ID   A0A1H1MIL8_9FLAO        Unreviewed;       376 AA.
AC   A0A1H1MIL8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:SDR86480.1};
GN   ORFNames=SAMN05216503_1201 {ECO:0000313|EMBL:SDR86480.1};
OS   Polaribacter sp. KT25b.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1855336 {ECO:0000313|EMBL:SDR86480.1, ECO:0000313|Proteomes:UP000199117};
RN   [1] {ECO:0000313|Proteomes:UP000199117}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT25b {ECO:0000313|Proteomes:UP000199117};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; LT629752; SDR86480.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1MIL8; -.
DR   STRING; 1855336.SAMN05216503_1201; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000199117; Chromosome i.
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; 3.
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:SDR86480.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199117};
KW   Transferase {ECO:0000313|EMBL:SDR86480.1}.
SQ   SEQUENCE   376 AA;  41366 MW;  75A07ED83947E878 CRC64;
     MPLFNVYPLY DVTPVKAKGV YVYDENKIEY LDLYGGHAVI SIGHSHPKYV EAISKQVSKL
     GFYSNAIQNP LQVKLANKLE TISGCKDYEL FLCNSGAEAN ENALKLASFK TGKSRVIAFK
     NGFHGRTSAA VAATDNKNII APINAQQKVT ILDLNDIEAV KTELEKGDVC AVIVEFIQGV
     GGLDEATKEF FEEVDVLCKA NNTFFIADEV QSGYGRSGKF FAFQHYNVTP DVISIAKGMG
     NGFPIGGILI HPCIEAKFGM LGTTFGGNHL ACAAGLSVIK VIEEEKLIDN VNEMSCYFIK
     IAKTIPQIKN IKGKGLMLGL EFDFEVGDLR KKLIYEYHIF TGGAMNKNLL RILPPLTIKK
     EHIDQFFEAL VDALDE
//