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P54575 (RIBC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Riboflavin biosynthesis protein RibC

Including the following 2 domains:

  1. Riboflavin kinase
    EC=2.7.1.26
    Alternative name(s):
    Flavokinase
  2. FMN adenylyltransferase
    EC=2.7.7.2
    Alternative name(s):
    FAD pyrophosphorylase
    FAD synthase
Gene names
Name:ribC
Ordered Locus Names:BSU16670
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + riboflavin = ADP + FMN.

ATP + FMN = diphosphate + FAD.

Pathway

Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.

Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.

Sequence similarities

Belongs to the RibF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Riboflavin biosynthesis protein RibC
PRO_0000194133

Experimental info

Sequence conflict1991G → N in CAA64624. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54575 [UniParc].

Last modified August 29, 2003. Version 2.
Checksum: 0B8F11D356B7D7B9

FASTA31635,662
        10         20         30         40         50         60 
MKTIHITHPH HLIKEEQAKS VMALGYFDGV HLGHQKVIGT AKQIAEEKGL TLAVMTFHPH 

        70         80         90        100        110        120 
PSHVLGRDKE PKDLITPLED KINQIEQLGT EVLYVVKFNE VFASLSPKQF IDQYIIGLNV 

       130        140        150        160        170        180 
QHAVAGFDFT YGKYGKGTMK TMPDDLDGKA GCTMVEKLTE QDKKISSSYI RTALQNGDVE 

       190        200        210        220        230        240 
LANVLLGQPY FIKGIVIHGD KRGRTIGFPT ANVGLNNSYI VPPTGVYAVK AEVNGEVYNG 

       250        260        270        280        290        300 
VCNIGYKPTF YEKRPEQPSI EVNLFDFNQE VYGAAIKIEW YKRIRSERKF NGIKELTEQI 

       310 
EKDKQEAIRY FSNLRK

« Hide

References

« Hide 'large scale' references
[1]"Primary structure and functional activity of the Bacillus subtilis ribC gene."
Gusarov I.I., Kreneva R.A., Rybak K.V., Podcherniaev D.A., Iomantas I.U.V., Kolibaba L.G., Polanuer B.M., Kozlov I.U.I., Perumov D.A.
Mol. Biol. (Mosk.) 31:820-825(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Molecular cloning and characterisation of the ribC gene from Bacillus subtilis: a point mutation in ribC results in riboflavin overproduction."
Coquard D., Huecas M., Ott M., van Dijl J.M., van Loon A.P., Hohmann H.P.
Mol. Gen. Genet. 254:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X95312 Genomic DNA. Translation: CAA64624.1.
Z80835 Genomic DNA. Translation: CAB02559.1.
AL009126 Genomic DNA. Translation: CAB13540.1.
PIRD69692.
RefSeqNP_389549.1. NC_000964.3.

3D structure databases

ProteinModelPortalP54575.
SMRP54575. Positions 1-310.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU16670.

Proteomic databases

PaxDbP54575.

Protocols and materials databases

DNASU938110.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13540; CAB13540; BSU16670.
GeneID938110.
KEGGbsu:BSU16670.
PATRIC18975141. VBIBacSub10457_1762.

Organism-specific databases

GenoListBSU16670. [Micado]

Phylogenomic databases

eggNOGCOG0196.
HOGENOMHOG000006844.
KOK11753.
OMAIRDEQPF.
ProtClustDBPRK05627.

Enzyme and pathway databases

BioCycBSUB:BSU16670-MONOMER.
MetaCyc:MONOMER-14605.
UniPathwayUPA00276; UER00406.
UPA00277; UER00407.

Family and domain databases

Gene3D2.40.30.30. 1 hit.
3.40.50.620. 1 hit.
InterProIPR004821. Cyt_trans-like.
IPR015864. FAD_synthase.
IPR023468. Riboflavin_kinase.
IPR002606. Riboflavin_kinase_bac.
IPR015865. Riboflavin_kinase_bac/euk.
IPR023465. Riboflavin_kinase_domain.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR22749. PTHR22749. 1 hit.
PfamPF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
[Graphical view]
PIRSFPIRSF004491. FAD_Synth. 1 hit.
SMARTSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMSSF82114. Riboflavin_kinase. 1 hit.
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00083. ribF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBC_BACSU
AccessionPrimary (citable) accession number: P54575
Secondary accession number(s): P70987
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 29, 2003
Last modified: May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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