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Protein

Riboflavin biosynthesis protein RibC

Gene

ribC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + riboflavin = ADP + FMN.
ATP + FMN = diphosphate + FAD.

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. FMN adenylyltransferase activity Source: UniProtKB-EC
  3. riboflavin kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. FAD biosynthetic process Source: UniProtKB-UniPathway
  2. FMN biosynthetic process Source: UniProtKB-UniPathway
  3. riboflavin biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU16670-MONOMER.
MetaCyc:MONOMER-14605.
BRENDAi2.7.1.26. 658.
2.7.7.2. 658.
UniPathwayiUPA00276; UER00406.
UPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin biosynthesis protein RibC
Including the following 2 domains:
Riboflavin kinase (EC:2.7.1.26)
Alternative name(s):
Flavokinase
FMN adenylyltransferase (EC:2.7.7.2)
Alternative name(s):
FAD pyrophosphorylase
FAD synthase
Gene namesi
Name:ribC
Ordered Locus Names:BSU16670
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU16670. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Riboflavin biosynthesis protein RibCPRO_0000194133Add
BLAST

Proteomic databases

PaxDbiP54575.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU16670.

Structurei

3D structure databases

ProteinModelPortaliP54575.
SMRiP54575. Positions 1-310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RibF family.Curated

Phylogenomic databases

eggNOGiCOG0196.
HOGENOMiHOG000006844.
InParanoidiP54575.
KOiK11753.
OMAiPEKRYEK.
OrthoDBiEOG6QP0ZV.
PhylomeDBiP54575.

Family and domain databases

Gene3Di2.40.30.30. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR004821. 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]
PANTHERiPTHR22749. PTHR22749. 1 hit.
PfamiPF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
[Graphical view]
PIRSFiPIRSF004491. FAD_Synth. 1 hit.
SMARTiSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMiSSF82114. SSF82114. 1 hit.
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00083. ribF. 1 hit.

Sequencei

Sequence statusi: Complete.

P54575-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTIHITHPH HLIKEEQAKS VMALGYFDGV HLGHQKVIGT AKQIAEEKGL
60 70 80 90 100
TLAVMTFHPH PSHVLGRDKE PKDLITPLED KINQIEQLGT EVLYVVKFNE
110 120 130 140 150
VFASLSPKQF IDQYIIGLNV QHAVAGFDFT YGKYGKGTMK TMPDDLDGKA
160 170 180 190 200
GCTMVEKLTE QDKKISSSYI RTALQNGDVE LANVLLGQPY FIKGIVIHGD
210 220 230 240 250
KRGRTIGFPT ANVGLNNSYI VPPTGVYAVK AEVNGEVYNG VCNIGYKPTF
260 270 280 290 300
YEKRPEQPSI EVNLFDFNQE VYGAAIKIEW YKRIRSERKF NGIKELTEQI
310
EKDKQEAIRY FSNLRK
Length:316
Mass (Da):35,662
Last modified:August 29, 2003 - v2
Checksum:i0B8F11D356B7D7B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991G → N in CAA64624 (PubMed:9454067).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95312 Genomic DNA. Translation: CAA64624.1.
Z80835 Genomic DNA. Translation: CAB02559.1.
AL009126 Genomic DNA. Translation: CAB13540.1.
PIRiD69692.
RefSeqiNP_389549.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13540; CAB13540; BSU16670.
GeneIDi938110.
KEGGibsu:BSU16670.
PATRICi18975141. VBIBacSub10457_1762.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95312 Genomic DNA. Translation: CAA64624.1.
Z80835 Genomic DNA. Translation: CAB02559.1.
AL009126 Genomic DNA. Translation: CAB13540.1.
PIRiD69692.
RefSeqiNP_389549.1. NC_000964.3.

3D structure databases

ProteinModelPortaliP54575.
SMRiP54575. Positions 1-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU16670.

Proteomic databases

PaxDbiP54575.

Protocols and materials databases

DNASUi938110.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13540; CAB13540; BSU16670.
GeneIDi938110.
KEGGibsu:BSU16670.
PATRICi18975141. VBIBacSub10457_1762.

Organism-specific databases

GenoListiBSU16670. [Micado]

Phylogenomic databases

eggNOGiCOG0196.
HOGENOMiHOG000006844.
InParanoidiP54575.
KOiK11753.
OMAiPEKRYEK.
OrthoDBiEOG6QP0ZV.
PhylomeDBiP54575.

Enzyme and pathway databases

UniPathwayiUPA00276; UER00406.
UPA00277; UER00407.
BioCyciBSUB:BSU16670-MONOMER.
MetaCyc:MONOMER-14605.
BRENDAi2.7.1.26. 658.
2.7.7.2. 658.

Family and domain databases

Gene3Di2.40.30.30. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR004821. 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]
PANTHERiPTHR22749. PTHR22749. 1 hit.
PfamiPF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
[Graphical view]
PIRSFiPIRSF004491. FAD_Synth. 1 hit.
SMARTiSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMiSSF82114. SSF82114. 1 hit.
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00083. ribF. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [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(1996) [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.
    , 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiRIBC_BACSU
AccessioniPrimary (citable) accession number: P54575
Secondary accession number(s): P70987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 29, 2003
Last modified: April 1, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.