ID   A0A0A1THP9_9HYPO        Unreviewed;       467 AA.
AC   A0A0A1THP9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=acetylornithine transaminase {ECO:0000256|ARBA:ARBA00012919};
DE            EC=2.6.1.11 {ECO:0000256|ARBA:ARBA00012919};
GN   ORFNames=VHEMI05718 {ECO:0000313|EMBL:CEJ89903.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ89903.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ89903.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000003; CEJ89903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1THP9; -.
DR   STRING; 1531966.A0A0A1THP9; -.
DR   HOGENOM; CLU_016922_10_1_1; -.
DR   OrthoDB; 5487467at2759; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000039046; 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   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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:CEJ89903.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039046};
KW   Transferase {ECO:0000313|EMBL:CEJ89903.1}.
SQ   SEQUENCE   467 AA;  49802 MW;  A6223DB5ADE8BF3F CRC64;
     MAFRLSLRSS ASLARCVART SGSRAFASSA GVGKSSLADS VKSEIARDAA LPNPDPADDS
     PSAALVAEHA PYMVATYSRP PPVFVQGEGS WLYDIENRKY LDFTAGIAVT ALGHSDEGFT
     RIIADQAKTL VHASNLYYNP WTGALSKLLV EKTLESGAMH DAAKVFVCNS GSEANEAALK
     FARKVGKELD PSGNKTEIVS FNNAFHGRTM GALSATHNPK YQKPFSPMVP GCKLGTYNDI
     EGIDALVTEK TCAVIVEPIQ GEGGVQPATD EFLVALAKRA RQVGAVLIYD EIQCGMGRTG
     QLWAHGHLPK EAHPDILSTA KALGNGFPVG AVLVNAHVAD KIKVGDHGTT FGGNPVASRI
     AHYMVSRLSD PTLQQEVLAK SEVFKAGFRK LQEKFPELVS EIRGRGLILG LQLTEDPTPI
     IKAARERGLL IITAGTNTVR FVPSLTITEG EIQTGLDILE KAITATR
//