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O84736 (RIBBA_CHLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. 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
Synonyms:ribA/ribB
Ordered Locus Names:CT_731
OrganismChlamydia trachomatis
Taxonomic identifier813 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length424 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 – 424424Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_0000151725

Regions

Nucleotide binding257 – 2615GTP By similarity
Nucleotide binding301 – 3033GTP By similarity
Region1 – 206206DHBP synthase HAMAP MF_01283
Region32 – 332D-ribulose 5-phosphate binding By similarity
Region145 – 1495D-ribulose 5-phosphate binding By similarity
Region207 – 424218GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3351Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3371Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding331Magnesium or manganese 1 By similarity
Metal binding331Magnesium or manganese 2 By similarity
Metal binding1481Magnesium or manganese 2 By similarity
Metal binding2621Zinc; catalytic By similarity
Metal binding2731Zinc; catalytic By similarity
Metal binding2751Zinc; catalytic By similarity
Binding site371D-ribulose 5-phosphate By similarity
Binding site1691D-ribulose 5-phosphate By similarity
Binding site2781GTP By similarity
Binding site3231GTP By similarity
Binding site3581GTP By similarity
Binding site3631GTP By similarity
Site1311Essential for DHBP synthase activity By similarity
Site1691Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
O84736 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D9576054927CBAE0

FASTA42446,675
        10         20         30         40         50         60 
MFTCEAGIAS VQQAIKDVAE GKFVIVIDAA SRENEGDLIL AGEKVSTEKM SFLLSHTTGI 

        70         80         90        100        110        120 
VCASLSREQA KSLDLPAMVQ DNQCAFKTAF TVSVDASSGV TTGVSASDRT RTVQLLADPA 

       130        140        150        160        170        180 
ATAESFVRPG HVFPLISQPG GAVQRPGHTE AAMDLMRLAG MQPCGIFAEL VNPDHSMMRQ 

       190        200        210        220        230        240 
QQVLAFAEQH DLTVITVDDL ITYRYTYDSL VTKISSARLP TKYGDFSIHV YESIIDGTQH 

       250        260        270        280        290        300 
FALVKGDIHE QEAVPVRVHS ECLTGDILGS CRCDCGAQLD MAMRYIAEEG LGVIVYLRGQ 

       310        320        330        340        350        360 
EGRGIGFGHK IRAYALQDLG YDTVDANLQL GFPIDAREYG MAAQVLKDLQ LTSVRLITHN 

       370        380        390        400        410        420 
PRKFFELQRL GIHVLDRIIL PVSISTENEG YLRTKKERMG HWLDLPVLDD VEEEYETVER 


MSCR

« Hide

References

[1]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed: 9784136] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001273 Genomic DNA. Translation: AAC68326.1.
PIRB71477.
RefSeqNP_220250.1. NC_000117.1.

3D structure databases

ProteinModelPortalO84736.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID884521.
GenomeReviewsGene locus CT_731 in contig AE001273_GR.
KEGGctr:CT731.
PATRIC20381134. VBIChlTra43535_0804.

Phylogenomic databases

HOGENOMHBG735778.
OMARCDCRMQ.
PhylomeDBO84736.
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_CHLTR
AccessionPrimary (citable) accession number: O84736
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: January 25, 2012
This is version 76 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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