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Q6MCT5 (Q6MCT5_PARUW) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Riboflavin biosynthesis protein RibBA HAMAP-Rule MF_01283
Gene names
Name:ribA EMBL CAF23614.1
Synonyms:ribBA HAMAP-Rule MF_01283
Ordered Locus Names:pc0890
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP] EMBL CAF23614.1
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Parachlamydiaceae › Candidatus Protochlamydia ›

Protein attributes

Sequence length412 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-Rule MF_01283 SAAS SAAS017945

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity. HAMAP-Rule MF_01283 SAAS SAAS017945

Catalytic activity

D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP-Rule MF_01283 SAAS SAAS017945

GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. HAMAP-Rule MF_01283 SAAS SAAS017945

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01283 SAAS SAAS017945

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity. HAMAP-Rule MF_01283 SAAS SAAS017945

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP-Rule MF_01283 SAAS SAAS017945

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. HAMAP-Rule MF_01283 SAAS SAAS017945

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 binding253 – 2575GTP By similarity HAMAP-Rule MF_01283
Nucleotide binding297 – 2993GTP By similarity HAMAP-Rule MF_01283
Region1 – 202202DHBP synthase By similarity HAMAP-Rule MF_01283
Region27 – 282D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region141 – 1455D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region203 – 412210GTP cyclohydrolase II By similarity HAMAP-Rule MF_01283

Sites

Active site3311Proton acceptor; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Active site3331Nucleophile; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Metal binding281Magnesium or manganese 1 By similarity HAMAP-Rule MF_01283
Metal binding281Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding1441Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding2581Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2691Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2711Zinc; catalytic By similarity HAMAP-Rule MF_01283
Binding site321D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site1651D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site2741GTP By similarity HAMAP-Rule MF_01283
Binding site3191GTP By similarity HAMAP-Rule MF_01283
Binding site3541GTP By similarity HAMAP-Rule MF_01283
Binding site3591GTP 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
Q6MCT5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5D48E399C35CF8B0

FASTA41246,075
        10         20         30         40         50         60 
MKTYRLEDAL LALKEGKFVI VVDDENRENE GDLILAAEKA HPSSLGFMIR HTTGIICLAM 

        70         80         90        100        110        120 
KGQRLDELKL PPMVTDNTDR KQTAFTVSVD YLHQGVTTGV SAEDRTKTIL SLIHPHTKPE 

       130        140        150        160        170        180 
DLGRPGHIFP LRYKEGGVLK RAGHTEAAVD LTNLAKLYPA GILAELINED GSMMRLPELE 

       190        200        210        220        230        240 
KFSDLHQIPI ITIAELIRFR RRHEKLVSCF SQSPIPTPFG DFNAYVYESQ LDGIQHIALV 

       250        260        270        280        290        300 
KGEIKNQKNI LVRMHSECLT GDVFGSKRCD CGSQLKLAME KIEQEGRGVI IYLRGHEGRG 

       310        320        330        340        350        360 
IGIGHKLKAY NLQDQGKDTL EANLELGFPI DSREYGIGAQ ILVDLGLSTI RLMTNNLAKY 

       370        380        390        400        410 
NGLAGYDLEI TERVPLPVCV TKENKHYLQT KKDKLGHLID LSEDKLEIHH ST

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References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UWE25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX908798 Genomic DNA. Translation: CAF23614.1.
RefSeqYP_007889.1. NC_005861.1.

3D structure databases

HSSPHSSP built from PDB template 1K49 based on UniProtKB Q8TG90.
ProteinModelPortalQ6MCT5.
ModBaseSearch...

Protein-protein interaction databases

STRING264201.pc0890.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF23614; CAF23614; pc0890.
GeneID2780041.
KEGGpcu:pc0890.
PATRIC31997129. VBICanPro72727_0904.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
HOGENOMHOG000115440.
KOK14652.
OMANIDPFIS.
ProtClustDBCLSK2762285.

Enzyme and pathway databases

BioCycPAMO264201:GH0M-891-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. DHBP_synth_RibB-like_a/b_dom. 1 hit.
TIGRFAMsTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ6MCT5_PARUW
AccessionPrimary (citable) accession number: Q6MCT5
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info