Reviewed, UniProtKB/Swiss-Prot Q5WH08 (RIBBA_BACSK)

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:	ABC1812

Organism

Bacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]

Taxonomic identifier

66692 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	397 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 – 397	397	Riboflavin biosynthesis protein ribBA HAMAP MF_01283		PRO_1000067420
Regions
	Nucleotide binding	250 – 254	5	GTP By similarity
	Nucleotide binding	293 – 295	3	GTP By similarity
	Region	1 – 199	199	DHBP synthase HAMAP MF_01283
	Region	26 – 27	2	D-ribulose 5-phosphate binding By similarity
	Region	138 – 142	5	D-ribulose 5-phosphate binding By similarity
	Region	200 – 397	198	GTP cyclohydrolase II HAMAP MF_01283
Sites
	Active site	327	1	Proton acceptor; for GTP cyclohydrolase activity Potential
	Active site	329	1	Nucleophile; for GTP cyclohydrolase activity By similarity
	Metal binding	27	1	Magnesium or manganese 1 By similarity
	Metal binding	27	1	Magnesium or manganese 2 By similarity
	Metal binding	141	1	Magnesium or manganese 2 By similarity
	Metal binding	255	1	Zinc; catalytic By similarity
	Metal binding	266	1	Zinc; catalytic By similarity
	Metal binding	268	1	Zinc; catalytic By similarity
	Binding site	31	1	D-ribulose 5-phosphate By similarity
	Binding site	162	1	D-ribulose 5-phosphate By similarity
	Binding site	271	1	GTP By similarity
	Binding site	315	1	GTP By similarity
	Binding site	350	1	GTP By similarity
	Binding site	355	1	GTP By similarity
	Site	124	1	Essential for DHBP synthase activity By similarity
	Site	162	1	Essential for DHBP synthase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5WH08-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 2FF80EDE7719B558	FASTA	397	43,544
	10 20 30 40 50 60 MFESIDEAIT QLKAGGMILV VDDEDRENEG DFLALAETAS PETINFMATH GRGLICVPLT 70 80 90 100 110 120 EEQAERLQLG QMVSHSTDPH GTAFTVSVDH SHTTTGISAF ERAETVRALA DANAQPSDFK 130 140 150 160 170 180 RPGHVFPLVA KNGGVLRRAG HTEAAVDFAK LCGAKPAGVI CEVMNEDGSM ARVPELRIIA 190 200 210 220 230 240 DQHNLPLVTI KDLIAYRRKT EKVVTREVAI SLPTEYGDFK AVGYTNTIDG KESVALVKGD 250 260 270 280 290 300 VGNGEPVLVR VHSECLTGDV FGSKRCDCGP QLHAALKQIE AEGRGVLLYM KQEGRGIGLI 310 320 330 340 350 360 NKFRAYKLQE EGYDTVEANE RLGFPADLRE YGIGAQILRD LGIRDMRLLT NNPRKIAGLE 370 380 390 GYDLNIVERV PLQMEAVAEN ERYLHTKREK LGHMLNL

References

[1]	"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16." Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AP006627 Genomic DNA. Translation: BAD64347.1.
RefSeq	YP_175308.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5WH08.
Genome annotation databases
GeneID	3201509.
GenomeReviews	Gene locus ABC1812 in contig AP006627_GR.
KEGG	bcl:ABC1812.
NMPDR	fig|66692.3.peg.1760.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5WH08.
OMA	LRCDCRM.
Enzyme and pathway databases
BioCyc	BCLA66692:ABC1812-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_BACSK

Accession

Primary (citable) accession number: Q5WH08

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 23, 2004
Last modified:	November 3, 2009
This is version 33 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)