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
Aquifex aeolicus (strain VF5)
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 sitei126 – 1261FAD; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei181 – 1811FAD1 Publication
Binding sitei377 – 3771FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 196FAD1 Publication
Nucleotide bindingi280 – 29415NADSequence 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

BioCyciAAEO224324:GJBH-547-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:aq_761
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 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 – 617617tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmGPRO_0000117046Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48311N.
STRINGi224324.aq_761.

Structurei

Secondary structure

1
617
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Beta strandi9 – 135Combined sources
Helixi17 – 2812Combined sources
Beta strandi33 – 386Combined sources
Helixi40 – 423Combined sources
Beta strandi50 – 534Combined sources
Helixi57 – 6711Combined sources
Helixi71 – 788Combined sources
Beta strandi79 – 868Combined sources
Helixi91 – 933Combined sources
Beta strandi95 – 1006Combined sources
Helixi102 – 11413Combined sources
Beta strandi119 – 1246Combined sources
Beta strandi126 – 14116Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi150 – 1545Combined sources
Beta strandi163 – 1664Combined sources
Beta strandi169 – 1724Combined sources
Helixi184 – 1907Combined sources
Beta strandi196 – 2027Combined sources
Beta strandi205 – 2073Combined sources
Helixi208 – 2103Combined sources
Beta strandi216 – 2194Combined sources
Beta strandi230 – 2345Combined sources
Beta strandi249 – 2535Combined sources
Helixi256 – 2649Combined sources
Helixi265 – 2684Combined sources
Turni281 – 2833Combined sources
Helixi287 – 2937Combined sources
Beta strandi301 – 3066Combined sources
Beta strandi313 – 3175Combined sources
Helixi325 – 3328Combined sources
Beta strandi343 – 3453Combined sources
Beta strandi348 – 3547Combined sources
Helixi357 – 3593Combined sources
Beta strandi364 – 3707Combined sources
Beta strandi372 – 3743Combined sources
Helixi376 – 3794Combined sources
Helixi384 – 40219Combined sources
Turni412 – 4143Combined sources
Helixi416 – 42712Combined sources
Helixi435 – 4373Combined sources
Turni441 – 4455Combined sources
Helixi451 – 46111Combined sources
Beta strandi463 – 4653Combined sources
Helixi467 – 48721Combined sources
Beta strandi491 – 4966Combined sources
Beta strandi499 – 5046Combined sources
Helixi505 – 5084Combined sources
Turni509 – 5124Combined sources
Helixi515 – 5228Combined sources
Helixi530 – 55223Combined sources
Helixi554 – 5607Combined sources
Helixi570 – 5723Combined sources
Helixi578 – 58710Combined sources
Helixi592 – 5954Combined sources
Helixi603 – 61210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZXHX-ray3.20A/B1-617[»]
2ZXIX-ray2.30A/B/C/D1-617[»]
ProteinModelPortaliO66962.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66962.

Family & Domainsi

Sequence similaritiesi

Belongs to the MnmG family.Curated

Phylogenomic databases

eggNOGiENOG4107RE5. Bacteria.
COG0445. LUCA.
HOGENOMiHOG000201059.
InParanoidiO66962.
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.

O66962-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWVVDEFDV VVIGGGHAGI EAALAAARMG AKTAMFVLNA DTIGQMSCNP
60 70 80 90 100
AIGGIAKGIV VREIDALGGE MGKAIDQTGI QFKMLNTRKG KAVQSPRAQA
110 120 130 140 150
DKKRYREYMK KVCENQENLY IKQEEVVDII VKNNQVVGVR TNLGVEYKTK
160 170 180 190 200
AVVVTTGTFL NGVIYIGDKM IPGGRLGEPR SEGLSDFYRR FDFPLIRFKT
210 220 230 240 250
GTPARLDKRT IDFSALEVAP GDDPPPKFSF WTEPVGSYWF PKGKEQVNCW
260 270 280 290 300
ITYTTPKTHE IIRKNLHRTA LYGGLIKGIG PRYCPSIEDK IVKFPDKERH
310 320 330 340 350
QIFLEPEGLD TIEIYPNGLS TSLPEEVQWE MYRSIPGLEN VVLIRPAYAI
360 370 380 390 400
EYDVVPPTEL YPTLETKKIR GLFHAGNFNG TTGYEEAAGQ GIVAGINAAL
410 420 430 440 450
RAFGKEPIYL RRDESYIGVM IDDLTTKGVT EPYRLFTSRS EYRLYIRQDN
460 470 480 490 500
AILRLAKLGR ELGLLSEEQY KLVKELEREI EKWKEFYKSE RVSVAVGGDT
510 520 530 540 550
RSYSVATLMT MNYTLDDVKE KFGYEVPQHP YVKEEVEIQL KYEPYIERER
560 570 580 590 600
KLNEKLKKLE DTKIPPDIDY DKIPGLTKEA REKLKKFKPI TVGQASRIDG
610
ITPAAITALL VYLGKLD
Length:617
Mass (Da):69,644
Last modified:August 1, 1998 - v1
Checksum:i1DAB1BDFEFCBA6DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06917.1.
PIRiG70366.
RefSeqiNP_213523.1. NC_000918.1.
WP_010880461.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC06917; AAC06917; aq_761.
GeneIDi1193412.
KEGGiaae:aq_761.
PATRICi20958950. VBIAquAeo85532_0606.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06917.1.
PIRiG70366.
RefSeqiNP_213523.1. NC_000918.1.
WP_010880461.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZXHX-ray3.20A/B1-617[»]
2ZXIX-ray2.30A/B/C/D1-617[»]
ProteinModelPortaliO66962.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48311N.
STRINGi224324.aq_761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC06917; AAC06917; aq_761.
GeneIDi1193412.
KEGGiaae:aq_761.
PATRICi20958950. VBIAquAeo85532_0606.

Phylogenomic databases

eggNOGiENOG4107RE5. Bacteria.
COG0445. LUCA.
HOGENOMiHOG000201059.
InParanoidiO66962.
KOiK03495.
OMAiFRPGYAI.
OrthoDBiEOG6W9X6J.

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-547-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO66962.

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: VF5.
  2. "Crystal structure of gidA from Aquifex aeolicus."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JAN-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT.

Entry informationi

Entry nameiMNMG_AQUAE
AccessioniPrimary (citable) accession number: O66962
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: January 20, 2016
This is version 104 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.