ARGD_YEAST
ID ARGD_YEAST Reviewed; 423 AA.
AC P18544; D6W1S9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Acetylornithine aminotransferase, mitochondrial;
DE Short=ACOAT;
DE EC=2.6.1.11 {ECO:0000269|PubMed:2199330};
DE Flags: Precursor;
GN Name=ARG8; OrderedLocusNames=YOL140W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2199330; DOI=10.1016/0378-1119(90)90440-3;
RA Heimberg H., Boyen A., Crabeel M., Glansdorff N.;
RT "Escherichia coli and Saccharomyces cerevisiae acetylornithine
RT aminotransferase: evolutionary relationship with ornithine
RT aminotransferase.";
RL Gene 90:69-78(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7502581; DOI=10.1002/yea.320111107;
RA Casas C., Aldea M., Casamayor A., Lafuente M.J., Gamo F.J., Gancedo C.,
RA Arino J., Herrero E.;
RT "Sequence analysis of a 9873 bp fragment of the left arm of yeast
RT chromosome XV that contains the ARG8 and CDC33 genes, a putative riboflavin
RT synthase beta chain gene, and four new open reading frames.";
RL Yeast 11:1061-1067(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=205532; DOI=10.1128/jb.133.3.1096-1107.1978;
RA Jauniaux J.-C., Urrestarazu L.A., Wiame J.-M.;
RT "Arginine metabolism in Saccharomyces cerevisiae: subcellular localization
RT of the enzymes.";
RL J. Bacteriol. 133:1096-1107(1978).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: catalyzes the conversion of N-acetylglutamate-gamma-
CC semialdehyde (NAGSA) to N-acetylornithine in arginine biosynthesis.
CC {ECO:0000269|PubMed:2199330}.
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 Evidence={ECO:0000269|PubMed:2199330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18051;
CC Evidence={ECO:0000305|PubMed:2199330};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for acetylornithine {ECO:0000269|PubMed:2199330};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 4/4. {ECO:0000305|PubMed:2199330}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:205532}.
CC -!- MISCELLANEOUS: The reaction catalyzed by ACOAT is highly reversible.
CC Moreover this enzyme may transaminate ornithine, although this activity
CC should be of little importance at physiological pH.
CC {ECO:0000305|PubMed:2199330}.
CC -!- MISCELLANEOUS: Present with 2300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M32795; AAA34436.1; -; Genomic_DNA.
DR EMBL; X84036; CAA58853.1; -; Genomic_DNA.
DR EMBL; Z74882; CAA99161.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10645.1; -; Genomic_DNA.
DR PIR; S61868; S61868.
DR RefSeq; NP_014501.1; NM_001183394.1.
DR AlphaFoldDB; P18544; -.
DR SMR; P18544; -.
DR BioGRID; 34277; 13.
DR DIP; DIP-2623N; -.
DR IntAct; P18544; 1.
DR MINT; P18544; -.
DR STRING; 4932.YOL140W; -.
DR MaxQB; P18544; -.
DR PaxDb; P18544; -.
DR PRIDE; P18544; -.
DR EnsemblFungi; YOL140W_mRNA; YOL140W; YOL140W.
DR GeneID; 854025; -.
DR KEGG; sce:YOL140W; -.
DR SGD; S000005500; ARG8.
DR VEuPathDB; FungiDB:YOL140W; -.
DR eggNOG; KOG1401; Eukaryota.
DR GeneTree; ENSGT00970000196319; -.
DR HOGENOM; CLU_016922_10_1_1; -.
DR InParanoid; P18544; -.
DR OMA; PFMVPTY; -.
DR BioCyc; MetaCyc:YOL140W-MON; -.
DR BioCyc; YEAST:YOL140W-MON; -.
DR UniPathway; UPA00068; UER00109.
DR PRO; PR:P18544; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P18544; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IDA:SGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006526; P:arginine biosynthetic process; TAS:SGD.
DR GO; GO:0006592; P:ornithine biosynthetic process; TAS:SGD.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00707; argD; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 14..423
FT /note="Acetylornithine aminotransferase, mitochondrial"
FT /id="PRO_0000002083"
FT MOD_RES 276
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 46681 MW; 0F468560865629DC CRC64;
MFKRYLSSTS SRRFTSILEE KAFQVTTYSR PEDLCITRGK NAKLYDDVNG KEYIDFTAGI
AVTALGHANP KVAEILHHQA NKLVHSSNLY FTKECLDLSE KIVEKTKQFG GQHDASRVFL
CNSGTEANEA ALKFAKKHGI MKNPSKQGIV AFENSFHGRT MGALSVTWNS KYRTPFGDLV
PHVSFLNLND EMTKLQSYIE TKKDEIAGLI VEPIQGEGGV FPVEVEKLTG LKKICQDNDV
IVIHDEIQCG LGRSGKLWAH AYLPSEAHPD IFTSAKALGN GFPIAATIVN EKVNNALRVG
DHGTTYGGNP LACSVSNYVL DTIADEAFLK QVSKKSDILQ KRLREIQAKY PNQIKTIRGK
GLMLGAEFVE PPTEVIKKAR ELGLLIITAG KSTVRFVPAL TIEDELIEEG MDAFEKAIEA
VYA
