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Protein

Acetylornithine aminotransferase, mitochondrial

Gene

ARG8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.

Cofactori

Pathwayi: L-arginine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Amino-acid acetyltransferase, mitochondrial (ARG2), Arginine biosynthesis bifunctional protein ArgJ, mitochondrial (ARG7)
  2. Protein ARG5,6, mitochondrial (ARG5,6)
  3. Protein ARG5,6, mitochondrial (ARG5,6)
  4. Acetylornithine aminotransferase, mitochondrial (ARG8)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • arginine biosynthetic process Source: SGD
  • ornithine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciYEAST:YOL140W-MONOMER.
ReactomeiR-SCE-1442490. Collagen degradation.
R-SCE-1483213. Synthesis of PE.
R-SCE-389661. Glyoxylate metabolism and glycine degradation.
R-SCE-71064. Lysine catabolism.
UniPathwayiUPA00068; UER00109.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylornithine aminotransferase, mitochondrial (EC:2.6.1.11)
Short name:
ACOAT
Gene namesi
Name:ARG8
Ordered Locus Names:YOL140W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL140W.
SGDiS000005500. ARG8.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 423Acetylornithine aminotransferase, mitochondrialPRO_0000002083
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei276 – 2761N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiP18544.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi34277. 9 interactions.
DIPiDIP-2623N.
IntActiP18544. 1 interaction.
MINTiMINT-424582.

Structurei

3D structure databases

ProteinModelPortaliP18544.
SMRiP18544. Positions 23-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000062907.
HOGENOMiHOG000020206.
InParanoidiP18544.
KOiK00818.
OMAiTGKMWGY.
OrthoDBiEOG7TJ3TD.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01107. ArgD_aminotrans_3.
InterProiIPR004636. AcOrn/SuccOrn_fam.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00707. argD. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18544-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKRYLSSTS SRRFTSILEE KAFQVTTYSR PEDLCITRGK NAKLYDDVNG
60 70 80 90 100
KEYIDFTAGI AVTALGHANP KVAEILHHQA NKLVHSSNLY FTKECLDLSE
110 120 130 140 150
KIVEKTKQFG GQHDASRVFL CNSGTEANEA ALKFAKKHGI MKNPSKQGIV
160 170 180 190 200
AFENSFHGRT MGALSVTWNS KYRTPFGDLV PHVSFLNLND EMTKLQSYIE
210 220 230 240 250
TKKDEIAGLI VEPIQGEGGV FPVEVEKLTG LKKICQDNDV IVIHDEIQCG
260 270 280 290 300
LGRSGKLWAH AYLPSEAHPD IFTSAKALGN GFPIAATIVN EKVNNALRVG
310 320 330 340 350
DHGTTYGGNP LACSVSNYVL DTIADEAFLK QVSKKSDILQ KRLREIQAKY
360 370 380 390 400
PNQIKTIRGK GLMLGAEFVE PPTEVIKKAR ELGLLIITAG KSTVRFVPAL
410 420
TIEDELIEEG MDAFEKAIEA VYA
Length:423
Mass (Da):46,681
Last modified:November 1, 1990 - v1
Checksum:i0F468560865629DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32795 Genomic DNA. Translation: AAA34436.1.
X84036 Genomic DNA. Translation: CAA58853.1.
Z74882 Genomic DNA. Translation: CAA99161.1.
BK006948 Genomic DNA. Translation: DAA10645.1.
PIRiS61868.
RefSeqiNP_014501.1. NM_001183394.1.

Genome annotation databases

EnsemblFungiiYOL140W; YOL140W; YOL140W.
GeneIDi854025.
KEGGisce:YOL140W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32795 Genomic DNA. Translation: AAA34436.1.
X84036 Genomic DNA. Translation: CAA58853.1.
Z74882 Genomic DNA. Translation: CAA99161.1.
BK006948 Genomic DNA. Translation: DAA10645.1.
PIRiS61868.
RefSeqiNP_014501.1. NM_001183394.1.

3D structure databases

ProteinModelPortaliP18544.
SMRiP18544. Positions 23-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34277. 9 interactions.
DIPiDIP-2623N.
IntActiP18544. 1 interaction.
MINTiMINT-424582.

Proteomic databases

MaxQBiP18544.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL140W; YOL140W; YOL140W.
GeneIDi854025.
KEGGisce:YOL140W.

Organism-specific databases

EuPathDBiFungiDB:YOL140W.
SGDiS000005500. ARG8.

Phylogenomic databases

GeneTreeiENSGT00530000062907.
HOGENOMiHOG000020206.
InParanoidiP18544.
KOiK00818.
OMAiTGKMWGY.
OrthoDBiEOG7TJ3TD.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00109.
BioCyciYEAST:YOL140W-MONOMER.
ReactomeiR-SCE-1442490. Collagen degradation.
R-SCE-1483213. Synthesis of PE.
R-SCE-389661. Glyoxylate metabolism and glycine degradation.
R-SCE-71064. Lysine catabolism.

Miscellaneous databases

PROiP18544.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01107. ArgD_aminotrans_3.
InterProiIPR004636. AcOrn/SuccOrn_fam.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00707. argD. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARGD_YEAST
AccessioniPrimary (citable) accession number: P18544
Secondary accession number(s): D6W1S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 6, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.