P18544 (ARGD_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	ARG8
Ordered Locus Names:	YOL140W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular location	Mitochondrion matrix.
Miscellaneous	The reaction catalyzed by ACOAT is highly reversible. Moreover this enzyme may transaminate ornithine. Present with 2300 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Traceable author statement. Source: SGD ornithine biosynthetic process Traceable author statement. Source: SGD
Cellular component	mitochondrial matrix Inferred from direct assay. Source: SGD
Molecular function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity Inferred from direct assay Ref.1. Source: SGD 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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 423		Acetylornithine aminotransferase, mitochondrial		PRO_0000002083
Amino acid modifications
	Modified residue	276	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P18544 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 0F468560865629DC	FASTA	423	46,681
	10 20 30 40 50 60 MFKRYLSSTS SRRFTSILEE KAFQVTTYSR PEDLCITRGK NAKLYDDVNG KEYIDFTAGI 70 80 90 100 110 120 AVTALGHANP KVAEILHHQA NKLVHSSNLY FTKECLDLSE KIVEKTKQFG GQHDASRVFL 130 140 150 160 170 180 CNSGTEANEA ALKFAKKHGI MKNPSKQGIV AFENSFHGRT MGALSVTWNS KYRTPFGDLV 190 200 210 220 230 240 PHVSFLNLND EMTKLQSYIE TKKDEIAGLI VEPIQGEGGV FPVEVEKLTG LKKICQDNDV 250 260 270 280 290 300 IVIHDEIQCG LGRSGKLWAH AYLPSEAHPD IFTSAKALGN GFPIAATIVN EKVNNALRVG 310 320 330 340 350 360 DHGTTYGGNP LACSVSNYVL DTIADEAFLK QVSKKSDILQ KRLREIQAKY PNQIKTIRGK 370 380 390 400 410 420 GLMLGAEFVE PPTEVIKKAR ELGLLIITAG KSTVRFVPAL TIEDELIEEG MDAFEKAIEA VYA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli and Saccharomyces cerevisiae acetylornithine aminotransferase: evolutionary relationship with ornithine aminotransferase." Heimberg H., Boyen A., Crabeel M., Glansdorff N. Gene 90:69-78(1990) [PubMed: 2199330] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of a 9873 bp fragment of the left arm of yeast chromosome XV that contains the ARG8 and CDC33 genes, a putative riboflavin synthase beta chain gene, and four new open reading frames." Casas C., Aldea M., Casamayor A., Lafuente M.J., Gamo F.J., Gancedo C., Arino J., Herrero E. Yeast 11:1061-1067(1995) [PubMed: 7502581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M32795 Genomic DNA. Translation: AAA34436.1. X84036 Genomic DNA. Translation: CAA58853.1. Z74882 Genomic DNA. Translation: CAA99161.1. BK006948 Genomic DNA. Translation: DAA10645.1.
PIR	S61868.
RefSeq	NP_014501.1. NM_001183394.1.
3D structure databases
ProteinModelPortal	P18544.
SMR	P18544. Positions 20-421.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2623N.
MINT	MINT-424582.
STRING	P18544.
Proteomic databases
PeptideAtlas	P18544.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOL140W; YOL140W; YOL140W.
GeneID	854025.
KEGG	sce:YOL140W.
NMPDR	fig|4932.3.peg.5587.
Organism-specific databases
CYGD	YOL140w.
SGD	S000005500. ARG8.
Phylogenomic databases
eggNOG	fuNOG06187.
GeneTree	EFGT00050000003450.
HOGENOM	HBG725944.
OMA	GTYNDIA.
OrthoDB	EOG4HMNJM.
Gene expression databases
ArrayExpress	P18544.
Genevestigator	P18544.
GermOnline	YOL140W. Saccharomyces cerevisiae.
Family and domain databases
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...
Other
NextBio	975565.

Entry information

Entry name

ARGD_YEAST

Accession

Primary (citable) accession number: P18544
Secondary accession number(s): D6W1S9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	December 14, 2011
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program