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Reviewed, UniProtKB/Swiss-Prot Q9PHU4 (RIBB_CAMJE)

Last modified February 9, 2010. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismCampylobacter jejuni [Complete proteome] [HAMAP]
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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. HAMAP MF_00180

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

fliGQ0PBJ01EBI-1195310,EBI-1191336

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3393393,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180
PRO_0000151722

Regions

Region1 – 206206DHBP synthase HAMAP MF_00180
Region27 – 282Substrate binding By similarity
Region139 – 1435Substrate binding By similarity
Region207 – 339133GTP cyclohydrolase II-like HAMAP MF_00180

Sites

Metal binding281Magnesium or manganese 1 By similarity
Metal binding281Magnesium or manganese 2 By similarity
Metal binding1421Magnesium or manganese 2 By similarity
Binding site321Substrate By similarity
Binding site1631Substrate By similarity
Site1251Essential for catalytic activity By similarity
Site1631Essential for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PHU4-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6D90CF5F6A3F3DD9

FASTA33937,925
        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 

« Hide

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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34718.1.
PIRC81404.
RefSeqYP_002344002.1.

3D structure databases

SMRQ9PHU4. Positions 2-202, 217-334.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9PHU4. 69 interactions.

Genome annotation databases

GeneID904897.
GenomeReviewsGene locus Cj0572 in contig AL111168_GR.
KEGGcje:Cj0572.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG735778.
OMAFAITHAK.
PhylomeDBQ9PHU4.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0572-MONOMER.
BRENDA4.1.99.12. 255835.

Family and domain databases

HAMAPMF_00180. RibB. Fused.
[Tree]
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlase_II.
IPR016299. Riboflavin_synth_RibA.
[Graphical view]
Gene3DG3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
PfamPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFPIRSF001259. RibA. 1 hit.
TIGRFAMsTIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBB_CAMJE
AccessionPrimary (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: February 9, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents