ID   K0IET6_NITGG            Unreviewed;       411 AA.
AC   K0IET6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:AFU58275.1};
DE            EC=2.6.1.11 {ECO:0000313|EMBL:AFU58275.1};
GN   Name=argD1 {ECO:0000313|EMBL:AFU58275.1};
GN   OrderedLocusNames=Ngar_c13370 {ECO:0000313|EMBL:AFU58275.1};
OS   Nitrososphaera gargensis (strain Ga9.2).
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC   Nitrososphaeraceae; Nitrososphaera.
OX   NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU58275.1, ECO:0000313|Proteomes:UP000008037};
RN   [1] {ECO:0000313|EMBL:AFU58275.1, ECO:0000313|Proteomes:UP000008037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037};
RX   PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x;
RA   Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N.,
RA   Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M.,
RA   Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C.,
RA   Spieck E., Streit W., Wagner M.;
RT   "The genome of the ammonia-oxidizing Candidatus Nitrososphaera gargensis:
RT   insights into metabolic versatility and environmental adaptations.";
RL   Environ. Microbiol. 14:3122-45(2012).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP002408; AFU58275.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0IET6; -.
DR   STRING; 1237085.Ngar_c13370; -.
DR   KEGG; nga:Ngar_c13370; -.
DR   PATRIC; fig|1237085.11.peg.1293; -.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   InParanoid; K0IET6; -.
DR   OrthoDB; 7184at2157; -.
DR   Proteomes; UP000008037; Chromosome.
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   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   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   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AFU58275.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008037};
KW   Transferase {ECO:0000313|EMBL:AFU58275.1}.
SQ   SEQUENCE   411 AA;  44609 MW;  90A56F715AF2A819 CRC64;
     MGSKIVTEPP GPAARRIIDV MKRNCYDSTF TYPLVIADGN GSFLHDVDGN SFLDFTSNIG
     SCPLGYSHPE IMQVLAEQAK NGAHKIAGQD FYCKEHAELS ERMISILPQG FRTFFINSGA
     EAVENAIKIA YRKMSTTTPS SLPGVSCVNA FHGRTLGALS FTFSKPVQKK GYPELPVLRI
     KFCTSDSDAE IDAAERLLAE NKVAFILSEV VQGEGGYNVA SKKFIQNLRR CADKYGVPLI
     LDEVQSGMGR TGKWWAFEHY GVKPDIMSAA KALQVGIAAY DSRLDPGEQG ALSSTWGGGS
     RIDMAVGAKI IEVIRKDRLL DNAAAMGVKL KKGLQELAGK GGMIDVRGLG LMIGLEFDSK
     QNRDERLARA FKKGLLLLPA GQKAMRVIPP LTVTEEEVQE GLGLMRQVLS G
//