Q818W2 (ARGD_BACCR) 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:	BC_4127

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31)

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	386 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.
Sequence caution	The sequence AAP11045.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference 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 – 386	386	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112717
Regions
	Region	208 – 211	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	123	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	126	1	N2-acetyl-L-ornithine By similarity
	Binding site	265	1	N2-acetyl-L-ornithine By similarity
	Binding site	266	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	237	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q818W2 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 04CD91BB091FD627	FASTA	386	42,060
	10 20 30 40 50 60 MTSHLFQTYG RRTIEFVKGT GTKVIDNKGK EYLDFTSGIG VCNLGHCHPT VLKGVQEQLD 70 80 90 100 110 120 DIWHISNLFT NSLQEEVASL LTENRALDYV FFCNSGAEAN EAALKLARKH TGKSLVVTCQ 130 140 150 160 170 180 QSFHGRTFGT MSATGQDKVK EGFGPLLPSF LHIPFNDIKA LEEVMNEEVA AVMVEVVQGE 190 200 210 220 230 240 GGVIPVDLSF LKEIETLCNK FGSLFIIDEV QTGIGRTGTL FAYEQVGIEP DIVTVAKALG 250 260 270 280 290 300 NGIPVGAMIG GKELGTSFTA GSHGSTFGGN YIAMAAAKEV LQVSKKPSFL KEVQEKGEYV 310 320 330 340 350 360 LEKLQEELQH VECIQNIRGK GLMIGIECKH EVASFIEQLE NEGLLVLQAG PNVIRLLPPL 370 380 IVTNEELEQA VYIIKKVVCT KNVSII

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP11045.1. Different initiation.
RefSeq	NP_833844.2. NC_004722.1.
3D structure databases
ProteinModelPortal	Q818W2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q818W2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000034107; EBBACP00000033313; EBBACG00000034098.
GeneID	1206472.
GenomeReviews	Gene locus BC_4127 in contig AE016877_GR.
KEGG	bce:BC4127.
PATRIC	32604324. VBIBacCer54481_4265.
Phylogenomic databases
eggNOG	COG4992.
GeneTree	EBGT00070000031861.
HOGENOM	HBG725944.
OMA	MTSHLFQ.
ProtClustDB	PRK02936.
Enzyme and pathway databases
BioCyc	BCER226900:BC_4127-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_BACCR

Accession

Primary (citable) accession number: Q818W2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 5, 2009
Last modified:	January 25, 2012
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program