Reviewed, UniProtKB/Swiss-Prot P0A6U3 (MNMG_ECOLI)

Names and origin

Protein names

Recommended name:
    tRNA uridine 5-carboxymethylaminomethyl modification enzyme mnmG
Alternative name(s):
    Glucose-inhibited division protein A

Gene names

Name:	mnmG
Synonyms:	gidA, trmF
Ordered Locus Names:	b3741, JW3719

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	629 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm5s2U34. Ref.7 Ref.8 Ref.9
Cofactor	FAD. Ref.9
Subunit structure	Homodimer. Heterotetramer of two mnmE and two mnmG subunits. Ref.10
Subcellular location	Cytoplasm. Ref.9
Sequence similarities	Belongs to the mnmG family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein NAD
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	tRNA wobble uridine modification Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mnmE	P25522	1	EBI-550977,EBI-550986

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 629

629

tRNA uridine 5-carboxymethylaminomethyl modification enzyme mnmG HAMAP MF_00129

PRO_0000117099

Regions

Nucleotide binding

13 – 18

6

FAD By similarity

Nucleotide binding

273 – 287

15

NAD Potential

Sites

Binding site

125

1

FAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

180

1

FAD By similarity

Binding site

370

1

FAD By similarity

Experimental info

Mutagenesis

13

1

G → A: Decrease in FAD binding and partial loss of activity. Loss of activity; when associated with A-15. Ref.9

Mutagenesis

15

1

G → A: Decrease in FAD binding and partial loss of activity. Loss of activity; when associated with A-13. Ref.9

Sequence conflict

515

1

Missing Ref.1

Sequence conflict

515

1

Missing Ref.2

Secondary structure

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629

Helix Strand Turn

Details...

Beta strand

8 – 13

6

Helix

17 – 27

11

Beta strand

32 – 35

4

Beta strand

49 – 52

4

Helix

56 – 65

10

Helix

70 – 77

8

Beta strand

78 – 84

7

Beta strand

86 – 88

3

Beta strand

94 – 99

6

Helix

101 – 113

13

Beta strand

118 – 121

4

Beta strand

126 – 131

6

Beta strand

134 – 139

6

Beta strand

145 – 147

3

Beta strand

149 – 153

5

Helix

182 – 188

7

Turn

189 – 191

3

Beta strand

197 – 201

5

Beta strand

204 – 206

3

Helix

207 – 209

3

Beta strand

215 – 218

4

Beta strand

227 – 230

4

Helix

233 – 235

3

Beta strand

242 – 245

4

Beta strand

295 – 300

6

Beta strand

306 – 309

4

Helix

318 – 326

9

Beta strand

341 – 345

5

Helix

350 – 352

3

Beta strand

357 – 363

7

Beta strand

365 – 367

3

Helix

370 – 372

3

Helix

377 – 395

19

Turn

405 – 407

3

Helix

409 – 419

11

Helix

426 – 428

3

Beta strand

431 – 433

3

Helix

434 – 438

5

Helix

444 – 453

10

Turn

454 – 456

3

Helix

460 – 482

23

Helix

492 – 495

4

Turn

496 – 498

3

Helix

509 – 513

5

Helix

520 – 525

6

Helix

527 – 529

3

Helix

536 – 547

12

Turn

549 – 552

4

Sequences

	Sequence		Length	Mass (Da)
	P0A6U3-1 [UniParc]. Last modified March 29, 2005. Version 1. Checksum: 54FD79807E901724	FASTA	629	69,521
	10 20 30 40 50 60 MFYPDPFDVI IIGGGHAGTE AAMAAARMGQ QTLLLTHNID TLGQMSCNPA IGGIGKGHLV 70 80 90 100 110 120 KEVDALGGLM AKAIDQAGIQ FRILNASKGP AVRATRAQAD RVLYRQAVRT ALENQPNLMI 130 140 150 160 170 180 FQQAVEDLIV ENDRVVGAVT QMGLKFRAKA VVLTVGTFLD GKIHIGLDNY SGGRAGDPPS 190 200 210 220 230 240 IPLSRRLREL PLRVGRLKTG TPPRIDARTI DFSVLAQQHG DNPMPVFSFM GNASQHPQQV 250 260 270 280 290 300 PCYITHTNEK THDVIRSNLD RSPMYAGVIE GVGPRYCPSI EDKVMRFADR NQHQIFLEPE 310 320 330 340 350 360 GLTSNEIYPN GISTSLPFDV QMQIVRSMQG MENAKIVRPG YAIEYDFFDP RDLKPTLESK 370 380 390 400 410 420 FIQGLFFAGQ INGTTGYEEA AAQGLLAGLN AARLSADKEG WAPARSQAYL GVLVDDLCTL 430 440 450 460 470 480 GTKEPYRMFT SRAEYRLMLR EDNADLRLTE IGRELGLVDD ERWARFNEKL ENIERERQRL 490 500 510 520 530 540 KSTWVTPSAE AAAEVNAHLT APLSREASGE DLLRRPEMTY EKLTTLTPFA PALTDEQAAE 550 560 570 580 590 600 QVEIQVKYEG YIARQQDEIE KQLRNENTLL PATLDYRQVS GLSNEVIAKL NDHKPASIGQ 610 620 ASRISGVTPA AISILLVWLK KQGMLRRSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS." Walker J.E., Gay N.J., Saraste M., Eberle A.N. Biochem. J. 224:799-815(1984) [PubMed: 6395859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R. Genomics 16:551-561(1993) [PubMed: 7686882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 515.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The replication origin region of Escherichia coli: nucleotide sequence and functional units." Buhk H.-J., Messer W. Gene 24:265-279(1983) [PubMed: 6357950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-196.
[6]	"Nucleotide sequence of Escherichia coli K-12 replication origin." Sugimoto K., Oka A., Sugisaki H., Takanami M., Nishimura A., Yasuda Y., Hirota Y. Proc. Natl. Acad. Sci. U.S.A. 76:575-579(1979) [PubMed: 370832] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5. Strain: K12.
[7]	"Novel temperature-sensitive mutants of Escherichia coli that are unable to grow in the absence of wild-type tRNA6Leu." Nakayashiki T., Inokuchi H. J. Bacteriol. 180:2931-2935(1998) [PubMed: 9603884] [Abstract] Cited for: FUNCTION.
[8]	"Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift." Bregeon D., Colot V., Radman M., Taddei F. Genes Dev. 15:2295-2306(2001) [PubMed: 11544186] [Abstract] Cited for: FUNCTION.
[9]	"Further insights into the tRNA modification process controlled by proteins MnmE and GidA of Escherichia coli." Yim L., Moukadiri I., Bjoerk G.R., Armengod M.-E. Nucleic Acids Res. 34:5892-5905(2006) [PubMed: 17062623] [Abstract] Cited for: FUNCTION, COFACTOR, INTERACTION WITH MNME, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-13 AND GLY-15. Strain: K12.
[10]	"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: 18565343] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBUNIT, NAD AND FAD BINDING.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

BVECQA. F65177.

RefSeq

AP_004046.1.
NP_418197.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CES	X-ray	2.41	A/B/C/D	1-629	[»]
3CP2	X-ray	2.90	A	1-629	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6U3. 12 interactions.

STRING

P0A6U3.

Genome annotation databases

GeneID

948248.

GenomeReviews

Gene locus JW3719 in contig AP009048_GR.
Gene locus b3741 in contig U00096_GR.

KEGG

ecj:JW3719.
eco:b3741.

Organism-specific databases

EchoBASE

EB0370.

EcoGene

EG10375. mnmG.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6U3.

OMA

GPAVWAL.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10375-MON.

Gene expression databases

Genevestigator

P0A6U3.

Family and domain databases

HAMAP

MF_00129.
[Tree]

InterPro

IPR004416. GidA.
IPR002218. GIDA-rel.
IPR020595. GIDA-rel_CS.
[Graphical view]

PANTHER

PTHR11806. GIDA. 1 hit.

Pfam

PF01134. GIDA. 1 hit.
[Graphical view]

ProDom

PD003738. GIDA. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00136. gidA. 1 hit.

PROSITE

PS01280. GIDA_1. 1 hit.
PS01281. GIDA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MNMG_ECOLI

Accession

Primary (citable) accession number: P0A6U3
Secondary accession number(s): P03816, P17112, Q2M859

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 29, 2005
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)