Reviewed, UniProtKB/Swiss-Prot P36839 (ARGD_BACSU)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	BSU11220

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	385 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 – 385	385	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112721
Regions
	Region	208 – 211	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	265	1	N(2)-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
Experimental info
	Sequence conflict	82	1	A → G in CAA81546. Ref.1
	Sequence conflict	96 – 97	2	AE → GQ in CAA81546. Ref.1
	Sequence conflict	103	1	I → Y in CAA81546. Ref.1
	Sequence conflict	351 – 357	7	NVIRLLP → ERDSAAA in CAA81546. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P36839-1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: C3EAD1AC28F1771C	FASTA	385	40,978
	10 20 30 40 50 60 MSSLFQTYGR WDIDIKKAKG TYVEDQNGKT YLDFIQGIAV SNLGHCHEAV TEAVKKQLDS 70 80 90 100 110 120 VWHVSNLFQN SLQEQAAQKL AAHSAGDLVF FCNSGAEANE GAIKLARKAT GKTKIITFLQ 130 140 150 160 170 180 SFHGRTYAGM AATGQDKIKT GFGPMLGGFH YLPYNDPSAF KALGEEGDIA AVMLETVQGE 190 200 210 220 230 240 GGVNPASAEF LSAVQSFCKE KQALLIIDEI QTGIGRTGKG FAYEHFGLSP DIITVAKGLG 250 260 270 280 290 300 NGFPVGAVIG KKQLGEAFTP GSHGTTFGGN MLAMAAVNAT LQIVFQPDFL QEAADKGAFL 310 320 330 340 350 360 KEQLEAELKS PFVKQIRGKG LMLGIECDGP VADIIAELQT LGLLVLPAGP NVIRLLPPLT 370 380 VTKDEIAEAV SKLKQAIAHH SAVNQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of the citrulline biosynthetic operon argC-F from Bacillus subtilis." O'Reilly M., Devine K.M. Microbiology 140:1023-1025(1994) [PubMed: 8025667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 82; 96-97; 103 AND 351-357.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z26919 Genomic DNA. Translation: CAA81546.1. AL009126 Genomic DNA. Translation: CAB12963.2.
PIR	I40375.
RefSeq	NP_389004.2.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	939357.
GenomeReviews	Gene locus BSU11220 in contig AL009126_GR.
KEGG	bsu:BSU11220.
NMPDR	fig|224308.1.peg.1123.
Organism-specific databases
SubtiList	BG10194. argD. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P36839.
OMA	FHYLPYN.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1123-MON.
BRENDA	2.6.1.11. 150.
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_BACSU

Accession

Primary (citable) accession number: P36839

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 16, 2009
Last modified:	November 3, 2009
This is version 80 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)