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A4QEG9 (RIBBA_CORGB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 39. 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:cgR_1643
OrganismCorynebacterium glutamicum (strain R) [Complete proteome] [HAMAP]
Taxonomic identifier340322 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length422 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 – 422422Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_1000067421

Regions

Nucleotide binding263 – 2675GTP By similarity
Nucleotide binding307 – 3093GTP By similarity
Region1 – 210210DHBP synthase HAMAP MF_01283
Region35 – 362D-ribulose 5-phosphate binding By similarity
Region147 – 1515D-ribulose 5-phosphate binding By similarity
Region211 – 422212GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3411Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3431Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding361Magnesium or manganese 1 By similarity
Metal binding361Magnesium or manganese 2 By similarity
Metal binding1501Magnesium or manganese 2 By similarity
Metal binding2681Zinc; catalytic By similarity
Metal binding2791Zinc; catalytic By similarity
Metal binding2811Zinc; catalytic By similarity
Binding site401D-ribulose 5-phosphate By similarity
Binding site1711D-ribulose 5-phosphate By similarity
Binding site2841GTP By similarity
Binding site3291GTP By similarity
Binding site3641GTP By similarity
Binding site3691GTP By similarity
Site1331Essential for DHBP synthase activity By similarity
Site1711Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A4QEG9 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 7A0F0460A1584480

FASTA42245,824
        10         20         30         40         50         60 
MSEHEQAHSQ LDSVEEAIAD IAAGKAVVVV DDEDRENEGD IIFAAELATP ELVAFMVRYS 

        70         80         90        100        110        120 
SGYICAPLTA KDADRLDLPP MTAHNQDARG TAYTVTVDAN TGTTGISATD RAHTLRLLAD 

       130        140        150        160        170        180 
PEADRTDFTR PGHVVPLRAR EGGVLVRAGH TEAAVDLARA AGLRPAGVIC EVVSEEDPTG 

       190        200        210        220        230        240 
MARVPELRRF CDEHDLKLIS IEQLIEWRRK NEILVERQVE TVLPTDFGTF KAVGYRSIID 

       250        260        270        280        290        300 
GTELVAIVAG DVASDGGENV LVRVHSECLT GDVFGSRRCD CGQQLHESLR LIQEAGRGVV 

       310        320        330        340        350        360 
VYMRGHEGRG IGLLAKLRAY QLQDEGADTV DANLALGLPA DAREFGTSAQ ILYDLGVRSL 

       370        380        390        400        410        420 
NLISNNPAKK VGLEGHGISI ASRTPIPVAV HEDNVRYLKT KRDRMGHDLP DVALWEQEHP 


EN

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References

[1]"Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
Microbiology 153:1042-1058(2007) [PubMed: 17379713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009044 Genomic DNA. Translation: BAF54635.1.
RefSeqYP_001138537.1. NC_009342.1.

3D structure databases

ProteinModelPortalA4QEG9.
SMRA4QEG9. Positions 10-210.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4QEG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4992851.
GenomeReviewsGene locus cgR_1643 in contig AP009044_GR.
KEGGcgt:cgR_1643.
PATRIC21507882. VBICorGlu58097_1692.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
HOGENOMHBG735778.
OMARCDCRMQ.
ProtClustDBPRK09311.

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_CORGB
AccessionPrimary (citable) accession number: A4QEG9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: December 14, 2011
This is version 39 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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