P30870 (GLNE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate-ammonia-ligase adenylyltransferase
EC=2.7.7.42

Alternative name(s):
Glutamine-synthetase adenylyltransferase
Short name=ATase
[Glutamate--ammonia-ligase] adenylyltransferase

Gene names

Name:	glnE
Ordered Locus Names:	b3053, JW3025

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	946 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adenylation and deadenylation of glutamate--ammonia ligase. Ref.1
Catalytic activity	ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]. HAMAP MF_00802
Sequence similarities	Belongs to the glnE family.

Ontologies

Keywords
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW [glutamate-ammonia-ligase] adenylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 946

946

Glutamate-ammonia-ligase adenylyltransferase HAMAP MF_00802

PRO_0000209244

Regions

Region

91 – 302

212

GlnE 1 HAMAP MF_00802

Region

609 – 830

222

GlnE 2 HAMAP MF_00802

Experimental info

Sequence conflict

524

1

Missing in CAA79892. Ref.1

Sequence conflict

624 – 625

2

QL → PV in CAA79892. Ref.1

Secondary structure

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946

Helix Strand Turn

Details...

Helix

6 – 16

11

Helix

25 – 27

3

Helix

30 – 38

9

Helix

40 – 48

9

Helix

51 – 58

8

Helix

63 – 68

6

Helix

69 – 76

8

Turn

77 – 79

3

Helix

83 – 106

24

Helix

112 – 141

30

Beta strand

156 – 159

4

Helix

161 – 164

4

Beta strand

174 – 180

7

Helix

195 – 211

17

Helix

230 – 232

3

Beta strand

235 – 238

4

Helix

239 – 249

11

Helix

252 – 258

7

Beta strand

262 – 265

4

Helix

270 – 283

14

Helix

290 – 310

21

Turn

316 – 318

3

Helix

323 – 337

15

Turn

338 – 340

3

Helix

342 – 344

3

Helix

349 – 358

10

Helix

364 – 385

22

Turn

386 – 389

4

Helix

399 – 408

10

Helix

414 – 434

21

Sequences

	Sequence		Length	Mass (Da)
	P30870 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 6FD2D7BDC619DB83	FASTA	946	108,418
	10 20 30 40 50 60 MKPLSSPLQQ YWQTVVERLP EPLAEESLSA QAKSVLTFSD FVQDSVIAHP EWLTELESQP 70 80 90 100 110 120 PQADEWQHYA AWLQEALCNV SDEAGLMREL RLFRRRIMVR IAWAQTLALV TEESILQQLS 130 140 150 160 170 180 YLAETLIVAA RDWLYDACCR EWGTPCNAQG EAQPLLILGM GKLGGGELNF SSDIDLIFAW 190 200 210 220 230 240 PEHGCTQGGR RELDNAQFFT RMGQRLIKVL DQPTQDGFVY RVDMRLRPFG ESGPLVLSFA 250 260 270 280 290 300 ALEDYYQEQG RDWERYAMVK ARIMGDSEGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK 310 320 330 340 350 360 GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLSAIAELH 370 380 390 400 410 420 LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL NRARLAWAMD FADWPQLTGA 430 440 450 460 470 480 LTAHMTNVRR VFNELIGDDE SETQEESLSE QWRELWQDAL QEDDTTPVLA HLSEDDRKQV 490 500 510 520 530 540 LTLIADFRKE LDKRTIGPRG RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT 550 560 570 580 590 600 YLELLSEFPA ALKHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ 610 620 630 640 650 660 YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA EAMIDAVVQQ 670 680 690 700 710 720 AWVQMVARYG KPNHLNEREG RGFAVVGYGK LGGWELGYSS DLDLIFLHDC PMDAMTDGER 730 740 750 760 770 780 EIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTSAEA FADYQKNEAW 790 800 810 820 830 840 TWEHQALVRA RVVYGDPQLT AHFDAVRREI MTLPREGKTL QTEVREMREK MRAHLGNKHR 850 860 870 880 890 900 DRFDIKADEG GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMAL 910 920 930 940 TRAYTTLRDE LHHLALQELP GHVSEDCFTA ERELVRASWQ KWLVEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli." van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D. Mol. Microbiol. 9:443-458(1993) [PubMed: 8412694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: K12 / CS520.
[2]	"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]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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.
[4]	"Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase." Xu Y., Zhang R., Joachimiak A., Carr P.D., Huber T., Vasudevan S.G., Ollis D.L. Structure 12:861-869(2004) [PubMed: 15130478] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-440.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z21844 Genomic DNA. Translation: CAA79892.1.
U00096 Genomic DNA. Translation: AAC76089.1.
AP009048 Genomic DNA. Translation: BAE77104.1.

PIR

C65093.

RefSeq

NP_417525.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V4A	X-ray	2.00	A	1-440	[»]
3K7D	X-ray	2.40	A/B	449-946	[»]

ProteinModelPortal

P30870.

SMR

P30870. Positions 1-437, 449-945.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9780N.

IntAct

P30870. 2 interactions.

PTM databases

PhosSite

P30870.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001929; EBESCP00000001929; EBESCG00000001582.
EBESCT00000014398; EBESCP00000013689; EBESCG00000013459.

GeneID

947552.

GenomeReviews

Gene locus JW3025 in contig AP009048_GR.
Gene locus b3053 in contig U00096_GR.

KEGG

ecj:JW3025.
eco:b3053.

PATRIC

32121518. VBIEscCol129921_3146.

Organism-specific databases

EchoBASE

EB1559.

EcoGene

EG11602. glnE.

Phylogenomic databases

eggNOG

COG1391.

GeneTree

EBGT00050000010757.

HOGENOM

HBG687047.

OMA

VEHRIQM.

PhylomeDB

P30870.

ProtClustDB

PRK11072.

Enzyme and pathway databases

BioCyc

EcoCyc:GLNE-MONOMER.
MetaCyc:GLNE-MONOMER.

Gene expression databases

Genevestigator

P30870.

Family and domain databases

HAMAP

MF_00802. GlnE.
[Tree]

InterPro

IPR023057. GlnE.
IPR005190. GlnE_rpt_dom.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]

KO

K00982.

Pfam

PF08335. GlnD_UR_UTase. 2 hits.
PF03710. GlnE. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLNE_ECOLI

Accession

Primary (citable) accession number: P30870
Secondary accession number(s): P78107, Q2M9F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program