ID ARGD_KLULA Reviewed; 423 AA.
AC O14433; Q6CMD6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=Acetylornithine aminotransferase, mitochondrial;
DE Short=ACOAT;
DE EC=2.6.1.11;
DE Flags: Precursor;
GN Name=ARG8; OrderedLocusNames=KLLA0E21153g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CK56-7A;
RX PubMed=9544247;
RX DOI=10.1002/(sici)1097-0061(199802)14:3<281::aid-yea212>3.0.co;2-e;
RA Janssen A., Chen X.J.;
RT "Cloning, sequencing and disruption of the ARG8 gene encoding
RT acetylornithine aminotransferase in the petite-negative yeast Kluyveromyces
RT lactis.";
RL Yeast 14:281-285(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-
CC acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57805; EC=2.6.1.11;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 4/4.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; U93209; AAC49934.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99990.1; -; Genomic_DNA.
DR PIR; T50923; T50923.
DR RefSeq; XP_454903.1; XM_454903.1.
DR AlphaFoldDB; O14433; -.
DR SMR; O14433; -.
DR STRING; 284590.O14433; -.
DR PaxDb; 284590-O14433; -.
DR GeneID; 2894291; -.
DR KEGG; kla:KLLA0_E21077g; -.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_016922_10_1_1; -.
DR InParanoid; O14433; -.
DR OMA; MVPGFKY; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00707; argD; 1.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..423
FT /note="Acetylornithine aminotransferase, mitochondrial"
FT /id="PRO_0000002079"
FT MOD_RES 276
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 227
FT /note="T -> S (in Ref. 1; AAC49934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 46641 MW; AF0495431184440D CRC64;
MRVIRQLHTS KRLLQSLVDK QKYQATTYAR PNHLVLTRGK NAILYDDVNN KEYIDFTAGI
AVTALGHANP EVAEIMYKQS KKLIHSSNLY YNEECLKLSE NLVEATKSFG GQYDASRVFL
CNSGTEANEA ALKFAKRYGI LKSPSKQGII AFQNSFHGRT MGALSVTSNP KYREPFGSLI
PGVEFLNIND ELTKLDQQVS SLKEKTAGLI VEPIQGEGGV FPIPLDTLVG LKKICEDHDI
IVIYDEIQCG LGRSGKLWAH SYLPKEAHPD IFTTAKALGN GFPIAATVTN DKVNDILKVG
DHGTTYGGNP LGSAVGNYVV NVIAEQKFLD EVNKKGEIIT NRLRKLQERF PEHIKDIRGK
GLMIGCDFDE APAKIVDAAR DSGLLIITAG KTTVRFVPAL TIEDNLLEKG LNIFEKAVEK
VYS
//
