Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG

Gene

mnmG

Organism
Bartonella quintana (strain Toulouse) (Rochalimaea quintana)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm5s2U34.UniRule annotation

Cofactori

FADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156FADUniRule annotation
Nucleotide bindingi269 – 28315NADUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciBQUI283165:GHZA-1354-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmGUniRule annotation
Alternative name(s):
Glucose-inhibited division protein AUniRule annotation
Gene namesi
Name:mnmGUniRule annotation
Synonyms:gidAUniRule annotation
Ordered Locus Names:BQ13560
OrganismiBartonella quintana (strain Toulouse) (Rochalimaea quintana)
Taxonomic identifieri283165 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
Proteomesi
  • UP000000597 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmGPRO_0000117060Add
BLAST

Proteomic databases

PRIDEiQ6FYB9.

Interactioni

Subunit structurei

Homodimer. Heterotetramer of two MnmE and two MnmG subunits.UniRule annotation

Protein-protein interaction databases

STRINGi283165.BQ13560.

Structurei

3D structure databases

ProteinModelPortaliQ6FYB9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MnmG family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107RE5. Bacteria.
COG0445. LUCA.
HOGENOMiHOG000201059.
KOiK03495.
OMAiFRPGYAI.
OrthoDBiPOG091H01O0.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_00129. MnmG_GidA. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR026904. GidA-assoc_3.
IPR004416. MnmG.
IPR002218. MnmG-rel.
IPR020595. MnmG-rel_CS.
[Graphical view]
PfamiPF01134. GIDA. 1 hit.
PF13932. GIDA_assoc. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR00136. gidA. 1 hit.
PROSITEiPS01280. GIDA_1. 1 hit.
PS01281. GIDA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6FYB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLYDVVIIG GGHAGCEAAS ASARSGACTA LVTHKISALG TMSCNPAIGG
60 70 80 90 100
LGKGHLVREI DALDGLMGRA ADIAGIQFRL LNRRKGPAVR GPRTQADRKL
110 120 130 140 150
YKKAIQKFLQ EQDNLILIED EAVDLIVKDN CVSGVVLKKQ GELFSGAVVL
160 170 180 190 200
TTGTFLNGLI HIGDKTWAAG RMGEHSSVQL AERLKKYDIN LGRLKTGTPA
210 220 230 240 250
RLSKKTINWN CLSKQKADED PVPFSLLTEK IEQPQIECAI TRTNTQTHQI
260 270 280 290 300
IRENIHRSAL YSGMIEGLGP RYCPSVEDKI VKFGERDGHQ IFLEPEGLND
310 320 330 340 350
DTIYPNGLST SLPEDVQVAL LRTIEGLESV KILQPGYAIE YDFVNPQQLT
360 370 380 390 400
KTLELRSLPG LFLAGQINGT TGYEEAAAQG LLAGLNAARK VGGLNEIIIS
410 420 430 440 450
RSTAYIGVMV DDLVSRGVSE PYRMFTSRAE FRLSLRSDNA DARLTPLAQQ
460 470 480 490 500
WGIVSQKRWD LYQQKQQRLD QARSICQKLF LTPNQASAHG LQVNHDGIRR
510 520 530 540 550
SAYDLLAYPH MSIERLSHFW QQLQSIDPKT VESLEIEAQY AVYLEKQAQD
560 570 580 590 600
ISALQRDERL EIPSSLDFQT ISGLSNELKT KIQKISPRSI ADAQKIDGMT
610 620
PAALSLIITY IQRQRREKAE SA
Length:622
Mass (Da):68,725
Last modified:July 19, 2004 - v1
Checksum:i9A32E94CE8B4B798
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX897700 Genomic DNA. Translation: CAF26814.1.
RefSeqiWP_011179968.1. NC_005955.1.

Genome annotation databases

EnsemblBacteriaiCAF26814; CAF26814; BQ13560.
KEGGibqu:BQ13560.
PATRICi31954189. VBIBarQui58630_1491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX897700 Genomic DNA. Translation: CAF26814.1.
RefSeqiWP_011179968.1. NC_005955.1.

3D structure databases

ProteinModelPortaliQ6FYB9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi283165.BQ13560.

Proteomic databases

PRIDEiQ6FYB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAF26814; CAF26814; BQ13560.
KEGGibqu:BQ13560.
PATRICi31954189. VBIBarQui58630_1491.

Phylogenomic databases

eggNOGiENOG4107RE5. Bacteria.
COG0445. LUCA.
HOGENOMiHOG000201059.
KOiK03495.
OMAiFRPGYAI.
OrthoDBiPOG091H01O0.

Enzyme and pathway databases

BioCyciBQUI283165:GHZA-1354-MONOMER.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_00129. MnmG_GidA. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR026904. GidA-assoc_3.
IPR004416. MnmG.
IPR002218. MnmG-rel.
IPR020595. MnmG-rel_CS.
[Graphical view]
PfamiPF01134. GIDA. 1 hit.
PF13932. GIDA_assoc. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR00136. gidA. 1 hit.
PROSITEiPS01280. GIDA_1. 1 hit.
PS01281. GIDA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMNMG_BARQU
AccessioniPrimary (citable) accession number: Q6FYB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 19, 2004
Last modified: September 7, 2016
This is version 79 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.