ID   A6EFH6_9SPHI            Unreviewed;       367 AA.
AC   A6EFH6;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:EDM35873.1};
GN   ORFNames=PBAL39_06826 {ECO:0000313|EMBL:EDM35873.1};
OS   Pedobacter sp. BAL39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM35873.1, ECO:0000313|Proteomes:UP000003664};
RN   [1] {ECO:0000313|EMBL:EDM35873.1, ECO:0000313|Proteomes:UP000003664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL39 {ECO:0000313|EMBL:EDM35873.1,
RC   ECO:0000313|Proteomes:UP000003664};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDM35873.1}.
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DR   EMBL; ABCM01000011; EDM35873.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6EFH6; -.
DR   STRING; 391596.PBAL39_06826; -.
DR   eggNOG; COG4992; Bacteria.
DR   Proteomes; UP000003664; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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: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   Aminotransferase {ECO:0000313|EMBL:EDM35873.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003664};
KW   Transferase {ECO:0000313|EMBL:EDM35873.1}.
SQ   SEQUENCE   367 AA;  40077 MW;  1DCFB64AD4C8BAC6 CRC64;
     MYLYDTTGKR HMDLIAGIGV SNVGHCHPAV VGAVKAQAEQ YMHIMVYGEF VQSPQVDFAK
     ALADILPPNL NCTYFVNSGA EAAEGAMKLA KRYTQRTEII SCHHSYHGST QGALSLMGNE
     DFKQAYRPLL PDISFIQYNV EEDLSRITER TAAVFVETIQ GEAGIRVADK DYFNALRSRC
     TATGTLLVLD EIQCGFGRTG KMFGFEHFDI VPDILLLAKG IGGGMPIGAF ISSTEIMASL
     TTNPILGHIS TFGGHPVSCA AGLATLQTIL REDLVSGVQE KGDLFKQLLV HPSILEVRGK
     GLMIAVEFEN FEFNKKVIDA CIADGVISDW FLHCSNSMRI APPLIINKDE IETACNIILK
     HVQAFSN
//