Reviewed, UniProtKB/Swiss-Prot A0PPL6 (RIBBA_MYCUA)

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
Ordered Locus Names:	MUL_1809

Organism

Mycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]

Taxonomic identifier

362242 [NCBI]

Taxonomic lineage

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

Protein attributes

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

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...

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_1000067427
Regions
	Nucleotide binding	259 – 263	5	GTP By similarity
	Nucleotide binding	303 – 305	3	GTP By similarity
	Region	1 – 204	204	DHBP synthase HAMAP MF_01283
	Region	28 – 29	2	D-ribulose 5-phosphate binding By similarity
	Region	141 – 145	5	D-ribulose 5-phosphate binding By similarity
	Region	205 – 425	221	GTP cyclohydrolase II HAMAP MF_01283
Sites
	Active site	337	1	Proton acceptor; for GTP cyclohydrolase activity Potential
	Active site	339	1	Nucleophile; for GTP cyclohydrolase activity By similarity
	Metal binding	29	1	Magnesium or manganese 1 By similarity
	Metal binding	29	1	Magnesium or manganese 2 By similarity
	Metal binding	144	1	Magnesium or manganese 2 By similarity
	Metal binding	264	1	Zinc; catalytic By similarity
	Metal binding	275	1	Zinc; catalytic By similarity
	Metal binding	277	1	Zinc; catalytic By similarity
	Binding site	33	1	D-ribulose 5-phosphate By similarity
	Binding site	165	1	D-ribulose 5-phosphate By similarity
	Binding site	280	1	GTP By similarity
	Binding site	325	1	GTP By similarity
	Binding site	360	1	GTP By similarity
	Binding site	365	1	GTP By similarity
	Site	127	1	Essential for DHBP synthase activity By similarity
	Site	165	1	Essential for DHBP synthase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0PPL6-1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 0703B615B9808B29	FASTA	425	46,106
	10 20 30 40 50 60 MTRLDSVERA VADIGAGKAV IVIDDEDREN EGDLIFAAEK ATPELVAFMV RYTSGYLCVP 70 80 90 100 110 120 LDGAVCDRLG LLPMYAVNQD KHGTAYTVTV DAKNGVGTGI SASDRATTMR LLADPASVAE 130 140 150 160 170 180 DFTRPGHVVP LRAKDGGVLR RPGHTEAAVD LARMAGLQPA GAICEIVSRK DEGSMAQTDE 190 200 210 220 230 240 LRVFADEHGL ALITIADLIE WRRKHEKHIE RVAEARIPTR RGEFRAIGYT SIYENVEHVA 250 260 270 280 290 300 LVRGEIAGPN SDGDDVLVRV HSECLTGDVF GSRRCDCGSQ LDAAMAMVAR EGRGVVLYMR 310 320 330 340 350 360 GHEGRGIGLL HKLQTYQLQD AGDDTVDANL KLGLPADARD YGIGAQILVD LGVRSMRLLT 370 380 390 400 410 420 NNPAKRVGLD GYGLHIIERV PLPVRANAEN IRYLMTKRDR MGHDLTGLDD FHESVHLPGE FGGAL

References

[1]

"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer." Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T. Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000325 Genomic DNA. Translation: ABL04285.1.
RefSeq	YP_905756.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A0PPL6.
Genome annotation databases
GeneID	4551696.
GenomeReviews	Gene locus MUL_1809 in contig CP000325_GR.
KEGG	mul:MUL_1809.
Organism-specific databases
BuruList	MUL_1809.
CMR	Search...
Phylogenomic databases
OMA	LRCDCRM.
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...

Entry information

Entry name

RIBBA_MYCUA

Accession

Primary (citable) accession number: A0PPL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	January 9, 2007
Last modified:	November 3, 2009
This is version 25 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)