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Q9Z734 (RIBBA_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. 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

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:CPn_0872, CP_0997, CpB0901
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length418 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 – 418418Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_0000151724

Regions

Nucleotide binding262 – 2665GTP By similarity
Nucleotide binding306 – 3083GTP By similarity
Region1 – 211211DHBP synthase HAMAP MF_01283
Region37 – 382D-ribulose 5-phosphate binding By similarity
Region150 – 1545D-ribulose 5-phosphate binding By similarity
Region212 – 418207GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3401Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3421Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding381Magnesium or manganese 1 By similarity
Metal binding381Magnesium or manganese 2 By similarity
Metal binding1531Magnesium or manganese 2 By similarity
Metal binding2671Zinc; catalytic By similarity
Metal binding2781Zinc; catalytic By similarity
Metal binding2801Zinc; catalytic By similarity
Binding site421D-ribulose 5-phosphate By similarity
Binding site1741D-ribulose 5-phosphate By similarity
Binding site2831GTP By similarity
Binding site3281GTP By similarity
Binding site3631GTP By similarity
Binding site3681GTP By similarity
Site1361Essential for DHBP synthase activity By similarity
Site1741Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z734 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 7A5A214BB0EC0E32

FASTA41845,846
        10         20         30         40         50         60 
MIETREEVGS ANFVSLERAI EDLRAGKFVI VVDEASREDE GDLIIAGEKI TVEKMTFLLQ 

        70         80         90        100        110        120 
HTTGVVCAAL SQERLLSLDL PPMVKDNRCR FKTPFTVSVD AAHGVTTGVS AADRTKVVQL 

       130        140        150        160        170        180 
LADPKSKPED FISPGHFFPL ASSPGGVLKR AGHTESTVDL MELAGLQPCG VLAELVNEDY 

       190        200        210        220        230        240 
SMMRLPQILE FARKHNIAVI PVTSIIAHRM LSDRLVSKIS SARLPTIYGD FTIHVYESLL 

       250        260        270        280        290        300 
EGMQHLALVK GNVAGKSNVL VRVHSECVTG DILGSKRCDC GEQLSSAMSY IAEKGTGVLV 

       310        320        330        340        350        360 
YLRGQEGRGI GLGHKVRAYA LQDNGYDTVD ANLAMGFPVD SREYGIGAQI LVDLKLTTIK 

       370        380        390        400        410 
LITHNPQKYF GLQGFGLSIT ERVPLPVRIS EDNEQYLRTK QERMGHWLDL PCCNNRVQ 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed: 10192388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed: 10871362] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD19010.1.
AE002161 Genomic DNA. Translation: AAF38775.1.
BA000008 Genomic DNA. Translation: BAA99080.1.
AE009440 Genomic DNA. Translation: AAP98830.1.
PIRF86599.
H72026.
RefSeqNP_225067.1. NC_000922.1.
NP_300929.1. NC_002491.1.
NP_445534.1. NC_002179.2.
NP_877173.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z734.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1467580.
895694.
919635.
963470.
GenomeReviewsGene locus CPn_0872 in contig AE001363_GR.
Gene locus CP_0997 in contig AE002161_GR.
Gene locus CpB0901 in contig AE009440_GR.
Gene locus ribBA in contig BA000008_GR.
KEGGcpa:CP0997.
cpn:CPn0872.
cpt:CpB0901.
TIGRCP_0997.

Phylogenomic databases

HOGENOMHBG735778.
OMARCDCRMQ.
ProtClustDBPRK09311.

Enzyme and pathway databases

BioCycCPNE115711:CP_0997-MONOMER.
CPNE115713:CPN0872-MONOMER.
CPNE138677:CPJ0872-MONOMER.
CPNE182082:CPB0901-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_CHLPN
AccessionPrimary (citable) accession number: Q9Z734
Secondary accession number(s): Q9JQ68
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 85 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