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Protein

tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG

Gene

mnmG

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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.By similarity

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201FAD; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei366 – 3661FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 136FAD1 Publication
Nucleotide bindingi269 – 28315NADSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciCTEP194439:GHN0-2332-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
Ordered Locus Names:CT2283
OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000001007 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 621621tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmGPRO_0000117086Add
BLAST

Interactioni

Subunit structurei

Homodimer. Heterotetramer of two MnmE and two MnmG subunits (By similarity).By similarity

Protein-protein interaction databases

STRINGi194439.CT2283.

Structurei

Secondary structure

1
621
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi11 – 2212Combined sources
Beta strandi27 – 326Combined sources
Helixi34 – 363Combined sources
Beta strandi44 – 474Combined sources
Helixi49 – 6113Combined sources
Helixi65 – 728Combined sources
Beta strandi73 – 797Combined sources
Beta strandi81 – 833Combined sources
Turni85 – 873Combined sources
Beta strandi89 – 946Combined sources
Helixi96 – 10813Combined sources
Beta strandi113 – 1175Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi129 – 1357Combined sources
Beta strandi140 – 1489Combined sources
Beta strandi157 – 1604Combined sources
Beta strandi163 – 1664Combined sources
Beta strandi168 – 1703Combined sources
Helixi179 – 1857Combined sources
Beta strandi190 – 1978Combined sources
Beta strandi200 – 2023Combined sources
Helixi203 – 2053Combined sources
Turni208 – 2103Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi223 – 2264Combined sources
Helixi231 – 2333Combined sources
Beta strandi238 – 2425Combined sources
Helixi245 – 2528Combined sources
Turni253 – 2575Combined sources
Helixi277 – 2826Combined sources
Beta strandi290 – 2978Combined sources
Beta strandi302 – 3065Combined sources
Helixi314 – 3218Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi337 – 3448Combined sources
Helixi346 – 3483Combined sources
Beta strandi353 – 3597Combined sources
Beta strandi361 – 3633Combined sources
Helixi366 – 3683Combined sources
Helixi373 – 39220Combined sources
Turni401 – 4033Combined sources
Helixi405 – 41511Combined sources
Turni424 – 4263Combined sources
Helixi433 – 4353Combined sources
Helixi437 – 4393Combined sources
Helixi440 – 45011Combined sources
Helixi456 – 47823Combined sources
Helixi483 – 49311Combined sources
Helixi505 – 5084Combined sources
Beta strandi509 – 5124Combined sources
Helixi515 – 5195Combined sources
Helixi523 – 5286Combined sources
Helixi531 – 5344Combined sources
Helixi536 – 54712Combined sources
Helixi549 – 56517Combined sources
Beta strandi572 – 5743Combined sources
Helixi586 – 5938Combined sources
Helixi598 – 6014Combined sources
Helixi609 – 6168Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CP8X-ray3.20A/B/C/D1-621[»]
ProteinModelPortaliQ8KA85.
SMRiQ8KA85. Positions 1-619.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8KA85.

Family & Domainsi

Sequence similaritiesi

Belongs to the MnmG family.Curated

Phylogenomic databases

eggNOGiENOG4105CWE. Bacteria.
COG0445. LUCA.
HOGENOMiHOG000201060.
KOiK03495.
OMAiFRPGYAI.
OrthoDBiEOG6W9X6J.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_00129. MnmG_GidA.
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.

Q8KA85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYDVIVVGAG HAGCEAALAV ARGGLHCLLI TSDLSAVARM SCNPAIGGVA
60 70 80 90 100
KGQITREIDA LGGEMGKAID ATGIQFRMLN RSKGPAMHSP RAQADKTQYS
110 120 130 140 150
LYMRRIVEHE PNIDLLQDTV IGVSANSGKF SSVTVRSGRA IQAKAAILAC
160 170 180 190 200
GTFLNGLIHI GMDHFPGGRS TAEPPVEGLT ESLASLGFSF GRLKTGTPPR
210 220 230 240 250
IDSRSVDYTI VTEQPGDVDP VPFSFSSTSV ANRNLVSCYL TKTTEKTHDI
260 270 280 290 300
LRTGFDRSPL FTGKVQGVGP RYCPSIEDKI SRFPDKSSHH IFLEPEGTDT
310 320 330 340 350
VEMYVNGFST SLPEDIQIAG LRSIPGLEEA KMIRPGYAIE YDFFHPWQIR
360 370 380 390 400
STMETRPVEN LFFAGQINGT SGYEEAAAQG LMAGINAVRK ILGKELIVLG
410 420 430 440 450
RDQAYIGVLI DDLITKETKE PYRMFTSSAE HRLILRHDNA DLRLRKIGYD
460 470 480 490 500
CNLVSSDDLH RTESIIKRVQ HCLEVMKTAK VTPAEINTLL MNKGLQELKT
510 520 530 540 550
PARALSLIKR PGISLQDILE HSLSVRSAAE ELCNDPRVAE QVQIEIKYEG
560 570 580 590 600
YIKREQLVAD RIARLDSLHI PDNFNYDSLN SLSSEGREKL LKHRPATIGQ
610 620
ASRILGVSPS DVSILMIRLG R
Length:621
Mass (Da):68,097
Last modified:October 1, 2002 - v1
Checksum:i752ED5CA7F9A38BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM73496.1.
RefSeqiNP_663154.1. NC_002932.3.
WP_010933931.1. NC_002932.3.

Genome annotation databases

EnsemblBacteriaiAAM73496; AAM73496; CT2283.
GeneIDi1007276.
KEGGicte:CT2283.
PATRICi21402363. VBIChlTep116050_2076.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM73496.1.
RefSeqiNP_663154.1. NC_002932.3.
WP_010933931.1. NC_002932.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CP8X-ray3.20A/B/C/D1-621[»]
ProteinModelPortaliQ8KA85.
SMRiQ8KA85. Positions 1-619.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi194439.CT2283.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM73496; AAM73496; CT2283.
GeneIDi1007276.
KEGGicte:CT2283.
PATRICi21402363. VBIChlTep116050_2076.

Phylogenomic databases

eggNOGiENOG4105CWE. Bacteria.
COG0445. LUCA.
HOGENOMiHOG000201060.
KOiK03495.
OMAiFRPGYAI.
OrthoDBiEOG6W9X6J.

Enzyme and pathway databases

BioCyciCTEP194439:GHN0-2332-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8KA85.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_00129. MnmG_GidA.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49652 / DSM 12025 / NBRC 103806 / TLS.
  2. "Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate."
    Meyer S., Scrima A., Versees W., Wittinghofer A.
    J. Mol. Biol. 380:532-547(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT.

Entry informationi

Entry nameiMNMG_CHLTE
AccessioniPrimary (citable) accession number: Q8KA85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: October 1, 2002
Last modified: January 20, 2016
This is version 83 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.