ID   ARGD_SCHPO              Reviewed;         441 AA.
AC   O74548; P78766;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Probable acetylornithine aminotransferase, mitochondrial;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
DE   Flags: Precursor;
GN   Name=arg1; ORFNames=SPCC777.09c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13776.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D89114; BAA13776.1; ALT_FRAME; mRNA.
DR   EMBL; CU329672; CAA20713.1; -; Genomic_DNA.
DR   PIR; T11715; T11715.
DR   PIR; T42091; T42091.
DR   RefSeq; NP_588255.1; NM_001023245.2.
DR   AlphaFoldDB; O74548; -.
DR   SMR; O74548; -.
DR   BioGRID; 275310; 10.
DR   STRING; 4896.SPCC777.09c.1; -.
DR   MaxQB; O74548; -.
DR   PaxDb; O74548; -.
DR   PRIDE; O74548; -.
DR   EnsemblFungi; SPCC777.09c.1; SPCC777.09c.1:pep; SPCC777.09c.
DR   GeneID; 2538726; -.
DR   KEGG; spo:SPCC777.09c; -.
DR   PomBase; SPCC777.09c; arg1.
DR   VEuPathDB; FungiDB:SPCC777.09c; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_016922_10_1_1; -.
DR   InParanoid; O74548; -.
DR   OMA; PFMVPTY; -.
DR   PhylomeDB; O74548; -.
DR   UniPathway; UPA00068; UER00109.
DR   PRO; PR:O74548; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
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:PomBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0006526; P:arginine biosynthetic process; IMP:PomBase.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IMP:PomBase.
DR   GO; GO:0006538; P:glutamate catabolic process; ISS:PomBase.
DR   GO; GO:0006592; P:ornithine biosynthetic process; IGI:PomBase.
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   2: Evidence at transcript level;
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           ?..441
FT                   /note="Probable acetylornithine aminotransferase,
FT                   mitochondrial"
FT                   /id="PRO_0000002081"
FT   MOD_RES         294
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        13
FT                   /note="S -> A (in Ref. 1; BAA13776)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="A -> D (in Ref. 1; BAA13776)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="K -> R (in Ref. 1; BAA13776)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="G -> E (in Ref. 1; BAA13776)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   441 AA;  47509 MW;  9EC88B1AC1B9ADB3 CRC64;
     MFQRRSLLSV RSSGSQIAFR RFVSLTHKDP TPDTTSCNII KKEGANIISV YARYPVVAAK
     GEGSYLFDKE GRKYIDFTSG VAVTSLGHAH PEVARLAADQ CSKLVHSSNL FYNEPAIELS
     NVINNSLAKN SGIAGPTKIF FANCGTEANE TALKFARKAA FEKYGEGKSQ IVYFNNSFHG
     RSLGSLSITA NPKYKRGFQP LLPDVVQAVY NDPASIEQFV NDKTAAVIVE PVQGEGGICP
     AKPEFLIALR KACDKVGASL IYDEIQCGLG RSGDLWAHSI VKDVASPDII TVAKPLANGL
     PIGATIVSSK IAAEIHPGEH GSTFGGNPVA CRVGTFCVNE LGSSKILQNV RKQHKALTSR
     FDDFVAKYPN LIRGYAGRGL LLGLQFTEPP AKFIELARQQ GLLLLPGGNN NTRVLPSLNV
     KDEVIAKGLD IMESTLKALS K