Reviewed, UniProtKB/Swiss-Prot Q8CUM9 (ARGD_OCEIH)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	OB1078

Organism

Oceanobacillus iheyensis [Complete proteome] [HAMAP]

Taxonomic identifier

182710 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Oceanobacillus

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Subcellular location	Cytoplasm Probable.
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: 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 – 399	399	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112762
Regions
	Region	220 – 223	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	135	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	138	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	277	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	278	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	249	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8CUM9-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 38B1EB28F39193F2	FASTA	399	43,410
	10 20 30 40 50 60 MSSTTKVSSA VMQTYNRFPI TATKGKGSFL WDDNGEKYLD YTSGIATCNL GHVPDNVQHA 70 80 90 100 110 120 ISNQLKDLWH CSNLYHIPSQ EKLAALLTEY SCLDQVFFCN SGAEANEAAI KIAKKYAKDK 130 140 150 160 170 180 GYDDRTEIIT FEQSFHGRTG STMAATAQEK IHQGFTPLTE GFRYLPFNNK ESLSEIDNGK 190 200 210 220 230 240 TSAVLLEVIQ GEGGIHTAEK DWLKQLAAIC KQADILLMID EIQTGIGRTG SLFAYQPYGI 250 260 270 280 290 300 EPDVITVAKG LGSGFPIGAM LAKQHIAASF SPGTHGSTFG GNPVAAAAGI ATLKEILSDG 310 320 330 340 350 360 FLENCKEGQE ELFNQLKSIK EISPLIKDIR GKGYLMGIEV MNQASAWIEK LREKQILVLP 370 380 390 AGEKVVRILP PLTTTKEELQ ICIQALKEVA LELGGNTNG

References

[1]

"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments." Takami H., Takaki Y., Uchiyama I. Nucleic Acids Res. 30:3927-3935(2002) [PubMed: 12235376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000028 Genomic DNA. Translation: BAC13034.1.
RefSeq	NP_691999.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1016977.
GenomeReviews	Gene locus OB1078 in contig BA000028_GR.
KEGG	oih:OB1078.
NMPDR	fig|221109.1.peg.1079.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8CUM9.
OMA	LENTAEP.
Enzyme and pathway databases
BioCyc	OIHE221109:OB1078-MON.
BRENDA	2.6.1.11. 278212.
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_OCEIH

Accession

Primary (citable) accession number: Q8CUM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 50 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)