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Reviewed, UniProtKB/Swiss-Prot A3MZA2 (RIBBA_ACTP2)

Last modified November 3, 2009. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Riboflavin biosynthesis protein ribBA
Including the following 2 domains:
    1- Recommended name:
            3,4-dihydroxy-2-butanone 4-phosphate synthase
                Short name=DHBP synthase
              EC=4.1.99.12
    2- Recommended name:
            GTP cyclohydrolase-2
              EC=3.5.4.25
        Alternative name(s):
            GTP cyclohydrolase II
Gene names
Name: ribBA
Ordered Locus Names: APL_0384
OrganismActinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]
Taxonomic identifier416269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity.

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-phosphoribosylamino)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.

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 – 401401Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_1000067412

Regions

Nucleotide binding254 – 2585GTP By similarity
Nucleotide binding297 – 2993GTP By similarity
Region1 – 203203DHBP synthase HAMAP MF_01283
Region30 – 312D-ribulose 5-phosphate binding By similarity
Region142 – 1465D-ribulose 5-phosphate binding By similarity
Region204 – 401198GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3311Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3331Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding311Magnesium or manganese 1 By similarity
Metal binding311Magnesium or manganese 2 By similarity
Metal binding1451Magnesium or manganese 2 By similarity
Metal binding2591Zinc; catalytic By similarity
Metal binding2701Zinc; catalytic By similarity
Metal binding2721Zinc; catalytic By similarity
Binding site351D-ribulose 5-phosphate By similarity
Binding site1661D-ribulose 5-phosphate By similarity
Binding site2751GTP By similarity
Binding site3191GTP By similarity
Binding site3541GTP By similarity
Binding site3591GTP By similarity
Site1281Essential for DHBP synthase activity By similarity
Site1661Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A3MZA2-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: DE108DB605B28DC9

FASTA40144,740
        10         20         30         40         50         60 
MTDFQFSKVE DAIEAIRQGK IILVTDDEDR ENEGDFICAA EFATPENINF MATYGKGLIC 

        70         80         90        100        110        120 
TPISTEIAKK LNFHPMVAVN QDNHETAFTV SVDHIDTGTG ISAFERSITA MKIVDDNAKA 

       130        140        150        160        170        180 
TDFRRPGHMF PLIAKEGGVL VRNGHTEATV DLARLAGLKH AGLCCEIMAD DGTMMTMPDL 

       190        200        210        220        230        240 
QKFAVEHNMP FITIQQLQEY RRKHDSLVKQ ISVVKMPTKY GEFMAHSFVE VISGKEHVAL 

       250        260        270        280        290        300 
VKGDLTDGEQ VLARIHSECL TGDAFGSQRC DCGQQFAAAM TQIEQEGRGV ILYLRQEGRG 

       310        320        330        340        350        360 
IGLINKLRAY ELQDKGMDTV EANVALGFKE DEREYYIGAQ MFQQLGVKSI RLLTNNPAKI 

       370        380        390        400 
EGLKEQGLNI VAREPIIVEP NKNDIDYLKV KQIKMGHMFN F 

« Hide

References

[1]"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)."
Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.
J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000569 Genomic DNA. Translation: ABN73488.1.
RefSeqYP_001053093.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA3MZA2.

Genome annotation databases

GeneID4850491.
GenomeReviewsGene locus APL_0384 in contig CP000569_GR.
KEGGapl:APL_0384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMANIVAREP.

Family and domain databases

HAMAPMF_01283.
[Tree]
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlase_II.
IPR016299. Riboflavin_synth_RibA.
[Graphical view]
Gene3DG3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
PfamPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFPIRSF001259. RibA. 1 hit.
ProDomPD003034. DHBP_synthase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBBA_ACTP2
AccessionPrimary (citable) accession number: A3MZA2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: November 3, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents