Q53940 (GNAT2_STRCL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate N-acetyltransferase 2
EC=2.3.1.35

Alternative name(s):
Ornithine acetyltransferase 2
Ornithine transacetylase 2
Short name=OATase 2

Cleaved into the following 2 chains:

1. Glutamate N-acetyltransferase 2 alpha chain
2. Glutamate N-acetyltransferase 2 beta chain

Gene names

Name:

oat2

Organism

Streptomyces clavuligerus

Taxonomic identifier

1901 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP MF_01106
Pathway	Antibiotic biosynthesis; clavulanate biosynthesis. HAMAP MF_01106
Subunit structure	Heterotetramer of two alpha and two beta chains.
Subcellular location	Cytoplasm By similarity HAMAP MF_01106.
Miscellaneous	The role of this protein is probably directed towards producing increased intracellular concentrations of arginine for clavam biosynthesis, rather than primary metabolism. HAMAP MF_01106
Sequence similarities	Belongs to the ArgJ family.
Mass spectrometry	Molecular mass is 18816.2 Da from positions 1 - 180. Determined by ESI. Ref.3 Molecular mass is 22811.7 Da from positions 181 - 393. Determined by ESI. Ref.3

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Autocatalytic cleavage
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: InterPro glutamate N-acetyltransferase 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 – 180

180

Glutamate N-acetyltransferase 2 alpha chain HAMAP MF_01106

PRO_0000002267

Chain

181 – 393

213

Glutamate N-acetyltransferase 2 beta chain HAMAP MF_01106

PRO_0000002268

Sites

Site

180 – 181

2

Cleavage; by autolysis

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

393

Helix Strand Turn

Details...

Beta strand

12 – 17

6

Beta strand

29 – 36

8

Beta strand

39 – 44

6

Helix

52 – 60

9

Turn

61 – 63

3

Beta strand

68 – 75

8

Helix

81 – 99

19

Helix

103 – 105

3

Beta strand

106 – 115

10

Helix

120 – 127

8

Beta strand

134 – 137

4

Helix

139 – 145

7

Beta strand

154 – 160

7

Beta strand

163 – 170

8

Beta strand

172 – 174

3

Beta strand

183 – 191

9

Helix

194 – 207

14

Helix

209 – 211

3

Beta strand

214 – 216

3

Beta strand

223 – 234

12

Helix

237 – 257

21

Beta strand

263 – 275

13

Helix

276 – 287

12

Helix

290 – 297

8

Helix

303 – 311

9

Turn

321 – 323

3

Beta strand

325 – 328

4

Beta strand

331 – 334

4

Helix

345 – 354

10

Beta strand

357 – 365

9

Beta strand

368 – 378

11

Helix

382 – 389

8

Sequences

	Sequence		Length	Mass (Da)
	Q53940 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 951ECEE6B9664E48	FASTA	393	41,608
	10 20 30 40 50 60 MSDSTPKTPR GFVVHTAPVG LADDGRDDFT VLASTAPATV SAVFTRSRFA GPSVVLCREA 70 80 90 100 110 120 VADGQARGVV VLARNANVAT GLEGEENARE VREAVARALG LPEGEMLIAS TGVIGRQYPM 130 140 150 160 170 180 ESIREHLKTL EWPAGEGGFD RAARAIMTTD TRPKEVRVSV GGATLVGIAK GVGMLEPDMA 190 200 210 220 230 240 TLLTFFATDA RLDPAEQDRL FRRVMDRTFN AVSIDTDTST SDTAVLFANG LAGEVDAGEF 250 260 270 280 290 300 EEALHTAALA LVKDIASDGE GAAKLIEVQV TGARDDAQAK RVGKTVVNSP LVKTAVHGCD 310 320 330 340 350 360 PNWGRVAMAI GKCSDDTDID QERVTIRFGE VEVYPPKARG DQADDALRAA VAEHLRGDEV 370 380 390 VIGIDLAIAD GAFTVYGCDL TEGYVRLNSE YTT

References

[1]	"Clavulanic acid biosynthesis in Streptomyces clavuligerus: gene cloning and characterization." Hodgson J.E., Fosberry A.P., Rawlinson N.S., Ross H.N.M., Neal R.J., Arnell J.C., Earl A.J., Lawlor E.J. Gene 166:49-55(1995) [PubMed: 8529893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Enzymes catalyzing the early steps of clavulanic acid biosynthesis are encoded by two sets of paralogous genes in Streptomyces clavuligerus." Jensen S.E., Elder K.J., Aidoo K.A., Paradkar A.S. Antimicrob. Agents Chemother. 44:720-726(2000) [PubMed: 10681345] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
[3]	"ORF6 from the clavulanic acid gene cluster of Streptomyces clavuligerus has ornithine acetyltransferase activity." Kershaw N.J., McNaughton H.J., Hewitson K.S., Hernandez H., Griffin J., Hughes C., Greaves P., Barton B., Robinson C.V., Schofield C.J. Eur. J. Biochem. 269:2052-2059(2002) [PubMed: 11985581] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10 AND 181-190, MASS SPECTROMETRY, CHARACTERIZATION.
[4]	"Two sets of paralogous genes encode the enzymes involved in the early stages of clavulanic acid and clavam metabolite biosynthesis in Streptomyces clavuligerus." Tahlan K., Park H.-U., Wong A., Beatty P.H., Jensen S.E. Antimicrob. Agents Chemother. 48:930-939(2004) [PubMed: 14982786] [Abstract] Cited for: PRESENCE OF PARALOGS. Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
[5]	Elkins J.M., Kershaw N.J., Schofield C.J. Submitted (MAY-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X84101 Genomic DNA. Translation: CAA58906.1.
U87786 Genomic DNA. Translation: AAF86622.1.

PIR

S57671.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VZ6	X-ray	2.75	A/B	1-393	[»]
1VZ7	X-ray	3.00	A/B/C/D	1-393	[»]
1VZ8	X-ray	2.75	A/B/C/D	1-393	[»]
2V4I	X-ray	2.20	A/C/E/G	8-180	[»]
			B/D/F/H	182-393	[»]
2VZK	X-ray	2.33	A/C/E/G	8-180	[»]
			B/D/F/H	181-393	[»]
2YEP	X-ray	2.70	A/C/E/G	1-180	[»]
			B/D/F/H	181-393	[»]

ProteinModelPortal

Q53940.

SMR

Q53940. Positions 8-393.

ModBase

Search...

Protein family/group databases

MEROPS

T05.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

PATRIC

29741633. VBIStrCla15562_0199.

Family and domain databases

HAMAP

MF_01106. ArgJ.
[Tree]

InterPro

IPR002813. Arg_biosynth_ArgJ.
IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ.
[Graphical view]

PANTHER

PTHR23100. ArgJ. 1 hit.

Pfam

PF01960. ArgJ. 1 hit.
[Graphical view]

ProDom

PD004193. Arg_biosynth_ArgJ. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.

TIGRFAMs

TIGR00120. ArgJ. 1 hit.

ProtoNet

Search...

Entry information

Entry name

GNAT2_STRCL

Accession

Primary (citable) accession number: Q53940

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program