSSINLSSSS PSTISLSRSR LSQSSTTLLH GLHRVTLPSN HPLSTFSIKT NTGKVKAAVI 

        70         80         90        100        110        120 
SREDDLLSFT NGNTPLSNGS LIDDRTEEPL EADSVSLGTL AADSAPAPAN GFVAEDDDFE 

       130        140        150        160        170        180 
LDLPTPGFSS IPEAIEDIRQ GKLVVVVDDE DRENEGDLVM AAQLATPEAM AFIVRHGTGI 

       190        200        210        220        230        240 
VCVSMKEDDL ERLHLPLMVN QKENEEKLST AFTVTVDAKH GTTTGVSARD RATTILSLAS 

       250        260        270        280        290        300 
RDSKPEDFNR PGHIFPLKYR EGGVLKRAGH TEASVDLTVL AGLDPVGVLC EIVDDDGSMA 

       310        320        330        340        350        360 
RLPKLREFAA ENNLKVVSIA DLIRYRRKRD KLVERASAAR IPTMWGPFTA YCYRSILDGI 

       370        380        390        400        410        420 
EHIAMVKGEI GDGQDILVRV HSECLTGDIF GSARCDCGNQ LALSMQQIEA TGRGVLVYLR 

       430        440        450        460        470        480 
GHEGRGIGLG HKLRAYNLQD AGRDTVEANE ELGLPVDSRE YGIGAQIIRD LGVRTMKLMT 

       490        500        510        520        530        540 
NNPAKYVGLK GYGLAIVGRV PLLSLITKEN KRYLETKRTK MGHMYGLKFK GDVVEKIESE 


SES 

« Hide

References

« Hide 'large scale' references
[1]"Biosynthesis of riboflavin in plants. The ribA gene of Arabidopsis thaliana specifies a bifunctional GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase."
Herz S.W., Eberhardt S., Bacher A.
Phytochemistry 53:723-731(2000) [PubMed: 10783978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
DNA Res. 4:401-414(1997) [PubMed: 9501997] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Isolation of cDNAs encoding GTP cyclohydrolase II from Arabidopsis thaliana."
Kobayashi M., Sugiyama M., Yamamoto K.
Gene 160:303-304(1995) [PubMed: 7642114] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 279-543.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ000053 Genomic DNA. Translation: CAA03884.1.
AB008268 Genomic DNA. Translation: BAB09861.1.
D45165 mRNA. Translation: BAA08113.1. Different initiation.
IPIIPI00522822.
PIRJC4209.
RefSeqNP_201235.4.
UniGeneAt.49217

3D structure databases

HSSPHSSP built from PDB template 1G58 based on UniProtKB P24199.
ModBaseSearch...

Protein-protein interaction databases

STRINGP47924.

Proteomic databases

PRIDEP47924.

Genome annotation databases

GeneID836551.
GenomeReviewsGene locus AT5G64300 in contig BA000015_GR.
KEGGath:AT5G64300.

Organism-specific databases

GeneFarm2299. 254.
TAIRAt5g64300.

Phylogenomic databases

OMALRCDCRM.

Enzyme and pathway databases

BRENDA3.5.4.25. 302.
4.1.99.12. 302.

Gene expression databases

ArrayExpressP47924.
GenevestigatorP47924.
GermOnlineAT5G64300. Arabidopsis thaliana.

Family and domain databases

InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlase_II.
[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]
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_ARATH
AccessionPrimary (citable) accession number: P47924
Secondary accession number(s): Q9SBA8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 10, 2003
Last modified: November 3, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

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