Reviewed, UniProtKB/Swiss-Prot Q6FXA4 (ARGD_CANGA)

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:	CAGL0B01507g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Subcellular location	Mitochondrion matrix By similarity.
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
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix 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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 427		Acetylornithine aminotransferase, mitochondrial		PRO_0000002077
Amino acid modifications
	Modified residue	279	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FXA4-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: BF964B26B2221362	FASTA	427	46,824
	10 20 30 40 50 60 MYKRYFSTSL KTNQQALKKI LEEKTYQVTT YARPSDLCIT RGLNAKLFDD FNNKEYIDFT 70 80 90 100 110 120 AGIAVTALGH ANPKVAEILQ TQATKLVHSS NLYFTKECLD LSEKLIEKTK KFGGQHDASK 130 140 150 160 170 180 VFLCNSGTEA NEAALKFAKK HGITKNPKKQ GIIAFENSFH GRTMGALSVT WNKKYRTPFG 190 200 210 220 230 240 DLVPHVSFLN INDELSKIKD FINTKKDEIA GLIIEPIQGE GGIFPIPIEK LVALKEICQK 250 260 270 280 290 300 NDIIVIYDEI QCGLGRTGNL WAHAALPKAA HPDIFTSAKA LGNGFPIAAT VVNEKVNNAL 310 320 330 340 350 360 QVGDHGTTYG GNPLGCAVSN YVLDVIGDQA FLDSVTKKGE LLKKGLLKIK EQHPDKISDV 370 380 390 400 410 420 RGSGLIWGVE FKDAPGAIVQ KARELGLLVI TAGKTTVRFV PSLTIEDEVV EEGLTIFNKA VNDVFSK

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380948 Genomic DNA. Translation: CAG57935.1.
RefSeq	XP_445035.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FXA4.
Genome annotation databases
GeneID	2886668.
GenomeReviews	Gene locus CAGL0B01507g in contig CR380948_GR.
KEGG	cgr:CAGL0B01507g.
Phylogenomic databases
HOGENOM	Q6FXA4.
OMA	HANPKVA.
Enzyme and pathway databases
BRENDA	2.6.1.11. 189220.
Family and domain databases
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_CANGA

Accession

Primary (citable) accession number: Q6FXA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)