Reviewed, UniProtKB/Swiss-Prot Q07907 (ARGD_BACST)

Names and origin

Protein names

Recommended name:
    Acetylornithine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11

Gene names

Name:

argD

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107
Cofactor	Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_01107
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107
Subunit structure	Homodimer By similarity. HAMAP MF_01107
Subcellular location	Cytoplasm Probable HAMAP MF_01107.
Miscellaneous	May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis. HAMAP MF_01107
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
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 – 385	385	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112720
Regions
	Region	207 – 210	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	122	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	125	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	264	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	265	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	236	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q07907-1 [UniParc]. Last modified April 23, 2003. Version 2. Checksum: A40E6AC2ED105604	FASTA	385	41,304
	10 20 30 40 50 60 MSALFPTYNR WNIAVQSAEG TVVTDVNGKQ YLDFVSGIAV CNLGHRHPHV QKSIEQQLNQ 70 80 90 100 110 120 YWHVSNLFTI PIQEEVASLL VAHSAGDYVF FCNSGAEANE AALKLARKHT GRHKVITFRQ 130 140 150 160 170 180 SFHGRTFATM AATGQEKVHS GFGPLLPEFI HLPLNDVDAL KQAMSEEVAA VMLEVVQGEG 190 200 210 220 230 240 GVRPVDPAFL QTASELCQQH GALLIIDEVQ TGIGRTGKPF AYQHFDVEPD IITAAKGLGS 250 260 270 280 290 300 GIPVGAMIGK AFLKESFGPG VHGSTFGGNP IAMAAAKATL EVVFDPAFLQ DVQEKGRYFL 310 320 330 340 350 360 ARLHDALASL DIVKDVRGLG LLVGIECQTD VAPLLPLIHE NGLLVLSAGP NVIRLLPLVV 370 380 TKAEIDEAVD ILTNVLNNAN ASAVL

References

[1]

"Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase." Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I., Pierard P., Glansdorff N. J. Gen. Microbiol. 139:393-402(1993) [PubMed: 8473852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-149. Strain: NCIB 8224 / CCM 2186.

[2]

"Cloning and characterization of the arginine-specific carbamoyl-phosphate synthetase from Bacillus stearothermophilus." Yang H., Park S.M., Nolan W.G., Lu C.-D., Abdelal A.T. Eur. J. Biochem. 249:443-449(1997) [PubMed: 9370352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-385. Strain: ATCC 12980 / DSM 22 / IFO 12550 / NCIB 8923 / NCTC 10339.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L06036 Genomic DNA. Translation: AAA22199.1. U43091 Genomic DNA. Translation: AAC78718.1.
PIR	I39768.
3D structure databases
SMR	Q07907. Positions 4-378.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.6.1.11. 266715.
Family and domain databases
HAMAP	MF_01107. ArgD_aminotrans_3. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase_major_dom. 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_BACST

Accession

Primary (citable) accession number: Q07907
Secondary accession number(s): Q9ZB64

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	April 23, 2003
Last modified:	February 9, 2010
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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