Q9PHU4 (RIBB_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3,4-dihydroxy-2-butanone 4-phosphate synthase
Short name=DHBP synthase
EC=4.1.99.12

Gene names

Name:	ribB
Ordered Locus Names:	Cj0572

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	339 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_00180
Catalytic activity	D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP MF_00180
Cofactor	Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_00180
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	Magnesium Manganese Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred from electronic annotation. Source: EC GTP cyclohydrolase II activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	3,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180		PRO_0000151722
Regions
	Region	1 – 206	206	DHBP synthase HAMAP MF_00180
	Region	27 – 28	2	Substrate binding By similarity
	Region	139 – 143	5	Substrate binding By similarity
	Region	207 – 339	133	GTP cyclohydrolase II-like HAMAP MF_00180
Sites
	Metal binding	28	1	Magnesium or manganese 1 By similarity
	Metal binding	28	1	Magnesium or manganese 2 By similarity
	Metal binding	142	1	Magnesium or manganese 2 By similarity
	Binding site	32	1	Substrate By similarity
	Binding site	163	1	Substrate By similarity
	Site	125	1	Essential for catalytic activity By similarity
	Site	163	1	Essential for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PHU4 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 6D90CF5F6A3F3DD9	FASTA	339	37,925
	10 20 30 40 50 60 MKFVSVEQAI KDLQAGKMLV MVDAEDRENE GDLIFPAQFS TQEKVNFMIK EARGVVCVAL 70 80 90 100 110 120 DETLAKKFEL PLMVPKNTSN HETAFTITVD AKDATTGVSA YERNMTIQIF ADDNAKASDF 130 140 150 160 170 180 VRPGHINPLI AKKGGVLERT GHTEGTVDLC KLAGLKGACV ICEIVKDNGD MARREDLEIF 190 200 210 220 230 240 CQKHDLNMIA VSDLIEYRLK HESLIKLEEK SQSVLAGFKA EKFIFSDHNQ TQHIAFCFKD 250 260 270 280 290 300 IKKCENVKFH ISGSDFELLT SDKFSKLLEQ IKFLSENGGV IVFMQGEKSS TTQYKNYGIG 310 320 330 AQILRYFGIE EIKLLSQSCD KDYIGLEGFG LNLKACNFN

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL34718.1.
PIR	C81404.
RefSeq	YP_002344002.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q9PHU4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PHU4. 70 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	904897.
GenomeReviews	Gene locus Cj0572 in contig AL111168_GR.
KEGG	cje:Cj0572.
PATRIC	20058088. VBICamJej33762_0564.
Phylogenomic databases
HOGENOM	HBG735778.
OMA	TSSHETA.
PhylomeDB	Q9PHU4.
ProtClustDB	PRK09314.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0572-MONOMER.
Family and domain databases
HAMAP	MF_00180. RibB. Fused. [Tree]
InterPro	IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR000422. DHBP_synthase_RibB. IPR000926. GTP_CycHdrlaseII_RibA. IPR016299. Riboflavin_synth_RibBA. [Graphical view]
Gene3D	G3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
KO	K14652.
Pfam	PF00926. DHBP_synthase. 1 hit. PF00925. GTP_cyclohydro2. 1 hit. [Graphical view]
PIRSF	PIRSF001259. RibA. 1 hit.
SUPFAM	SSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit.
TIGRFAMs	TIGR00506. RibB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RIBB_CAMJE

Accession

Primary (citable) accession number: Q9PHU4
Secondary accession number(s): Q0PAU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program