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Protein

tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG

Gene

mnmG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm5s2U34.3 Publications

Cofactori

FAD1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei125FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei180FADBy similarity1
Binding sitei370FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 18FADBy similarity6
Nucleotide bindingi273 – 287NADSequence analysisAdd BLAST15

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: EcoCyc

GO - Biological processi

  • response to UV Source: EcoCyc
  • tRNA methylation Source: EcoCyc
  • tRNA wobble uridine modification Source: EcoCyc

Keywordsi

Biological processtRNA processing
LigandFAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciEcoCyc:EG10375-MONOMER
MetaCyc:EG10375-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG
Alternative name(s):
Glucose-inhibited division protein A
Gene namesi
Name:mnmG
Synonyms:gidA, trmF
Ordered Locus Names:b3741, JW3719
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10375 mnmG

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13G → A: Decrease in FAD binding and partial loss of activity. Loss of activity; when associated with A-15. 1 Publication1
Mutagenesisi15G → A: Decrease in FAD binding and partial loss of activity. Loss of activity; when associated with A-13. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001170991 – 629tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmGAdd BLAST629

Proteomic databases

EPDiP0A6U3
PaxDbiP0A6U3
PRIDEiP0A6U3

Interactioni

Subunit structurei

Homodimer. Heterotetramer of two MnmE and two MnmG subunits.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
mnmEP255226EBI-550977,EBI-550986

Protein-protein interaction databases

BioGridi4263258, 181 interactors
DIPiDIP-35786N
IntActiP0A6U3, 12 interactors
STRINGi316385.ECDH10B_3928

Structurei

Secondary structure

1629
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 12Combined sources6
Helixi16 – 27Combined sources12
Beta strandi32 – 37Combined sources6
Helixi39 – 41Combined sources3
Beta strandi46 – 53Combined sources8
Helixi56 – 65Combined sources10
Helixi70 – 77Combined sources8
Beta strandi78 – 85Combined sources8
Beta strandi86 – 88Combined sources3
Helixi90 – 92Combined sources3
Beta strandi94 – 99Combined sources6
Helixi101 – 113Combined sources13
Beta strandi118 – 122Combined sources5
Beta strandi125 – 140Combined sources16
Beta strandi143 – 153Combined sources11
Turni157 – 159Combined sources3
Beta strandi162 – 164Combined sources3
Helixi182 – 188Combined sources7
Turni189 – 191Combined sources3
Beta strandi194 – 197Combined sources4
Beta strandi204 – 206Combined sources3
Helixi207 – 209Combined sources3
Helixi212 – 214Combined sources3
Beta strandi215 – 218Combined sources4
Beta strandi227 – 230Combined sources4
Helixi233 – 235Combined sources3
Beta strandi242 – 246Combined sources5
Helixi249 – 257Combined sources9
Helixi258 – 261Combined sources4
Helixi280 – 286Combined sources7
Beta strandi289 – 291Combined sources3
Beta strandi294 – 300Combined sources7
Beta strandi306 – 310Combined sources5
Helixi318 – 326Combined sources9
Beta strandi336 – 338Combined sources3
Beta strandi341 – 348Combined sources8
Helixi350 – 352Combined sources3
Beta strandi357 – 363Combined sources7
Beta strandi365 – 367Combined sources3
Helixi370 – 372Combined sources3
Helixi377 – 395Combined sources19
Turni405 – 407Combined sources3
Helixi409 – 420Combined sources12
Helixi426 – 428Combined sources3
Helixi429 – 433Combined sources5
Helixi434 – 438Combined sources5
Helixi441 – 443Combined sources3
Helixi444 – 455Combined sources12
Helixi460 – 481Combined sources22
Helixi492 – 496Combined sources5
Beta strandi499 – 501Combined sources3
Helixi509 – 513Combined sources5
Helixi520 – 523Combined sources4
Turni527 – 529Combined sources3
Helixi536 – 547Combined sources12
Turni549 – 552Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CESX-ray2.41A/B/C/D1-629[»]
3CP2X-ray2.90A1-629[»]
ProteinModelPortaliP0A6U3
SMRiP0A6U3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6U3

Family & Domainsi

Sequence similaritiesi

Belongs to the MnmG family.Curated

Phylogenomic databases

eggNOGiENOG4107RE5 Bacteria
COG0445 LUCA
HOGENOMiHOG000201059
InParanoidiP0A6U3
KOiK03495
OMAiFRPGYAI
PhylomeDBiP0A6U3

Family and domain databases

Gene3Di3.50.50.60, 2 hits
HAMAPiMF_00129 MnmG_GidA, 1 hit
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR026904 GidA-assoc_3
IPR004416 MnmG
IPR002218 MnmG-rel
IPR020595 MnmG-rel_CS
PANTHERiPTHR11806 PTHR11806, 1 hit
PTHR11806:SF0 PTHR11806:SF0, 1 hit
PfamiView protein in Pfam
PF01134 GIDA, 1 hit
PF13932 GIDA_assoc, 1 hit
SUPFAMiSSF51905 SSF51905, 2 hits
TIGRFAMsiTIGR00136 gidA, 1 hit
PROSITEiView protein in PROSITE
PS01280 GIDA_1, 1 hit
PS01281 GIDA_2, 1 hit

Sequencei

Sequence statusi: Complete.

P0A6U3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFYPDPFDVI IIGGGHAGTE AAMAAARMGQ QTLLLTHNID TLGQMSCNPA
60 70 80 90 100
IGGIGKGHLV KEVDALGGLM AKAIDQAGIQ FRILNASKGP AVRATRAQAD
110 120 130 140 150
RVLYRQAVRT ALENQPNLMI FQQAVEDLIV ENDRVVGAVT QMGLKFRAKA
160 170 180 190 200
VVLTVGTFLD GKIHIGLDNY SGGRAGDPPS IPLSRRLREL PLRVGRLKTG
210 220 230 240 250
TPPRIDARTI DFSVLAQQHG DNPMPVFSFM GNASQHPQQV PCYITHTNEK
260 270 280 290 300
THDVIRSNLD RSPMYAGVIE GVGPRYCPSI EDKVMRFADR NQHQIFLEPE
310 320 330 340 350
GLTSNEIYPN GISTSLPFDV QMQIVRSMQG MENAKIVRPG YAIEYDFFDP
360 370 380 390 400
RDLKPTLESK FIQGLFFAGQ INGTTGYEEA AAQGLLAGLN AARLSADKEG
410 420 430 440 450
WAPARSQAYL GVLVDDLCTL GTKEPYRMFT SRAEYRLMLR EDNADLRLTE
460 470 480 490 500
IGRELGLVDD ERWARFNEKL ENIERERQRL KSTWVTPSAE AAAEVNAHLT
510 520 530 540 550
APLSREASGE DLLRRPEMTY EKLTTLTPFA PALTDEQAAE QVEIQVKYEG
560 570 580 590 600
YIARQQDEIE KQLRNENTLL PATLDYRQVS GLSNEVIAKL NDHKPASIGQ
610 620
ASRISGVTPA AISILLVWLK KQGMLRRSA
Length:629
Mass (Da):69,521
Last modified:March 29, 2005 - v1
Checksum:i54FD79807E901724
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti515Missing (PubMed:6395859).Curated1
Sequence conflicti515Missing (PubMed:7686882).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01631 Genomic DNA Translation: CAA25773.1
L10328 Genomic DNA Translation: AAA62093.1
U00096 Genomic DNA Translation: AAC76764.1
AP009048 Genomic DNA Translation: BAE77547.1
K00826 Genomic DNA Translation: AAA24250.2
J01657 Genomic DNA No translation available.
PIRiF65177 BVECQA
RefSeqiNP_418197.1, NC_000913.3
WP_000499788.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76764; AAC76764; b3741
BAE77547; BAE77547; BAE77547
GeneIDi948248
KEGGiecj:JW3719
eco:b3741
PATRICifig|1411691.4.peg.2959

Similar proteinsi

Entry informationi

Entry nameiMNMG_ECOLI
AccessioniPrimary (citable) accession number: P0A6U3
Secondary accession number(s): P03816, P17112, Q2M859
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 29, 2005
Last modified: March 28, 2018
This is version 109 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health