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C7LSH6 (C7LSH6_DESBD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 31. Feed History...

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

Sequence length404 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. SAAS SAAS000422 HAMAP-Rule MF_01283

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity. SAAS SAAS000422 HAMAP-Rule MF_01283

Catalytic activity

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

GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. SAAS SAAS016299 HAMAP-Rule MF_01283

Cofactor

Binds 1 zinc ion per subunit By similarity. SAAS SAAS016299 HAMAP-Rule MF_01283

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

Pathway

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

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. SAAS SAAS016299 HAMAP-Rule MF_01283

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 binding252 – 2565GTP By similarity HAMAP-Rule MF_01283
Nucleotide binding295 – 2973GTP By similarity HAMAP-Rule MF_01283
Region1 – 201201DHBP synthase By similarity HAMAP-Rule MF_01283
Region27 – 282D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region202 – 404203GTP cyclohydrolase II By similarity HAMAP-Rule MF_01283

Sites

Active site3291Proton acceptor; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Active site3311Nucleophile; 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 binding2571Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2681Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2701Zinc; catalytic By similarity HAMAP-Rule MF_01283
Binding site321D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site1641D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site2731GTP By similarity HAMAP-Rule MF_01283
Binding site3171GTP By similarity HAMAP-Rule MF_01283
Binding site3521GTP By similarity HAMAP-Rule MF_01283
Binding site3571GTP By similarity HAMAP-Rule MF_01283
Site1261Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283
Site1641Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283

Sequences

Sequence LengthMass (Da)Tools
C7LSH6 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: D4CB39048F1F5266

FASTA40444,379
        10         20         30         40         50         60 
MHKCSAEEAI KEIKAGKMII LVDDEDRENE GDLTIAAEMV TPEAINFMAK YGRGLICLAL 

        70         80         90        100        110        120 
EPALVDKLEL PLMARRNTSK FGTNFTVSIE AKQGVTTGIS AHDRALTIQT AVADQTTPED 

       130        140        150        160        170        180 
LATPGHIFPL RAKPGGVLVR AGQTEGSVDL ARLAGLKGAA VICEIMNDDG SMSRMPDLRK 

       190        200        210        220        230        240 
FAEEHDMKIA TIADLIAYRS RKDSLVRRVA EARMPTCYGE FTIVAYENDI DSHTHIALVK 

       250        260        270        280        290        300 
GEINEETPVL VRVHSECLTG DVFGSMRCDC GSQLQRAMQM VNDEGAGVIL YMRQEGRGIG 

       310        320        330        340        350        360 
LGNKIKAYHL QDEGRDTVEA NLELGFAPDL RDYGLGAQIL VDLGVKRMRL LTNNPKKIIG 

       370        380        390        400 
LEGYGLKVEE RISIEIPACD DNKCYLHTKH SKLGHLLQFE AENK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001629 Genomic DNA. Translation: ACU88190.1.
RefSeqYP_003156606.1. NC_013173.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING525897.Dbac_0060.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACU88190; ACU88190; Dbac_0060.
GeneID8375693.
KEGGdba:Dbac_0060.
PATRIC21702370. VBIDesBac69216_0058.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
HOGENOMHOG000115440.
KOK14652.
OMALMVDRNT.
OrthoDBEOG679TK8.
ProtClustDBCLSK2556023.

Enzyme and pathway databases

BioCycDBAC525897:GI50-62-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. SSF55821. 1 hit.
TIGRFAMsTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC7LSH6_DESBD
AccessionPrimary (citable) accession number: C7LSH6
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: February 19, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)