Reviewed, UniProtKB/Swiss-Prot O24752 (RIBBA_CORAM)

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

Corynebacterium ammoniagenes (Brevibacterium ammoniagenes)

Taxonomic identifier

1697 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
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. HAMAP MF_01283 Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity. HAMAP MF_01283
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. HAMAP MF_01283 Binds 1 zinc ion per subunit By similarity. HAMAP MF_01283
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 – 423	423	Riboflavin biosynthesis protein ribBA HAMAP MF_01283		PRO_0000151726
Regions
	Nucleotide binding	264 – 268	5	GTP By similarity
	Nucleotide binding	308 – 310	3	GTP By similarity
	Region	1 – 210	210	DHBP synthase HAMAP MF_01283
	Region	35 – 36	2	D-ribulose 5-phosphate binding By similarity
	Region	147 – 151	5	D-ribulose 5-phosphate binding By similarity
	Region	211 – 423	213	GTP cyclohydrolase II HAMAP MF_01283
Sites
	Active site	342	1	Proton acceptor; for GTP cyclohydrolase activity Potential
	Active site	344	1	Nucleophile; for GTP cyclohydrolase activity By similarity
	Metal binding	36	1	Magnesium or manganese 1 By similarity
	Metal binding	36	1	Magnesium or manganese 2 By similarity
	Metal binding	150	1	Magnesium or manganese 2 By similarity
	Metal binding	269	1	Zinc; catalytic By similarity
	Metal binding	280	1	Zinc; catalytic By similarity
	Metal binding	282	1	Zinc; catalytic By similarity
	Binding site	40	1	D-ribulose 5-phosphate By similarity
	Binding site	171	1	D-ribulose 5-phosphate By similarity
	Binding site	285	1	GTP By similarity
	Binding site	330	1	GTP By similarity
	Binding site	365	1	GTP By similarity
	Binding site	370	1	GTP By similarity
	Site	133	1	Essential for DHBP synthase activity By similarity
	Site	171	1	Essential for DHBP synthase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	O24752-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: EBBE9CA3E902BD25	FASTA	423	46,399
	10 20 30 40 50 60 MNAPLNSAVR LDSIEEAIAD IAAGKAVVVV DNEDRENEGD LIFAAELATP ELVAFMVRYS 70 80 90 100 110 120 SGYICVPLLP EDCKRLNLPP MMGRNEDVRG TAYTVTVDAN TGTTGISATS RAETMLRLAD 130 140 150 160 170 180 PMSVVDDFTR PGHVVPLAAR PNGVLERDGH TEAAIDLARL AGLRPAGVLC EIVSEEDPTT 190 200 210 220 230 240 MARSEELRRF SDEHDLKMIS IEQLIEWRRH NETQVRRTVE TQLPTDFGSF TALGYKHEID 250 260 270 280 290 300 GQEHVALIAG GVEELNGAED VFVRVHSECL TGDVFHSRRC DCGQQLHQSM EIIQEAGQGI 310 320 330 340 350 360 IIYLRGHEGR GIGLLAKLKA YSLQDSGLDT VDANLEQGLP EDAREYSVAG QILRDLGIKS 370 380 390 400 410 420 ANLLTNNPHK GEGLRGFGVE ASAHTPVEIE PNADNIDYLR TKRDRMNHDL PQVARWDAAH ALK

References

[1]	"Process for producing riboflavin." Koizumi S., Yonetani Y., Teshiba S. Patent number US5589355, 31-DEC-1996 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB003693 Genomic DNA. Translation: BAA20055.1.
3D structure databases
SMR	O24752. Positions 11-210, 214-389.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.5.4.25. 259964. 4.1.99.12. 259964.
Family and domain databases
HAMAP	MF_01283. RibBA. [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.
TIGRFAMs	TIGR00505. ribA. 1 hit. TIGR00506. ribB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RIBBA_CORAM

Accession

Primary (citable) accession number: O24752

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 60 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)