Reviewed, UniProtKB/Swiss-Prot Q0AXM5 (RIBBA_SYNWW)

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:	Swol_1220

Organism

Syntrophomonas wolfei subsp. wolfei (strain Goettingen) [Complete proteome] [HAMAP]

Taxonomic identifier

335541 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Syntrophomonadaceae › Syntrophomonas

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_1000067431
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 – 398	199	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)
	Q0AXM5-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 90A6358014178453	FASTA	398	44,443
	10 20 30 40 50 60 MFSSIEEVIQ DIKEGKMIVL VDDEDRENEG DVIIAAEKAG PEAINFMATH AKGLICMPII 70 80 90 100 110 120 GERLDELEIH DMVTENTDNH ETAFTVTVDY RGTTTGISAF ERAATVKALI DSVSKPSDFR 130 140 150 160 170 180 KPGHIFPLRY REGGVLRRAG HTEGSIDLTR LAGLYPAAVI CEVMNEDGTM ARLPQLLEFA 190 200 210 220 230 240 RQHNLKLASI ADLIEYRRRK EKLVVRVTDA QLPTMYGDFV AVAYESLLDN KGHIALVKGE 250 260 270 280 290 300 WEEDEPILVR VHSECLTGDV FGSRRCDCGE QLETAMSMIA SEGKGVLLYM RQEGRGIGLL 310 320 330 340 350 360 NKIKAYKLQD NGRDTVEANL ELGFPADLRD YGIGAQILVD LGVRKMRLMT NNPKKIRGLE 370 380 390 GYGLEVVERV AIEMPHKPEN TRYLRTKKEK MGHLLASL

References

[1]

"Complete sequence of Syntrophomonas wolfei subsp. wolfei str. Goettingen." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Sims D., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R., McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J., Stams A.J.M., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000448 Genomic DNA. Translation: ABI68529.1.
RefSeq	YP_753900.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0AXM5.
Genome annotation databases
GeneID	4282485.
GenomeReviews	Gene locus Swol_1220 in contig CP000448_GR.
KEGG	swo:Swol_1220.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0AXM5.
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_SYNWW

Accession

Primary (citable) accession number: Q0AXM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 17, 2006
Last modified:	November 3, 2009
This is version 29 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)