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P51695 (RIBBA_BACAM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 73. 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
Synonyms:ribA
OrganismBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifier1390 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

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-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. 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. HAMAP-Rule MF_01283

Cofactor

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.

Binds 1 zinc ion per subunit 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. HAMAP-Rule 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-Rule MF_01283
PRO_0000151720

Regions

Nucleotide binding251 – 2555GTP By similarity
Nucleotide binding294 – 2963GTP By similarity
Region1 – 199199DHBP synthase HAMAP-Rule MF_01283
Region26 – 272D-ribulose 5-phosphate binding By similarity
Region138 – 1425D-ribulose 5-phosphate binding By similarity
Region200 – 398199GTP cyclohydrolase II HAMAP-Rule 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
P51695 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F3B9849AF877E260

FASTA39844,098
        10         20         30         40         50         60 
MFHPIEEALE ALKKGEVIIV VDDEDRENEG DFVALAEHAT PEVVNFMATH GRGLICTPLS 

        70         80         90        100        110        120 
EDIAGRLDLH PMVDHNTDSH ETAFTVSIDH KLTKTGISAQ ERSFTIQALL DEESVPGDFQ 

       130        140        150        160        170        180 
RPGHIFPLIA KKGGVLKRAG HTEAAVDLAK ACGSQGADVI CEIMNEDGTM ARVPEISEIA 

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

       250        260        270        280        290        300 
VPFNSGPVLV RVHSECLTGD VFASHRCDCG PQLHAALRQI AEEGRGVLLY LRQEGRGIGL 

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

       370        380        390 
EGYGLSISDR VPLQMEASEH NKQYLQTKMK KLGHLLHF

« Hide

References

[1]"Riboflavin biosynthetic genes in Bacillus amyloliquefaciens: primary structure, organization and regulation of activity."
Gusarov I.I., Kreneva R.A., Podcharniaev D.A., Iomantas I.U.V., Abalakina E.G., Stoinova N.V., Perumov D.A., Kozlov I.U.I.
Mol. Biol. (Mosk.) 31:446-453(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A 50.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X95955 Genomic DNA. Translation: CAA65191.1.
PIRT50543.

3D structure databases

ProteinModelPortalP51695.
SMRP51695. Positions 204-374.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00275; UER00399.
UPA00275; UER00400.

Family and domain databases

Gene3D3.90.870.10. 1 hit.
HAMAPMF_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 nameRIBBA_BACAM
AccessionPrimary (citable) accession number: P51695
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 29, 2013
This is version 73 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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