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C1B4K9 (C1B4K9_RHOOB) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Riboflavin biosynthesis protein RibBA HAMAP-Rule MF_01283
Gene names
Name:ribA EMBL BAH55198.1
Synonyms:ribBA HAMAP-Rule MF_01283
Ordered Locus Names:ROP_69510 EMBL BAH55198.1
OrganismRhodococcus opacus (strain B4) [Complete proteome] [HAMAP] EMBL BAH55198.1
Taxonomic identifier632772 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length417 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. SAAS SAAS000422 HAMAP-Rule MF_01283

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity. SAAS SAAS000422 HAMAP-Rule MF_01283

Catalytic activity

D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP-Rule MF_01283

GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. SAAS SAAS016299 HAMAP-Rule MF_01283

Cofactor

Binds 1 zinc ion per subunit By similarity. SAAS SAAS016299 HAMAP-Rule MF_01283

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity. HAMAP-Rule MF_01283

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP-Rule MF_01283

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. SAAS SAAS016299 HAMAP-Rule MF_01283

Sequence similarities

In the C-terminal section; belongs to the GTP cyclohydrolase II family. HAMAP-Rule MF_01283

In the N-terminal section; belongs to the DHBP synthase family. HAMAP-Rule MF_01283

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding259 – 2635GTP By similarity HAMAP-Rule MF_01283
Nucleotide binding303 – 3053GTP By similarity HAMAP-Rule MF_01283
Region1 – 204204DHBP synthase By similarity HAMAP-Rule MF_01283
Region28 – 292D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region141 – 1455D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region205 – 417213GTP cyclohydrolase II By similarity HAMAP-Rule MF_01283

Sites

Active site3371Proton acceptor; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Active site3391Nucleophile; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Metal binding291Magnesium or manganese 1 By similarity HAMAP-Rule MF_01283
Metal binding291Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding1441Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding2641Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2751Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2771Zinc; catalytic By similarity HAMAP-Rule MF_01283
Binding site331D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site1651D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site2801GTP By similarity HAMAP-Rule MF_01283
Binding site3251GTP By similarity HAMAP-Rule MF_01283
Binding site3601GTP By similarity HAMAP-Rule MF_01283
Binding site3651GTP By similarity HAMAP-Rule MF_01283
Site1271Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283
Site1651Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283

Sequences

Sequence LengthMass (Da)Tools
C1B4K9 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 96C9BD0ECEC2F875

FASTA41745,184
        10         20         30         40         50         60 
MTRFDTIERA VADIAAGKAV VVVDDEDREN EGDLIFAAEK ATPELVAFMV RYTSGYLCVP 

        70         80         90        100        110        120 
LDGADCDRLG LPPMYATNQD KHGTAYTVTV DAREGIGTGI SASDRAATMR LLADPSSGAQ 

       130        140        150        160        170        180 
DFTRPGHVVP LRAKEGGVLR RPGHTEAAVD LARMADLRPA GVICEIVSQK DEGHMAQTDE 

       190        200        210        220        230        240 
LRVFADDHDL ALISIADLIA WRRKHEKHVE RVASARIPTR HGEFTAVGYR SIYDDVEHVA 

       250        260        270        280        290        300 
LVRGDLPGPD GDGSDVLVRV HSECLTGDVF GSLRCDCGPQ LDAALDMVAQ EGRGVVLYMR 

       310        320        330        340        350        360 
GHEGRGIGLM HKLQAYQLQD AGSDTVDANL ELGLPADARD YGIGAQILVD LGISSMRLLT 

       370        380        390        400        410 
NNPAKRVGLD GYGLQITERV SMPLRANAEN LTYLRTKRDR MGHDLIGLDD FEAGEML 

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References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B4 EMBL BAH55198.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP011115 Genomic DNA. Translation: BAH55198.1.
RefSeqYP_002784143.1. NC_012522.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING632772.ROP_69510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH55198; BAH55198; ROP_69510.
GeneID7744531.
KEGGrop:ROP_69510.
PATRIC23231355. VBIRhoOpa21106_7036.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
HOGENOMHOG000115440.
KOK14652.
OMALMVDRNT.
OrthoDBEOG679TK8.
ProtClustDBPRK09311.

Enzyme and pathway databases

BioCycROPA632772:GH0Q-7007-MONOMER.
UniPathwayUPA00275; UER00399.
UPA00275; UER00400.

Family and domain databases

Gene3D3.90.870.10. 1 hit.
HAMAPMF_00179. RibA.
MF_00180. RibB.
MF_01283. RibBA.
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlaseII_RibA.
IPR016299. Riboflavin_synth_RibBA.
[Graphical view]
PfamPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFPIRSF001259. RibA. 1 hit.
SUPFAMSSF55821. SSF55821. 1 hit.
TIGRFAMsTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC1B4K9_RHOOB
AccessionPrimary (citable) accession number: C1B4K9
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)