Skip Header

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

Q8NQ52 (RIBBA_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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
Ordered Locus Names:Cgl1595, cg1798
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [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_1000067422

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
Q8NQ52 [UniParc].

Last modified October 1, 2002. 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

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000036 Genomic DNA. Translation: BAB98988.1.
BX927152 Genomic DNA. Translation: CAF21603.1.
RefSeqNP_600809.1. NC_003450.3.
YP_225879.1. NC_006958.1.

3D structure databases

HSSPHSSP built from PDB template 2BZ0 based on UniProtKB P0A7I7.
ProteinModelPortalQ8NQ52.
SMRQ8NQ52. Positions 10-210.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019563.
3343515.
GenomeReviewsGene locus Cgl1595 in contig BA000036_GR.
Gene locus cg1798 in contig BX927147_GR.
KEGGcgb:cg1798.
cgl:NCgl1533.
PATRIC21495227. VBICorGlu203724_1557.

Phylogenomic databases

HOGENOMHBG735778.
OMARCDCRMQ.
PhylomeDBQ8NQ52.
ProtClustDBPRK09311.

Enzyme and pathway databases

BioCycCGLU196627:CG1798-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_CORGL
AccessionPrimary (citable) accession number: Q8NQ52
Secondary accession number(s): Q6M505
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 64 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