Reviewed, UniProtKB/Swiss-Prot Q99TA0 (RIBBA_STAAM)

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
Ordered Locus Names:	SAV1769

Organism

Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]

Taxonomic identifier

158878 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 – 393	393	Riboflavin biosynthesis protein ribBA HAMAP MF_01283		PRO_0000151734
Regions
	Nucleotide binding	249 – 253	5	GTP By similarity
	Nucleotide binding	291 – 293	3	GTP By similarity
	Region	1 – 200	200	DHBP synthase HAMAP MF_01283
	Region	27 – 28	2	D-ribulose 5-phosphate binding By similarity
	Region	139 – 143	5	D-ribulose 5-phosphate binding By similarity
	Region	201 – 393	193	GTP cyclohydrolase II HAMAP MF_01283
Sites
	Active site	325	1	Proton acceptor; for GTP cyclohydrolase activity Potential
	Active site	327	1	Nucleophile; for GTP cyclohydrolase activity By similarity
	Metal binding	28	1	Magnesium or manganese 1 By similarity
	Metal binding	28	1	Magnesium or manganese 2 By similarity
	Metal binding	142	1	Magnesium or manganese 2 By similarity
	Metal binding	254	1	Zinc; catalytic By similarity
	Metal binding	265	1	Zinc; catalytic By similarity
	Metal binding	267	1	Zinc; catalytic By similarity
	Binding site	32	1	D-ribulose 5-phosphate By similarity
	Binding site	163	1	D-ribulose 5-phosphate By similarity
	Binding site	270	1	GTP By similarity
	Binding site	313	1	GTP By similarity
	Binding site	348	1	GTP By similarity
	Binding site	353	1	GTP By similarity
	Site	125	1	Essential for DHBP synthase activity By similarity
	Site	163	1	Essential for DHBP synthase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99TA0-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 764A49DFDD46792C	FASTA	393	44,148
	10 20 30 40 50 60 MQFDNIDSAL MALKNGETII VVDDENRENE GDLVAVTEWM NDNTINFMAK EARGLICAPV 70 80 90 100 110 120 SKDIAQRLDL VQMVDDNSDI FGTQFTVSID HVDTTTGISA YERTLTAKKL IDPSSEAKDF 130 140 150 160 170 180 NRPGHLFPLV AQDKGVLARN GHTEAAVDLA KLTGAKPAGV ICEIMNDDGT MAKGQDLQNF 190 200 210 220 230 240 KEKHQLKMIT IDDLIEYRKK LEPEIEFKAK VKMPTDFGTF DMYGFKATYT DEEIVVLTKG 250 260 270 280 290 300 AIRQHENVRL HSACLTGDIF HSQRCDCGAQ LESSMKYINE HGGMIIYLPQ EGRGIGLLNK 310 320 330 340 350 360 LRAYELIEQG YDTVTANLAL GFDEDLRDYH IAAQILKYFN IEHINLLSNN PSKFEGLKQY 370 380 390 GIDIAERIEV IVPETVHNHD YMVTKKIKMG HLI

References

[1]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000017 Genomic DNA. Translation: BAB57931.1.
RefSeq	NP_372293.1.
3D structure databases
HSSP	HSSP built from PDB template 1G58 based on UniProtKB P24199.
ModBase	Search...
Protein-protein interaction databases
STRING	Q99TA0.
2-D gel databases
World-2DPAGE	0002:Q99TA0.
Genome annotation databases
GeneID	1121743.
GenomeReviews	Gene locus SAV1769 in contig BA000017_GR.
KEGG	sav:SAV1769.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q99TA0.
OMA	LRCDCRM.
Enzyme and pathway databases
BioCyc	SAUR158878:SAV1769-MON.
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_STAAM

Accession

Primary (citable) accession number: Q99TA0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 51 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)