Reviewed, UniProtKB/Swiss-Prot P17620 (RIBBA_BACSU)

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:	BSU23260

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	398 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 – 398	398	Riboflavin biosynthesis protein ribBA HAMAP MF_01283		PRO_0000151721
Regions
	Nucleotide binding	251 – 255	5	GTP By similarity
	Nucleotide binding	294 – 296	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 – 398	199	GTP cyclohydrolase II HAMAP MF_01283
Sites
	Active site	328	1	Proton acceptor; for GTP cyclohydrolase activity Potential
	Active site	330	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	256	1	Zinc; catalytic By similarity
	Metal binding	267	1	Zinc; catalytic By similarity
	Metal binding	269	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	272	1	GTP By similarity
	Binding site	316	1	GTP By similarity
	Binding site	351	1	GTP By similarity
	Binding site	356	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)
	P17620-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: D9162EA7DAE611AA	FASTA	398	44,121
	10 20 30 40 50 60 MFHPIEEALD ALKKGEVIIV VDDEDRENEG DFVALAEHAT PEVINFMATH GRGLICTPLS 70 80 90 100 110 120 EEIADRLDLH PMVEHNTDSH HTAFTVSIDH RETKTGISAQ ERSFTVQALL DSKSVPSDFQ 130 140 150 160 170 180 RPGHIFPLIA KKGGVLKRAG HTEAAVDLAE ACGSPGAGVI CEIMNEDGTM ARVPELIEIA 190 200 210 220 230 240 KKHQLKMITI KDLIQYRYNL TTLVEREVDI TLPTDFGTFK VYGYTNEVDG KEHVAFVMGD 250 260 270 280 290 300 VPFGEEPVLV RVHSECLTGD VFGSHRCDCG PQLHAALNQI AAEGRGVLLY LRQEGRGIGL 310 320 330 340 350 360 INKLKAYKLQ EQGYDTVEAN EALGFLPDLR NYGIGAQILR DLGVRNMKLL TNNPRKIAGL 370 380 390 EGYGLSISER VPLQMEAKEH NKKYLQTKMN KLGHLLHF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data." Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P. Mol. Microbiol. 10:385-395(1993) [PubMed: 7934829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg.
[2]	Mironov V.N. Thesis (1989), USSR Academy of Sciences, Russia Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / SHGW.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L09228 Genomic DNA. Translation: AAA67483.1. X51510 Genomic DNA. Translation: CAA35880.1. AL009126 Genomic DNA. Translation: CAB14258.1.
PIR	S45545.
RefSeq	NP_390207.1.
3D structure databases
HSSP	HSSP built from PDB template 1G58 based on UniProtKB P24199.
ModBase	Search...
Genome annotation databases
GeneID	938946.
GenomeReviews	Gene locus BSU23260 in contig AL009126_GR.
KEGG	bsu:BSU23260.
NMPDR	fig|224308.1.peg.2330.
Organism-specific databases
SubtiList	BG10520. ribBA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P17620.
OMA	LRCDCRM.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU2325-MON.
BRENDA	3.5.4.25. 150. 4.1.99.12. 150.
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_BACSU

Accession

Primary (citable) accession number: P17620

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	November 3, 2009
This is version 80 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)