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Q9X2E6 (RIBBA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:TM_1826
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length388 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 – 388388Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_0000151744

Regions

Nucleotide binding235 – 2395GTP By similarity
Nucleotide binding277 – 2793GTP By similarity
Region1 – 186186DHBP synthase HAMAP MF_01283
Region21 – 222D-ribulose 5-phosphate binding By similarity
Region125 – 1295D-ribulose 5-phosphate binding By similarity
Region187 – 388202GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3111Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3131Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding221Magnesium or manganese 1 By similarity
Metal binding221Magnesium or manganese 2 By similarity
Metal binding1281Magnesium or manganese 2 By similarity
Metal binding2401Zinc; catalytic By similarity
Metal binding2511Zinc; catalytic By similarity
Metal binding2531Zinc; catalytic By similarity
Binding site261D-ribulose 5-phosphate By similarity
Binding site1491D-ribulose 5-phosphate By similarity
Binding site2561GTP By similarity
Binding site2991GTP By similarity
Binding site3341GTP By similarity
Binding site3391GTP By similarity
Site1131Essential for DHBP synthase activity By similarity
Site1491Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9X2E6 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 65514DDDC7EDD734

FASTA38843,927
        10         20         30         40         50         60 
MEELREAFEE GKPVILIDRN RENEADFVFP AQLITEDVVS FFVTYGKGLF CVTADEEDLL 

        70         80         90        100        110        120 
KRGFVKLSSN YGANYFVPVD WGTGTGISAL ERAETCRKLA EGRYFHEFRY PGHVTVIGGI 

       130        140        150        160        170        180 
GFQRRKGHTE ASLEISELAG FSRHAVIVEI LDEKGNSHNL DYVLKLSEKF SLPVLEMDDV 

       190        200        210        220        230        240 
WREFVKRKLL MKKKAEATLP TDFGVFKVVS FENHLDGKEH FAIVKEPLED PVAVRIHSEC 

       250        260        270        280        290        300 
VTGDVLSSLR CDCGSQLANF LRYMSAHGGI LIYLRQEGRG IGLSNKIAAY SLQDKGLDTV 

       310        320        330        340        350        360 
EANRVLGFSE DERDYAPAAQ ILKALGIERV LLFTNNQRKT VGLEKYGIEV VETKRLYGRV 

       370        380 
TPHNRFYLST KMKKLGHELE EIFREVNS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000512 Genomic DNA. Translation: AAD36889.1.
PIRE72207.
RefSeqNP_229623.1. NC_000853.1.

3D structure databases

ProteinModelPortalQ9X2E6.
SMRQ9X2E6. Positions 192-354.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID897563.
GenomeReviewsGene locus TM_1826 in contig AE000512_GR.
KEGGtma:TM1826.
NMPDRfig|243274.1.peg.1807.
PATRIC23938639. VBITheMar51294_1846.
TIGRTM_1826.

Phylogenomic databases

HOGENOMHBG735778.
OMANIDPFIS.
PhylomeDBQ9X2E6.
ProtClustDBPRK09318.

Enzyme and pathway databases

BioCycTMAR243274:TM_1826-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.
ProtoNetSearch...

Entry information

Entry nameRIBBA_THEMA
AccessionPrimary (citable) accession number: Q9X2E6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 83 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

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