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P0A5V1 (RIBBA_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:ribA2
Ordered Locus Names:Mb1450
OrganismMycobacterium bovis [Complete proteome] [HAMAP]
Taxonomic identifier1765 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium 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-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 – 425425Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_0000151727

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
P0A5V1 [UniParc].

Last modified March 15, 2005. 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		BX248338 Genomic DNA. Translation: CAD94311.1.
RefSeqNP_855102.1. NC_002945.3.

3D structure databases

ProteinModelPortalP0A5V1.
SMRP0A5V1. Positions 3-204, 208-384.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000018061; EBMYCP00000017896; EBMYCG00000018056.
GeneID1092307.
GenomeReviewsGene locus Mb1450 in contig BX248333_GR.
KEGGmbo:Mb1450.
PATRIC18004876. VBIMycBov88188_1585.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000015301.
HOGENOMHBG735778.
OMARCDCRMQ.
ProtClustDBPRK09311.

Enzyme and pathway databases

BioCycMBOV233413:MB1450-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_MYCBO
AccessionPrimary (citable) accession number: P0A5V1
Secondary accession number(s): O07714, P71684
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 48 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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