Reviewed, UniProtKB/Swiss-Prot P40732 (ARGD_SALTY)

Names and origin

Protein names

Recommended name:
    Acetylornithine/succinyldiaminopimelate aminotransferase
      Short name=ACOAT
      Short name=Succinyldiaminopimelate transferase
      Short name=DapATase
    EC=2.6.1.11
    EC=2.6.1.17

Gene names

Name:	argD
Synonyms:	dapC, dtu
Ordered Locus Names:	STM3468

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	405 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)

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-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate. HAMAP MF_01107
Cofactor	Binds 1 pyridoxal phosphate per subunit. Ref.3
Enzyme regulation	Inhibited by gabaculine (Gcn). Ref.3
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 DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 2/3. HAMAP MF_01107
Subunit structure	Homodimer. Ref.3
Subcellular location	Cytoplasm Probable.
Miscellaneous	The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine. HAMAP MF_01107
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
Biophysicochemical properties	Kinetic parameters: KM=37 µM for N-acetylornithine (at pH 9.5 and 25 degrees Celsius) HAMAP MF_01107 KM=640 µM for ornithine (at pH 9.5 and 25 degrees Celsius) pH dependence: Optimum pH is 9.5. At pH 8.0, the activity is reduced by 50%.

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 succinyldiaminopimelate transaminase 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

Initiator methionine

1

1

Removed By similarity

Chain

2 – 405

404

Acetylornithine/succinyldiaminopimelate aminotransferase HAMAP MF_01107

PRO_0000112777

Regions

Region

108 – 109

2

Pyridoxal phosphate binding HAMAP MF_01107

Region

226 – 229

4

Pyridoxal phosphate binding HAMAP MF_01107

Sites

Binding site

141

1

Pyridoxal phosphate; via carbonyl oxygen HAMAP MF_01107

Binding site

144

1

N(2)-acetyl-L-ornithine By similarity

Binding site

283

1

N(2)-acetyl-L-ornithine By similarity

Binding site

284

1

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

255

1

N6-(pyridoxal phosphate)lysine HAMAP MF_01107

Experimental info

Sequence conflict

3

1

T → I in AAA24265. Ref.2

Sequence conflict

3

1

T → I in AAA27178. Ref.2

Secondary structure

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405

Helix Strand Turn

Details...

Helix

13 – 16

4

Beta strand

28 – 33

6

Beta strand

35 – 38

4

Beta strand

43 – 48

6

Helix

49 – 52

4

Helix

61 – 71

11

Helix

84 – 96

13

Beta strand

100 – 107

8

Helix

108 – 126

19

Beta strand

133 – 137

5

Helix

146 – 151

6

Helix

155 – 158

4

Beta strand

161 – 163

3

Beta strand

168 – 171

4

Helix

176 – 182

7

Beta strand

187 – 192

6

Beta strand

194 – 196

3

Turn

197 – 200

4

Beta strand

201 – 203

3

Helix

206 – 219

14

Beta strand

222 – 226

5

Turn

228 – 235

8

Beta strand

236 – 239

4

Helix

240 – 244

5

Beta strand

249 – 253

5

Helix

255 – 258

4

Beta strand

264 – 268

5

Helix

270 – 273

4

Helix

289 – 302

14

Helix

305 – 329

25

Beta strand

332 – 338

7

Beta strand

341 – 346

6

Helix

348 – 350

3

Helix

354 – 363

10

Beta strand

369 – 372

4

Beta strand

375 – 378

4

Helix

386 – 404

19

Sequences

	Sequence		Length	Mass (Da)
	P40732-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 26A69C62831E986C	FASTA	405	43,670
	10 20 30 40 50 60 MATEQTAITR ATFDEVILPV YAPADFIPVK GKGSRVWDQQ GKEYIDFAGG IAVTALGHCH 70 80 90 100 110 120 PALVEALKSQ GETLWHTSNV FTNEPALRLG RKLIDATFAE RVLFMNSGTE ANETAFKLAR 130 140 150 160 170 180 HYACVRHSPF KTKIIAFHNA FHGRSLFTVS VGGQPKYSDG FGPKPADIIH VPFNDLHAVK 190 200 210 220 230 240 AVMDDHTCAV VVEPIQGEGG VQAATPEFLK GLRDLCDEHQ ALLVFDEVQC GMGRTGDLFA 250 260 270 280 290 300 YMHYGVTPDI LTSAKALGGG FPVSAMLTTQ EIASAFHVGS HGSTYGGNPL ACAVAGAAFD 310 320 330 340 350 360 IINTPEVLQG IHTKRQQFVQ HLQAIDEQFD IFSDIRGMGL LIGAELKPKY KGRARDFLYA 370 380 390 400 GAEAGVMVLN AGADVMRFAP SLVVEEADIH EGMQRFAQAV GKVVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"Chromosomal organization and expression of Escherichia coli pabA." Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P. J. Bacteriol. 172:397-410(1990) [PubMed: 2403545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
[3]	"Structure of biosynthetic N-acetylornithine aminotransferase from Salmonella typhimurium: studies on substrate specificity and inhibitor binding." Rajaram V., Ratna Prasuna P., Savithri H.S., Murthy M.R. Proteins 70:429-441(2008) [PubMed: 17680699] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEXES WITH PLP, COFACTOR, SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE006468 Genomic DNA. Translation: AAL22330.1.
M32354 Genomic DNA. Translation: AAA24265.1.
M32355 Genomic DNA. Translation: AAA27178.1.

RefSeq

NP_462371.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PB0	X-ray	1.96	A/B	1-405	[»]
2PB2	X-ray	1.91	A/B	1-405	[»]

ModBase

Search...

Proteomic databases

PRIDE

P40732.

Genome annotation databases

GeneID

1254991.

GenomeReviews

Gene locus STM3468 in contig AE006468_GR.

KEGG

stm:STM3468.

NMPDR

fig|99287.1.peg.3348.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P40732.

OMA

EHNALLV.

Enzyme and pathway databases

BioCyc

STYP99287:STM3468-MON.

BRENDA

2.6.1.11. 2.
2.6.1.17. 2.

Family and domain databases

HAMAP

MF_01107.
[Tree]

InterPro

IPR004636. AcOrn/succinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR017652. SuccinylOrn_transaminase.
[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

TIGR03246. arg_catab_astC. 1 hit.
TIGR00707. argD. 1 hit.

PROSITE

PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ARGD_SALTY

Accession

Primary (citable) accession number: P40732

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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