Riboflavin biosynthesis protein ribBA - Mycobacterium tuberculosis

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P0A5V0 (RIBBA_MYCTU)

Last modified November 3, 2009. Version 31. 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

Hide | Top

Names and origin

Protein names

Recommended 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
Synonyms:	ribA, ribA2
Ordered Locus Names:	Rv1415, MT1458
ORF Names:	MTCY21B4.33

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Hide | Top

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	GTP-binding Magnesium Manganese Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Lyase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase II activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 425

425

Riboflavin biosynthesis protein ribBA HAMAP MF_01283

PRO_0000151728

Regions

Nucleotide binding

259 – 263

GTP By similarity

Nucleotide binding

303 – 305

GTP By similarity

Region

1 – 204

204

DHBP synthase HAMAP MF_01283

Region

28 – 29

D-ribulose 5-phosphate binding By similarity

Region

141 – 145

D-ribulose 5-phosphate binding By similarity

Region

205 – 425

221

GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site

337

Proton acceptor; for GTP cyclohydrolase activity Potential

Active site

339

Nucleophile; for GTP cyclohydrolase activity By similarity

Metal binding

Magnesium or manganese 1 By similarity

Metal binding

Magnesium or manganese 2 By similarity

Metal binding

144

Magnesium or manganese 2 By similarity

Metal binding

264

Zinc; catalytic By similarity

Metal binding

275

Zinc; catalytic By similarity

Metal binding

277

Zinc; catalytic By similarity

Binding site

D-ribulose 5-phosphate By similarity

Binding site

165

D-ribulose 5-phosphate By similarity

Binding site

280

GTP By similarity

Binding site

325

GTP By similarity

Binding site

360

GTP By similarity

Binding site

365

GTP By similarity

Site

127

Essential for DHBP synthase activity By similarity

Site

165

Essential for DHBP synthase activity By similarity

Experimental info

Sequence conflict

A → P in AAB60877. Ref.1

Sequence conflict

C → S in AAB60877. Ref.1

Sequence conflict

L → F in AAB60877. Ref.1

Sequence conflict

109 – 110

MR → IG in AAB60877. Ref.1

Sequence conflict

119

A → S in AAB60877. Ref.1

Sequence conflict

124

R → P in AAB60877. Ref.1

Sequence conflict

147 – 148

AA → TP in AAB60877. Ref.1

Sequence conflict

152

A → S in AAB60877. Ref.1

Sequence conflict

378

E → G in AAB60877. Ref.1

Sequence conflict

393

Y → C in AAB60877. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P0A5V0-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: FA7F73868814591F
Show »

FASTA

425

46,017

        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

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a gene expressed by a virulent strain of Mycobacterium tuberculosis H37Rv that is not expressed by the less virulent H37Ra." Kikuta-Oshima L.C., King C.H., Shinnick T.M., Ribot E.M., Wagner P.A., Utt E.A., Quinn F.D. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[3]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Hide | Top

Cross-references

Sequence databases
	AF001929 Genomic DNA. Translation: AAB60877.1. BX842576 Genomic DNA. Translation: CAB02199.1. AE000516 Genomic DNA. Translation: AAK45723.1.
PIR	D70902.
RefSeq	NP_215931.1. NP_335909.1.
3D structure databases
HSSP	HSSP built from PDB template 1K49 based on UniProtKB Q8TG90.
ModBase	Search...
Genome annotation databases
GeneID	886694. 924514.
GenomeReviews	Gene locus MT1458 in contig AE000516_GR. Gene locus Rv1415 in contig AL123456_GR.
KEGG	mtc:MT1458. mtu:Rv1415.
TIGR	MT1458.
Organism-specific databases
TubercuList	Rv1415.
Phylogenomic databases
HOGENOM	P0A5V0.
OMA	LRCDCRM.
Enzyme and pathway databases
BRENDA	3.5.4.25. 809. 4.1.99.12. 809.
Family and domain databases
HAMAP	MF_01283. [Tree]
InterPro	IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR000422. DHBP_synthase_RibB. IPR000926. GTP_CycHdrlase_II. IPR016299. Riboflavin_synth_RibA. [Graphical view]
Gene3D	G3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
Pfam	PF00926. DHBP_synthase. 1 hit. PF00925. GTP_cyclohydro2. 1 hit. [Graphical view]
PIRSF	PIRSF001259. RibA. 1 hit.
ProDom	PD003034. DHBP_synthase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00505. ribA. 1 hit. TIGR00506. ribB. 1 hit.
ProtoNet	Search...

Hide | Top

Entry information

Entry name

RIBBA_MYCTU

Accession

Primary (citable) accession number: P0A5V0
Secondary accession number(s): O07714, P71684

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

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)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents