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A0Q3H7 (RIBBA_CLONN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:NT01CX_0713
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length414 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 – 414414Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_1000073187

Regions

Nucleotide binding254 – 2585GTP By similarity
Nucleotide binding297 – 2993GTP By similarity
Region1 – 203203DHBP synthase HAMAP MF_01283
Region30 – 312D-ribulose 5-phosphate binding By similarity
Region142 – 1465D-ribulose 5-phosphate binding By similarity
Region204 – 414211GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3311Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3331Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding311Magnesium or manganese 1 By similarity
Metal binding311Magnesium or manganese 2 By similarity
Metal binding1451Magnesium or manganese 2 By similarity
Metal binding2591Zinc; catalytic By similarity
Metal binding2701Zinc; catalytic By similarity
Metal binding2721Zinc; catalytic By similarity
Binding site351D-ribulose 5-phosphate By similarity
Binding site1661D-ribulose 5-phosphate By similarity
Binding site2751GTP By similarity
Binding site3191GTP By similarity
Binding site3541GTP By similarity
Binding site3591GTP By similarity
Site1281Essential for DHBP synthase activity By similarity
Site1661Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A0Q3H7 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 79F6FA3898C24B71

FASTA41446,198
        10         20         30         40         50         60 
MEQFKFNTIE EAIEDIKNGK MVVVVDDEDR ENEGDLLMAA EKVTPEAINF MAKYARGLIC 

        70         80         90        100        110        120 
MPMTEEKLKE LDLYQMVINN TDTKETAFTV SIDSVETTTG ISAFERALTI TKAVEKGAKA 

       130        140        150        160        170        180 
KDFQRPGHIF PLRARKGGVL KRAGHTEAAV DLATLAGLTP AGTICEIMNE DGTMARVPDL 

       190        200        210        220        230        240 
MKYVKVHNLK IVTIADLIEY RRKTESFIER QGSASLPTKY GEFEIIGYED KLTGKEHVAL 

       250        260        270        280        290        300 
VKGDIKNGEP VLIRVHSECL TGDVLGSLRC DCGDQLAQAL RQINKEGRGA LLYMRQEGRG 

       310        320        330        340        350        360 
IGLINKIKAY KLQDNGMDTV DANLALGFPE DLRDYGIGAQ ILKDLGVEKV RLMTNNPKKV 

       370        380        390        400        410 
SGISGYGIEI VERVPIEIEC NKKNEFYLRT KKERMGHILN FKNIKKYDKS IKEA

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed: 17115055] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000382 Genomic DNA. Translation: ABK61746.1.
RefSeqYP_879179.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0Q3H7.
SMRA0Q3H7. Positions 5-203, 208-376.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0Q3H7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4541126.
GenomeReviewsGene locus NT01CX_0713 in contig CP000382_GR.
KEGGcno:NT01CX_0713.
PATRIC19481982. VBICloNov112828_2218.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
HOGENOMHBG735778.
OMARCDCRMQ.
ProtClustDBCLSK850058.

Enzyme and pathway databases

BioCycCNOV386415:NT01CX_0713-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_CLONN
AccessionPrimary (citable) accession number: A0Q3H7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 40 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

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