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E8USW7 (E8USW7_THEBF) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 19. Feed History...

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

Sequence length396 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 binding249 – 2535GTP By similarity HAMAP-Rule MF_01283
Nucleotide binding291 – 2933GTP By similarity HAMAP-Rule MF_01283
Region1 – 199199DHBP synthase By similarity HAMAP-Rule MF_01283
Region26 – 272D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region138 – 1425D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region200 – 396197GTP cyclohydrolase II By similarity HAMAP-Rule MF_01283

Sites

Active site3251Proton acceptor; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Active site3271Nucleophile; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Metal binding271Magnesium or manganese 1 By similarity HAMAP-Rule MF_01283
Metal binding271Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding1411Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding2541Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2651Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2671Zinc; catalytic By similarity HAMAP-Rule MF_01283
Binding site311D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site1621D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site2701GTP By similarity HAMAP-Rule MF_01283
Binding site3131GTP By similarity HAMAP-Rule MF_01283
Binding site3481GTP By similarity HAMAP-Rule MF_01283
Binding site3531GTP By similarity HAMAP-Rule MF_01283
Site1241Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283
Site1621Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283

Sequences

Sequence LengthMass (Da)Tools
E8USW7 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 089B2F43178A8D60

FASTA39644,558
        10         20         30         40         50         60 
MFDRIEDAIE DIKQGKMIIV VDDENRENEG DLVMAAEKVT GEHINFMIKY GRGLVCVPMT 

        70         80         90        100        110        120 
EKRLNELGIY QMVENNTDHK ETAFTVSVDY KECTTGISAF ERALTVKKLV DDNSKPEDFT 

       130        140        150        160        170        180 
KPGHIFPLRA KDGGVLVRAG HTEAAVDLAV LAGLKPAGVI CEIIKDDGNM ARLPDLLEFA 

       190        200        210        220        230        240 
KKFGLRIISI EDLIKYRMKN EILVRRVAQA KLPTKYGNFE IVGYEEILTR KQHVALIKGD 

       250        260        270        280        290        300 
INKEPVLVRI HSECLTGDIL GSLRCDCGDQ LHAAMERIGQ EGGVLVYLRQ EGRGIGLLNK 

       310        320        330        340        350        360 
IKAYHLQDQG LDTVEANIKL GFPPDLREYS IAAQILKDIG VKKIRIMTNN PQKIMELSDY 

       370        380        390 
GLDVVERVSI EICPNHYNEK YLKTKKERMG HLILEV 

« Hide

References

[1]"Complete sequence of Thermoanaerobacter brockii finnii Ako-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.
Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43586 / DSM 3389 / AKO-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002466 Genomic DNA. Translation: ADV78655.1.
RefSeqYP_004185038.1. NC_014964.1.

3D structure databases

ProteinModelPortalE8USW7.
SMRE8USW7. Positions 1-199, 203-372.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADV78655; ADV78655; Thebr_0023.
GeneID10162249.
KEGGtbo:Thebr_0023.
PATRIC47037878. VBITheBro57020_0025.

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 nameE8USW7_THEBF
AccessionPrimary (citable) accession number: E8USW7
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)