Q9K8V5 (ARGD_BACHD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	BH2897

Organism

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]

Taxonomic identifier

272558 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	384 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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine 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: EC 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 – 384	384	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112719
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	N2-acetyl-L-ornithine By similarity
	Binding site	264	1	N2-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)
	Q9K8V5 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 0667027A4575FAE0	FASTA	384	41,198
	10 20 30 40 50 60 MSHLFPTYAK WDVTITSGKG TKLYDNQGNE YLDFVSGIAV CNLGHCHPKV VAAVEEQLHS 70 80 90 100 110 120 FWHVSNLFHI PIQENVAALL TEQSGMDAVF FCNSGAEANE AAIKLARKAT GKHEIVTFTQ 130 140 150 160 170 180 SFHGRTLGTM SATGQDKIKT GFGPMLETFH HVPFNDIAAL KQVVNEQTAA IVLEVIQGEG 190 200 210 220 230 240 GVNLIDPEFA ASVNHVCQEH GILLIIDEIQ TGIGRTGTAF AFQQYELTPD IITVAKGLGN 250 260 270 280 290 300 GFPVGAMLGK QHLIDAFSAG SHGSTFGGNP LAMAAAQAVL TEVFQPNFLQ AVQEKGKQLL 310 320 330 340 350 360 SGLNEALSGL EIVKEIRGNG LLVGIELQEE GAPFIKQLRE KGLLVLNAGP NVIRLLPPLV 370 380 VTSEELHEAV TQLKEVLDQA SVHA

References

[1]

"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000004 Genomic DNA. Translation: BAB06616.1.
PIR	A84012.
RefSeq	NP_243763.1. NC_002570.2.
3D structure databases
ProteinModelPortal	Q9K8V5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000051699; EBBACP00000050338; EBBACG00000051690.
GeneID	893097.
GenomeReviews	Gene locus BH2897 in contig BA000004_GR.
KEGG	bha:BH2897.
NMPDR	fig|272558.1.peg.2897.
PATRIC	18943026. VBIBacHal18977_3014.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00070000031861.
HOGENOM	HBG725944.
OMA	MTSHLFQ.
PhylomeDB	Q9K8V5.
ProtClustDB	PRK02936.
Enzyme and pathway databases
BioCyc	BHAL272558:BH2897-MONOMER.
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. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K00818.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00707. ArgD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_BACHD

Accession

Primary (citable) accession number: Q9K8V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program