Reviewed, UniProtKB/Swiss-Prot P50855 (RIBBA_ACTPL)

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

Organism

Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae)

Taxonomic identifier

715 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	401 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 Probable. 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	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 – 401	401	Riboflavin biosynthesis protein ribBA HAMAP MF_01283		PRO_0000151718
Regions
	Nucleotide binding	254 – 258	5	GTP By similarity
	Nucleotide binding	297 – 299	3	GTP By similarity
	Region	1 – 203	203	DHBP synthase HAMAP MF_01283
	Region	30 – 31	2	D-ribulose 5-phosphate binding By similarity
	Region	142 – 146	5	D-ribulose 5-phosphate binding By similarity
	Region	204 – 401	198	GTP cyclohydrolase II HAMAP MF_01283
Sites
	Active site	331	1	Proton acceptor; for GTP cyclohydrolase activity Potential
	Active site	333	1	Nucleophile; for GTP cyclohydrolase activity By similarity
	Metal binding	31	1	Magnesium or manganese 1 By similarity
	Metal binding	31	1	Magnesium or manganese 2 By similarity
	Metal binding	145	1	Magnesium or manganese 2 By similarity
	Metal binding	259	1	Zinc; catalytic By similarity
	Metal binding	270	1	Zinc; catalytic By similarity
	Metal binding	272	1	Zinc; catalytic By similarity
	Binding site	35	1	D-ribulose 5-phosphate By similarity
	Binding site	166	1	D-ribulose 5-phosphate By similarity
	Binding site	275	1	GTP By similarity
	Binding site	319	1	GTP By similarity
	Binding site	354	1	GTP By similarity
	Binding site	359	1	GTP By similarity
	Site	128	1	Essential for DHBP synthase activity By similarity
	Site	166	1	Essential for DHBP synthase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50855-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: DE108DB605B28DC9	FASTA	401	44,740
	10 20 30 40 50 60 MTDFQFSKVE DAIEAIRQGK IILVTDDEDR ENEGDFICAA EFATPENINF MATYGKGLIC 70 80 90 100 110 120 TPISTEIAKK LNFHPMVAVN QDNHETAFTV SVDHIDTGTG ISAFERSITA MKIVDDNAKA 130 140 150 160 170 180 TDFRRPGHMF PLIAKEGGVL VRNGHTEATV DLARLAGLKH AGLCCEIMAD DGTMMTMPDL 190 200 210 220 230 240 QKFAVEHNMP FITIQQLQEY RRKHDSLVKQ ISVVKMPTKY GEFMAHSFVE VISGKEHVAL 250 260 270 280 290 300 VKGDLTDGEQ VLARIHSECL TGDAFGSQRC DCGQQFAAAM TQIEQEGRGV ILYLRQEGRG 310 320 330 340 350 360 IGLINKLRAY ELQDKGMDTV EANVALGFKE DEREYYIGAQ MFQQLGVKSI RLLTNNPAKI 370 380 390 400 EGLKEQGLNI VAREPIIVEP NKNDIDYLKV KQIKMGHMFN F

References

[1]	"Characterization of Actinobacillus pleuropneumoniae riboflavin biosynthesis genes." Fuller T.E., Mulks M.H. J. Bacteriol. 177:7265-7270(1995) [PubMed: 8522537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ISU-178 / Serotype 5.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U27202 Genomic DNA. Translation: AAA86524.1.
PIR	T50548.
3D structure databases
HSSP	HSSP built from PDB template 1G58 based on UniProtKB P24199.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.5.4.25. 257522. 4.1.99.12. 257522.
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_ACTPL

Accession

Primary (citable) accession number: P50855

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	September 22, 2009
This is version 52 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)