Reviewed, UniProtKB/Swiss-Prot Q5SHH5 (ARGD_THET8)

Names and origin

Protein names

Recommended name:
    Acetylornithine/acetyl-lysine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11
    EC=2.6.1.-

Gene names

Name:	argD
Synonyms:	lysJ
Ordered Locus Names:	TTHA1755

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in both the arginine and lysine biosynthetic pathways By similarity.
Catalytic activity	N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107 N(2)-acetyl-L-lysine + 2-oxoglutarate = N-acetyl-L-aminoadipate semialdehyde + L-glutamate. HAMAP MF_01107
Cofactor	Binds 1 pyridoxal phosphate per subunit. HAMAP MF_01107
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107 Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5. HAMAP MF_01107
Subunit structure	Homodimer Probable.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 395

395

Acetylornithine/acetyl-lysine aminotransferase HAMAP MF_01107

PRO_0000311262

Regions

Region

113 – 114

2

Pyridoxal phosphate binding HAMAP MF_01107

Region

225 – 228

4

Pyridoxal phosphate binding HAMAP MF_01107

Sites

Binding site

140

1

Pyridoxal phosphate; via carbonyl oxygen By similarity

Binding site

143

1

N(2)-acetyl-L-ornithine HAMAP MF_01107

Binding site

282

1

N(2)-acetyl-L-ornithine HAMAP MF_01107

Binding site

283

1

Pyridoxal phosphate HAMAP MF_01107

Amino acid modifications

Modified residue

254

1

N6-(pyridoxal phosphate)lysine HAMAP MF_01107

Secondary structure

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395

Helix Strand Turn

Details...

Helix

10 – 19

10

Beta strand

31 – 36

6

Beta strand

38 – 41

4

Beta strand

46 – 51

6

Helix

52 – 55

4

Helix

64 – 76

13

Helix

87 – 98

12

Beta strand

104 – 112

9

Helix

113 – 128

16

Beta strand

132 – 136

5

Helix

145 – 149

5

Helix

154 – 157

4

Helix

158 – 160

3

Beta strand

167 – 170

4

Helix

175 – 181

7

Beta strand

186 – 191

6

Beta strand

193 – 195

3

Turn

196 – 199

4

Beta strand

200 – 202

3

Helix

205 – 218

14

Beta strand

221 – 225

5

Turn

227 – 234

8

Beta strand

235 – 238

4

Helix

240 – 243

4

Beta strand

248 – 252

5

Helix

254 – 257

4

Beta strand

263 – 268

6

Helix

269 – 273

5

Helix

288 – 304

17

Helix

307 – 322

16

Beta strand

329 – 335

7

Beta strand

338 – 345

8

Helix

348 – 358

11

Beta strand

363 – 366

4

Beta strand

369 – 372

4

Helix

380 – 394

15

Sequences

	Sequence		Length	Mass (Da)
	Q5SHH5-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 1D3B73EAC3454C3A	FASTA	395	43,423
	10 20 30 40 50 60 METRTLEDWR ALLEAEKTLD SGVYNKHDLL IVRGQGARVW DAEGNEYIDC VGGYGVANLG 70 80 90 100 110 120 HGNPEVVEAV KRQAETLMAM PQTLPTPMRG EFYRTLTAIL PPELNRVFPV NSGTEANEAA 130 140 150 160 170 180 LKFARAHTGR KKFVAAMRGF SGRTMGSLSV TWEPKYREPF LPLVEPVEFI PYNDVEALKR 190 200 210 220 230 240 AVDEETAAVI LEPVQGEGGV RPATPEFLRA AREITQEKGA LLILDEIQTG MGRTGKRFAF 250 260 270 280 290 300 EHFGIVPDIL TLAKALGGGV PLGAAVMREE VARSMPKGGH GTTFGGNPLA MAAGVAAIRY 310 320 330 340 350 360 LERTRLWERA AELGPWFMEK LRAIPSPKIR EVRGMGLMVG LELKEKAAPY IARLEKEHRV 370 380 390 LALQAGPTVI RFLPPLVIEK EDLERVVEAV RAVLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Three-dimensional structure of acetylornithine aminotransferase from Thermus thermophilus HB8." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEXES WITH ANALOGS SUBSTRATE AND PLP.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AP008226 Genomic DNA. Translation: BAD71578.1.

RefSeq

YP_145021.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VEF	X-ray	1.35	A/B	1-395	[»]
1WKG	X-ray	2.25	A/B	1-395	[»]
1WKH	X-ray	2.25	A/B	1-395	[»]

SMR

Q5SHH5. Positions 9-395.

ModBase

Search...

Protein-protein interaction databases

STRING

Q5SHH5.

Genome annotation databases

GeneID

3169449.

GenomeReviews

Gene locus TTHA1755 in contig AP008226_GR.

KEGG

ttj:TTHA1755.

NMPDR

fig|300852.3.peg.1027.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q5SHH5.

OMA

WEPKYRE.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA1755-MON.

Family and domain databases

HAMAP

MF_01107.
[Tree]

InterPro

IPR004636. AcOrn/succinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

PANTHER

PTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF19. ArgD_aminotrans. 1 hit.

Pfam

PF00202. Aminotran_3. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00707. argD. 1 hit.

PROSITE

PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ARGD_THET8

Accession

Primary (citable) accession number: Q5SHH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	December 21, 2004
Last modified:	November 3, 2009
This is version 32 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)