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B0KAI2 (RIBBA_THEP3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:Teth39_0023
OrganismThermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) [Complete proteome] [HAMAP]
Taxonomic identifier340099 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Thermoanaerobacter

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 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 – 396396Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_1000140367

Regions

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

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B0KAI2 [UniParc].

Last modified March 18, 2008. 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 pseudethanolicus 39E."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33223 / 39E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000924 Genomic DNA. Translation: ABY93696.1.
RefSeqYP_001664032.1. NC_010321.1.

3D structure databases

ProteinModelPortalB0KAI2.
SMRB0KAI2. Positions 1-199, 203-372.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0KAI2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5875623.
GenomeReviewsGene locus Teth39_0023 in contig CP000924_GR.
KEGGtpd:Teth39_0023.
PATRIC23884558. VBIThePse6203_0025.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG735778.
OMARCDCRMQ.
ProtClustDBCLSK985899.

Enzyme and pathway databases

BioCycTPSE340099:TETH39_0023-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.
TIGR00506. RibB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBBA_THEP3
AccessionPrimary (citable) accession number: B0KAI2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 18, 2008
Last modified: January 25, 2012
This is version 30 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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