ID   ARGD_ALNGL              Reviewed;         451 AA.
AC   O04866;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Acetylornithine aminotransferase, mitochondrial;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
DE   AltName: Full=Acetylornithine transaminase;
DE            Short=AOTA;
DE   Flags: Precursor;
GN   Name=AG118;
OS   Alnus glutinosa (European alder) (Betula alnus var. glutinosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Alnus.
OX   NCBI_TaxID=3517;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root nodule;
RX   PubMed=9002618; DOI=10.1007/bf00041403;
RA   Guan C., Ribeiro A., Akkermans A.D.L., Jing Y., van Kammen A.,
RA   Bisseling T., Pawlowski K.;
RT   "Nitrogen metabolism in actinorhizal nodules of Alnus glutinosa: expression
RT   of glutamine synthetase and acetylornithine transaminase.";
RL   Plant Mol. Biol. 32:1177-1184(1996).
CC   -!- FUNCTION: Involved in the biosynthesis of citrulline.
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   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 4/4.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Found at highest levels in nodules, confined to the
CC       infected cells.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y08680; CAA69936.1; -; mRNA.
DR   AlphaFoldDB; O04866; -.
DR   SMR; O04866; -.
DR   UniPathway; UPA00068; UER00109.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 3.40.640.10; -; 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; Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..451
FT                   /note="Acetylornithine aminotransferase, mitochondrial"
FT                   /id="PRO_0000002075"
FT   MOD_RES         302
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   451 AA;  48832 MW;  B8DFC693F0A3B196 CRC64;
     MTSLQYFSLN RPVFPATHLH RPGIRHLQVS ACANVEVQAP SSVKKQGVSK EVMEAAGRVL
     VGTYARVPVV LSRGKGCKLY DPEGREYLDL SAGIAVNVLG HADSDWLRAV TEQAATLTHV
     SNVFYSIPQV ELAKRLVASS FADRVFFSNS GTEANEAAIK FARKFQRFTR PDEKQPATEF
     VSFSNSFHGR TMGSLALTSK ENYRSPFEPV MPGVTFLEYG NIEAATQLIQ RRKIAAVFVE
     PIQGEGGVYS ATKEFLYALR KACDDSGTLL VFDEVQCGLG RTGYLWAHEI YDVFPDIMTL
     AKPLAGGLPI GAVLVTERVA SAITYGDHGT TFAGGPLVCK AALTVLDKIL RPGFLASVSK
     KGHYFKEMLI NKLGGNSHVR EVRGVGLIVG IELDVSASPL VNACLNSGLL VLTAGKGNVV
     RIVPPLIITE QELEKAAEIL LQCLPALDRH G