ID   A0A177CDX2_9PLEO        Unreviewed;       487 AA.
AC   A0A177CDX2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=acetylornithine transaminase {ECO:0000256|ARBA:ARBA00012919};
DE            EC=2.6.1.11 {ECO:0000256|ARBA:ARBA00012919};
GN   ORFNames=CC84DRAFT_811029 {ECO:0000313|EMBL:OAG04978.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG04978.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG04978.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG04978.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00005024}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; KV441553; OAG04978.1; -; Genomic_DNA.
DR   RefSeq; XP_018035343.1; XM_018187519.1.
DR   AlphaFoldDB; A0A177CDX2; -.
DR   STRING; 1460663.A0A177CDX2; -.
DR   GeneID; 28771005; -.
DR   InParanoid; A0A177CDX2; -.
DR   OrthoDB; 5487467at2759; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:OAG04978.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW   Transferase {ECO:0000313|EMBL:OAG04978.1}.
SQ   SEQUENCE   487 AA;  52343 MW;  2B4DA96B724D014B CRC64;
     MSVMALRFST KRFATTLRAS RANCGPARYA STAAALKGSS LPQDVKDSIE REASLPTPDP
     PSTSKTAGLV NQQLPYMVPT YVRPPPMFEK GEGCYLYDVE NRKYLDFTSG IAVNALGHCD
     PGVTQAISEQ AQLLMHTSNL YHNPLTGLLS KQLIQLTHAT GGFATATKTF ICNSGSEANE
     AAIKFARKVG KEVAPGKDKY DIVSFTGSFH GRTMGSLSAT PNPKYQKPFA PMVPGFRYGT
     FNDVDAVNDL VTEGTCGVIV EPIQGEGGVN VATPEFLLAL RKRCTEVGAV LIYDEIQCGL
     GRTGTFWAHA SYPKEAHPDI VTTAKALGNG FPIGATIVND FVCDHIKIGD HGTTFGGNPL
     GCRVASHILS RLSSPEILDS IPAKSAAFKK HFALLQERFP DRVKEIRGQG LILGLQLDED
     PTPIVTAARE RGLLIITCGT NTLRFVPPLV ITEAEIDAGM TIVAEAMESV WTKGEQVPGT
     PGQQEMR
//