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D5URV9 (D5URV9_TSUPD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length415 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 binding257 – 2615GTP By similarity HAMAP-Rule MF_01283
Nucleotide binding301 – 3033GTP 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 – 415211GTP cyclohydrolase II By similarity HAMAP-Rule MF_01283

Sites

Active site3351Proton acceptor; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Active site3371Nucleophile; 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 binding2621Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2731Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2751Zinc; 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 site2781GTP By similarity HAMAP-Rule MF_01283
Binding site3231GTP By similarity HAMAP-Rule MF_01283
Binding site3581GTP By similarity HAMAP-Rule MF_01283
Binding site3631GTP 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
D5URV9 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: 0C74C151BEB9177D

FASTA41544,515
        10         20         30         40         50         60 
MTRFDSIERA IEDIAAGKAV VVVDDEDREN EGDLIFAAEK ATPELVAFMV RYTSGYLCVP 

        70         80         90        100        110        120 
LDGATCDKLG LPPMYATNQD KHGTAYTVTV DAKAGVGTGI SAADRATTML KLADPDSTVD 

       130        140        150        160        170        180 
DFTRPGHVVP LRAKEGGVLR RPGHTEAAVD LATMAGLAPA GVICEIVSEK DPGGMAQTDE 

       190        200        210        220        230        240 
LRVFADDHDL ALISIADLIA WRRKHEKHVV QVASARIPTA HGDFQAVGYT SIHDDVEHVA 

       250        260        270        280        290        300 
LVKGDITADG GADVLVRVHS ECLTGDVFGS LRCDCGPQLD AAMEMVAQEG RGVVLYMRGH 

       310        320        330        340        350        360 
EGRGIGLMHK LQAYQLQDGG ADTVDANLQL GLPADARDYG LGAQILVDLG ITSMRLLTNN 

       370        380        390        400        410 
PAKRVGLDGY GLQITERVPM PLRANAENIH YLRTKRDRMG HDMRDLDHFD QGGTA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001966 Genomic DNA. Translation: ADG79164.1.
RefSeqYP_003647503.1. NC_014158.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADG79164; ADG79164; Tpau_2561.
GeneID9156722.
KEGGtpr:Tpau_2561.
PATRIC38308431. VBITsuPau718_2561.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000115440.
KOK14652.

Enzyme and pathway databases

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 nameD5URV9_TSUPD
AccessionPrimary (citable) accession number: D5URV9
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: May 1, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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