ID   ARGD_DICDI              Reviewed;         453 AA.
AC   Q55DT8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Probable acetylornithine aminotransferase, mitochondrial;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
DE   Flags: Precursor;
GN   Name=argD; Synonyms=arg8; ORFNames=DDB_G0269526;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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         Evidence={ECO:0000250};
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; AAFI02000005; EAL72113.1; -; Genomic_DNA.
DR   RefSeq; XP_646043.1; XM_640951.1.
DR   AlphaFoldDB; Q55DT8; -.
DR   SMR; Q55DT8; -.
DR   STRING; 44689.DDB0231481; -.
DR   PaxDb; Q55DT8; -.
DR   PRIDE; Q55DT8; -.
DR   EnsemblProtists; EAL72113; EAL72113; DDB_G0269526.
DR   GeneID; 8616990; -.
DR   KEGG; ddi:DDB_G0269526; -.
DR   dictyBase; DDB_G0269526; argD.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_016922_10_1_1; -.
DR   InParanoid; Q55DT8; -.
DR   OMA; PFMVPTY; -.
DR   PhylomeDB; Q55DT8; -.
DR   UniPathway; UPA00068; UER00109.
DR   PRO; PR:Q55DT8; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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; ISS:dictyBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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   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           ?..453
FT                   /note="Probable acetylornithine aminotransferase,
FT                   mitochondrial"
FT                   /id="PRO_0000327776"
FT   MOD_RES         302
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   453 AA;  50122 MW;  4328E466B96BCDFD CRC64;
     MFNKLNKINK IKNCFNKSIY QINYSSKPIF KEGITNVKLD RDNKDGTSDY IKLHDNVIMN
     TYGRVSDIVF THGKDSWLYD MKGDKYLDFG AGIAVNALGH SNDGWSEVVA NQSKKLTHLS
     NLYYNQPAIE LAQSMIASTP IFDKVFFANS GTEANEAALK FAKKIGIAKG GVDKHEIIAF
     SHGFSGRSMG SLSCTHKSKY REIYGPLVPG VHFAEYNDIE SVKKLMSKSK TCAVIIEPVQ
     GEGGLEAATV EFMQQLYKLC KENDCLLIVD EVQCGIGRTG QLWAHTRFDT EKCKPDIMTL
     AKPLAGGLPI GAVLVSDKVA SEIKPGDHGT TFGGGPLVCE VGKYVFERIS QPSFLKEVQE
     KGKYLTDGLK KLKDQFPNSI LEIRTVGGLF VGIQLDHNVS DLVSYAKSQK ILIINAGDDV
     IRFCPPLTIT KQEIDQLLLV LKNYLIKVNS NKK