Click here to switch to the map view.

The map label for this gene is ribH

Identifier: 52786211

GI number: 52786211

Start: 2405545

End: 2406009

Strand: Reverse

Name: ribH

Synonym: BLi02472

Alternate gene names: 52786211

Gene position: 2406009-2405545 (Counterclockwise)

Preceding gene: 52786212

Following gene: 52786210

Centisome position: 56.98

GC content: 49.25

Gene sequence:

>465_bases
ATGAATAAAATAGAAGGTCATGTAATTGGAACAGATTTGAAAATTGGGATCGTTGTGTCAAGGTTCAACGATTTTATTAC
AAGCAAACTTCTAAGCGGCGCAGAAGACACGCTGTTGAGACATGGGGTCAAAGCTGATGATATTGATGTCGCCTGGGTTC
CCGGCGCTTTCGAAATTCCGCTCATCGCCAAAAAAATGGCTGAAACGAAAAAATACGACGCAGTGATTACGCTGGGCACG
GTTATCAGAGGAGCGACAAGCCACTATGACTATGTCTGCAATGAAGCGGCTAAGGGGATTGCAGCGAGCAGCATGTCAAC
AGGCGTTCCGGTGATCTTCGGCGTATTGACGACAGACACGATCGAGCAGGCGGTCGAACGCGCCGGAACAAAAGCCGGAA
ATAAAGGTGCAGAAGCTGCCGCGGCAGCGATTGAAATGGCGAACCTGACCCGGTCGCTTCAATAA

Upstream 100 bases:

>100_bases
AAAAAAGATAATGAAAAGTATCTAAAAACGAAAAAATCAAAATTGGGGCATATGCTTCATTTTTAAACTAAAATCAATCA
CAAAAAAGGACGGGATTCAT

Downstream 100 bases:

>100_bases
TTGCCGAAAAAGAGTTTAAAAAGGTTATAAAAATGTTTATAATGTGATGTGAAGCGACTAGCCTTCGTTAGATCCACATT
TTGATATATTGAGGGGTATT

Product: 6,7-dimethyl-8-ribityllumazine synthase

Products: NA

Alternate protein names: DMRL synthase; Lumazine synthase; Riboflavin synthase beta chain

Number of amino acids: Translated: 154; Mature: 154

Protein sequence:

>154_residues
MNKIEGHVIGTDLKIGIVVSRFNDFITSKLLSGAEDTLLRHGVKADDIDVAWVPGAFEIPLIAKKMAETKKYDAVITLGT
VIRGATSHYDYVCNEAAKGIAASSMSTGVPVIFGVLTTDTIEQAVERAGTKAGNKGAEAAAAAIEMANLTRSLQ

Sequences:

>Translated_154_residues
MNKIEGHVIGTDLKIGIVVSRFNDFITSKLLSGAEDTLLRHGVKADDIDVAWVPGAFEIPLIAKKMAETKKYDAVITLGT
VIRGATSHYDYVCNEAAKGIAASSMSTGVPVIFGVLTTDTIEQAVERAGTKAGNKGAEAAAAAIEMANLTRSLQ
>Mature_154_residues
MNKIEGHVIGTDLKIGIVVSRFNDFITSKLLSGAEDTLLRHGVKADDIDVAWVPGAFEIPLIAKKMAETKKYDAVITLGT
VIRGATSHYDYVCNEAAKGIAASSMSTGVPVIFGVLTTDTIEQAVERAGTKAGNKGAEAAAAAIEMANLTRSLQ

Specific function: Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)- ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2- butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The beta subunit catalyzes

COG id: COG0054

COG function: function code H; Riboflavin synthase beta-chain

Gene ontology:

Cell location: Cytoplasm [C]

Metaboloic importance: Non_Essential [C]

Operon status: Not Known

Operon components: None

Similarity: Belongs to the DMRL synthase family

Homologues:

Organism=Escherichia coli, GI1786617, Length=155, Percent_Identity=55.4838709677419, Blast_Score=174, Evalue=3e-45,
Organism=Saccharomyces cerevisiae, GI6324429, Length=147, Percent_Identity=34.0136054421769, Blast_Score=92, Evalue=3e-20,

Paralogues:

None

Copy number: NA

Swissprot (AC and ID): RISB_BACLD (Q65HW7)

Other databases:

- EMBL:   CP000002
- EMBL:   AE017333
- RefSeq:   YP_079631.1
- RefSeq:   YP_092040.1
- HSSP:   P11998
- ProteinModelPortal:   Q65HW7
- SMR:   Q65HW7
- STRING:   Q65HW7
- EnsemblBacteria:   EBBACT00000054668
- EnsemblBacteria:   EBBACT00000062174
- GeneID:   3028563
- GeneID:   3099511
- GenomeReviews:   AE017333_GR
- GenomeReviews:   CP000002_GR
- KEGG:   bld:BLi02472
- KEGG:   bli:BL01888
- NMPDR:   fig|279010.5.peg.318
- eggNOG:   COG0054
- GeneTree:   EBGT00050000002577
- HOGENOM:   HBG311126
- OMA:   KAGNKGW
- ProtClustDB:   PRK00061
- BioCyc:   BLIC279010-1:BLI02472-MONOMER
- BioCyc:   BLIC279010:BL01888-MONOMER
- HAMAP:   MF_00178
- InterPro:   IPR002180
- Gene3D:   G3DSA:3.40.50.960
- PANTHER:   PTHR21058
- TIGRFAMs:   TIGR00114

Pfam domain/function: PF00885 DMRL_synthase; SSF52121 DMRL_synthase

EC number: =2.5.1.9

Molecular weight: Translated: 16207; Mature: 16207

Theoretical pI: Translated: 6.26; Mature: 6.26

Prosite motif: NA

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

0.6 %Cys     (Translated Protein)
2.6 %Met     (Translated Protein)
3.2 %Cys+Met (Translated Protein)
0.6 %Cys     (Mature Protein)
2.6 %Met     (Mature Protein)
3.2 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MNKIEGHVIGTDLKIGIVVSRFNDFITSKLLSGAEDTLLRHGVKADDIDVAWVPGAFEIP
CCCCCCEEECCCEEEEHHHHHHHHHHHHHHHCCHHHHHHHCCCCCCCCEEEEECCCCCCH
LIAKKMAETKKYDAVITLGTVIRGATSHYDYVCNEAAKGIAASSMSTGVPVIFGVLTTDT
HHHHHHHHHHHHHHEEEHHHHHHCCCCHHHHHHHHHHCCCCCCCCCCCCHHHHHHHHHHH
IEQAVERAGTKAGNKGAEAAAAAIEMANLTRSLQ
HHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHCCC
>Mature Secondary Structure
MNKIEGHVIGTDLKIGIVVSRFNDFITSKLLSGAEDTLLRHGVKADDIDVAWVPGAFEIP
CCCCCCEEECCCEEEEHHHHHHHHHHHHHHHCCHHHHHHHCCCCCCCCEEEEECCCCCCH
LIAKKMAETKKYDAVITLGTVIRGATSHYDYVCNEAAKGIAASSMSTGVPVIFGVLTTDT
HHHHHHHHHHHHHHEEEHHHHHHCCCCHHHHHHHHHHCCCCCCCCCCCCHHHHHHHHHHH
IEQAVERAGTKAGNKGAEAAAAAIEMANLTRSLQ
HHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHCCC

PDB accession: NA

Resolution: NA

Structure class: Unstructured

Cofactors: NA

Metal ions: NA

Kcat value (1/min): NA

Specific activity: NA

Km value (mM): NA

Substrates: NA

Specific reaction: NA

General reaction: NA

Inhibitor: NA

Structure determination priority: 10.0

TargetDB status: NA

Availability: NA

References: NA