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Q81MB6 (RIBBA_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BA_4333, GBAA_4333, BAS4020
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length397 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 – 397397Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_1000067415

Regions

Nucleotide binding250 – 2545GTP By similarity
Nucleotide binding293 – 2953GTP 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 – 397198GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3271Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3291Nucleophile; 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 binding2551Zinc; catalytic By similarity
Metal binding2661Zinc; catalytic By similarity
Metal binding2681Zinc; catalytic By similarity
Binding site311D-ribulose 5-phosphate By similarity
Binding site1621D-ribulose 5-phosphate By similarity
Binding site2711GTP By similarity
Binding site3151GTP By similarity
Binding site3501GTP By similarity
Binding site3551GTP By similarity
Site1241Essential for DHBP synthase activity By similarity
Site1621Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81MB6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 771BDE2064509963

FASTA39743,907
        10         20         30         40         50         60 
MFHRIEEALE DLKQGKVVIV CDDENRENEG DFIALAEYIT PETINFMITH GRGLVCVPIT 

        70         80         90        100        110        120 
EGYAERLQLE PMVSHNTDSH HTAFTVSIDH VSTTTGISAH ERATTIQQLL NPASKGADFN 

       130        140        150        160        170        180 
RPGHIFPLIA KEGGVLRRAG HTEAAVDLAQ LCGAEPAGVI CEIINEDGTM ARVPDLLQCA 

       190        200        210        220        230        240 
KQFDIKMITI EDLIAYRRHH ETLVTREVEI TLPTDFGTFQ AIGYSNSLDT KEHIALVKGD 

       250        260        270        280        290        300 
ISTGEPVLVR VHSECLTGDV FGSCRCDCGP QLHAALAQIE REGKGVLLYM RQEGRGIGLL 

       310        320        330        340        350        360 
NKLRAYKLQE EGFDTVEANE KLGFPADLRD YGIGAQILKD LGLQHLRLLT NNPRKIAGLQ 

       370        380        390 
GYDLTVTERV PLQMPAKEEN KTYLQTKVNK LGHLLNL

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[3]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016879 Genomic DNA. Translation: AAP28052.1.
AE017334 Genomic DNA. Translation: AAT33454.1.
AE017225 Genomic DNA. Translation: AAT56321.1.
RefSeqNP_846566.1. NC_003997.3.
YP_020979.1. NC_007530.2.
YP_030270.1. NC_005945.1.

3D structure databases

HSSPHSSP built from PDB template 2BZ0 based on UniProtKB P0A7I7.
ProteinModelPortalQ81MB6.
SMRQ81MB6. Positions 204-373.
ModBaseSearch...

Protein-protein interaction databases

IntActQ81MB6. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000011097; EBBACP00000010853; EBBACG00000011089.
EBBACT00000016348; EBBACP00000015969; EBBACG00000016340.
EBBACT00000022845; EBBACP00000022330; EBBACG00000022836.
GeneID1087528.
2818522.
2850961.
GenomeReviewsGene locus BA_4333 in contig AE016879_GR.
Gene locus BAS4020 in contig AE017225_GR.
Gene locus GBAA_4333 in contig AE017334_GR.
KEGGban:BA_4333.
bar:GBAA_4333.
bat:BAS4020.
TIGRBA_4333.
GBAA_4333.

Phylogenomic databases

GeneTreeEBGT00050000001077.
HOGENOMHBG735778.
OMARCDCRMQ.
ProtClustDBPRK09311.

Enzyme and pathway databases

BioCycBANT260799:BAS4020-MONOMER.
BANT261594:GBAA4333-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_BACAN
AccessionPrimary (citable) accession number: Q81MB6
Secondary accession number(s): Q6HTR8, Q6KN06
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 71 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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