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Reviewed, UniProtKB/Swiss-Prot A1KIK4 (RIBBA_MYCBP)

Last modified February 9, 2010. Version 29. 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: BCG_1476
OrganismMycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]
Taxonomic identifier410289 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length425 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-phosphoribosylamino)pyrimidine + diphosphate. HAMAP MF_01283

Cofactor

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity. HAMAP MF_01283

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 – 425425Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_1000067424

Regions

Nucleotide binding259 – 2635GTP By similarity
Nucleotide binding303 – 3053GTP By similarity
Region1 – 204204DHBP synthase HAMAP MF_01283
Region28 – 292D-ribulose 5-phosphate binding By similarity
Region141 – 1455D-ribulose 5-phosphate binding By similarity
Region205 – 425221GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3371Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3391Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding291Magnesium or manganese 1 By similarity
Metal binding291Magnesium or manganese 2 By similarity
Metal binding1441Magnesium or manganese 2 By similarity
Metal binding2641Zinc; catalytic By similarity
Metal binding2751Zinc; catalytic By similarity
Metal binding2771Zinc; catalytic By similarity
Binding site331D-ribulose 5-phosphate By similarity
Binding site1651D-ribulose 5-phosphate By similarity
Binding site2801GTP By similarity
Binding site3251GTP By similarity
Binding site3601GTP By similarity
Binding site3651GTP By similarity
Site1271Essential for DHBP synthase activity By similarity
Site1651Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A1KIK4-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: FA7F73868814591F

FASTA42546,017
        10         20         30         40         50         60 
MTRLDSVERA VADIAAGKAV IVIDDEDREN EGDLIFAAEK ATPEMVAFMV RYTSGYLCVP 

        70         80         90        100        110        120 
LDGAICDRLG LLPMYAVNQD KHGTAYTVTV DARNGIGTGI SASDRATTMR LLADPTSVAD 

       130        140        150        160        170        180 
DFTRPGHVVP LRAKDGGVLR RPGHTEAAVD LARMAGLQPA GAICEIVSQK DEGSMAHTDE 

       190        200        210        220        230        240 
LRVFADEHGL ALITIADLIE WRRKHEKHIE RVAEARIPTR HGEFRAIGYT SIYEDVEHVA 

       250        260        270        280        290        300 
LVRGEIAGPN ADGDDVLVRV HSECLTGDVF GSRRCDCGPQ LDAALAMVAR EGRGVVLYMR 

       310        320        330        340        350        360 
GHEGRGIGLM HKLQAYQLQD AGADTVDANL KLGLPADARD YGIGAQILVD LGVRSMRLLT 

       370        380        390        400        410        420 
NNPAKRVGLD GYGLHIIERV PLPVRANAEN IRYLMTKRDK LGHDLAGLDD FHESVHLPGE 


FGGAL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM408590 Genomic DNA. Translation: CAL71463.1.
RefSeqYP_977568.1.

3D structure databases

SMRA1KIK4. Positions 3-204, 208-384.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1KIK4.

Genome annotation databases

GeneID4696694.
GenomeReviewsGene locus BCG_1476 in contig AM408590_GR.
KEGGmbb:BCG_1476.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0807.
HOGENOMHBG735778.
OMALRCDCRM.

Family and domain databases

HAMAPMF_01283. RibBA.
[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.
TIGRFAMsTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBBA_MYCBP
AccessionPrimary (citable) accession number: A1KIK4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: February 9, 2010
This is version 29 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