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P0AFU9

- RISA_SHIFL

UniProt

P0AFU9 - RISA_SHIFL

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Protein

Riboflavin synthase

Gene

ribE

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.By similarity

Catalytic activityi

2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine.

Pathwayi

GO - Molecular functioni

  1. oxidoreductase activity Source: InterPro
  2. riboflavin synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. riboflavin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Riboflavin biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00275; UER00405.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin synthase (EC:2.5.1.9)
Short name:
RS
Gene namesi
Name:ribE
Synonyms:ribC
Ordered Locus Names:SF1690, S1822
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Riboflavin synthasePRO_0000068172Add
BLAST

Proteomic databases

PaxDbiP0AFU9.
PRIDEiP0AFU9.

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

STRINGi198214.SF1690.

Structurei

3D structure databases

ProteinModelPortaliP0AFU9.
SMRiP0AFU9. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 9797Lumazine-binding 1Add
BLAST
Repeati98 – 19598Lumazine-binding 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 63Substrate bindingBy similarity
Regioni48 – 503Substrate bindingBy similarity
Regioni62 – 676Substrate bindingBy similarity

Sequence similaritiesi

Contains 2 lumazine-binding repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0307.
HOGENOMiHOG000151758.
KOiK00793.
OMAiNHQIWFR.
OrthoDBiEOG6VMTQH.

Family and domain databases

Gene3Di2.40.30.20. 2 hits.
InterProiIPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR21098. PTHR21098. 1 hit.
PfamiPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFiPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMiSSF63380. SSF63380. 2 hits.
TIGRFAMsiTIGR00187. ribE. 1 hit.
PROSITEiPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AFU9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFTGIVQGTA KLVSIDEKPN FRTHVVELPD HMLDGLETGA SVAHNGCCLT
60 70 80 90 100
VTEINGNHVS FDLMKETLRI TNLGDLKVGD WVNVERAAKF SDEIGGHLMS
110 120 130 140 150
GHIMTTAEVA KILTSENNRQ IWFKVQDSQL MKYILYKGFI GIDGISLTVG
160 170 180 190 200
EVTPTRFCVH LIPETLERTT LGKKKLGARV NIEIDPQTQA VVDTVERVLA
210
ARENAMNQPG TEA
Length:213
Mass (Da):23,445
Last modified:December 20, 2005 - v1
Checksum:iCD1C7E40E4AC88B6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN43269.1.
AE014073 Genomic DNA. Translation: AAP17158.1.
RefSeqiNP_707562.1. NC_004337.2.
NP_837349.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN43269; AAN43269; SF1690.
AAP17158; AAP17158; S1822.
GeneIDi1024885.
1078160.
KEGGisfl:SF1690.
sfx:S1822.
PATRICi18705046. VBIShiFle31049_2021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN43269.1 .
AE014073 Genomic DNA. Translation: AAP17158.1 .
RefSeqi NP_707562.1. NC_004337.2.
NP_837349.1. NC_004741.1.

3D structure databases

ProteinModelPortali P0AFU9.
SMRi P0AFU9. Positions 1-206.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198214.SF1690.

Proteomic databases

PaxDbi P0AFU9.
PRIDEi P0AFU9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN43269 ; AAN43269 ; SF1690 .
AAP17158 ; AAP17158 ; S1822 .
GeneIDi 1024885.
1078160.
KEGGi sfl:SF1690.
sfx:S1822.
PATRICi 18705046. VBIShiFle31049_2021.

Phylogenomic databases

eggNOGi COG0307.
HOGENOMi HOG000151758.
KOi K00793.
OMAi NHQIWFR.
OrthoDBi EOG6VMTQH.

Enzyme and pathway databases

UniPathwayi UPA00275 ; UER00405 .

Family and domain databases

Gene3Di 2.40.30.20. 2 hits.
InterProi IPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
PANTHERi PTHR21098. PTHR21098. 1 hit.
Pfami PF00677. Lum_binding. 2 hits.
[Graphical view ]
PIRSFi PIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMi SSF63380. SSF63380. 2 hits.
TIGRFAMsi TIGR00187. ribE. 1 hit.
PROSITEi PS51177. LUMAZINE_BIND. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiRISA_SHIFL
AccessioniPrimary (citable) accession number: P0AFU9
Secondary accession number(s): P29015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: October 1, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3