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A7Z675 (RIBBA_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:RBAM_021400
OrganismBacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length398 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 – 398398Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_1000067413

Regions

Nucleotide binding251 – 2555GTP By similarity
Nucleotide binding294 – 2963GTP 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 – 398199GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3281Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3301Nucleophile; 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 binding2561Zinc; catalytic By similarity
Metal binding2671Zinc; catalytic By similarity
Metal binding2691Zinc; catalytic By similarity
Binding site311D-ribulose 5-phosphate By similarity
Binding site1621D-ribulose 5-phosphate By similarity
Binding site2721GTP By similarity
Binding site3161GTP By similarity
Binding site3511GTP By similarity
Binding site3561GTP By similarity
Site1241Essential for DHBP synthase activity By similarity
Site1621Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A7Z675 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 7D5B923E23FA5745

FASTA39844,170
        10         20         30         40         50         60 
MFHPIEEALE ALKKGEVIIV VDDEDRENEG DFVALAEHAT PEVVNFMATH GRGLICTPLS 

        70         80         90        100        110        120 
EDIAGRLDLH PMVDHNTDSH ETAFTVSIDH RLTKTGISAQ ERSFTIQALL NEESVSDDFQ 

       130        140        150        160        170        180 
RPGHIFPLIA KKGGVLKRAG HTEAAVDLAK ACGSQGAGVI CEIMNEDGTM ARVPELAEIA 

       190        200        210        220        230        240 
ERHQLKMITI KDLIEYRYNI TTLVNREVDI TLPTDFGTFR VYGYTNEVDG KEHLAFVMGD 

       250        260        270        280        290        300 
VPFNSEPVLV RVHSECLTGD VFASHRCDCG PQLHAALAQI AEEGRGVLLY LRQEGRGIGL 

       310        320        330        340        350        360 
INKLKAYRLQ EQGYDTVEAN EALGFLPDLR NYGIGAQILR DLGVQHMKLL TNNPRKIAGL 

       370        380        390 
EGYGLSISER VPLQMEASEH NKQYLQTKMK KLGHLLHF 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000560 Genomic DNA. Translation: ABS74501.1.
RefSeqYP_001421732.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z675.
SMRA7Z675. Positions 204-374.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7Z675.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000007095; EBBACP00000006973; EBBACG00000007087.
GeneID5462558.
GenomeReviewsGene locus RBAM_021400 in contig CP000560_GR.
KEGGbay:RBAM_021400.
PATRIC18749362. VBIBacAmy31356_2157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
GeneTreeEBGT00050000001077.
HOGENOMHBG735778.
OMARCDCRMQ.
ProtClustDBPRK09311.

Enzyme and pathway databases

BioCycBAMY326423:RBAM_021400-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_BACA2
AccessionPrimary (citable) accession number: A7Z675
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 36 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