ID   A0A086MWF4_9ACTN        Unreviewed;       431 AA.
AC   A0A086MWF4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:KFG73222.1};
GN   ORFNames=FM21_20570 {ECO:0000313|EMBL:KFG73222.1};
OS   Streptomyces mutabilis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67332 {ECO:0000313|EMBL:KFG73222.1, ECO:0000313|Proteomes:UP000029095};
RN   [1] {ECO:0000313|EMBL:KFG73222.1, ECO:0000313|Proteomes:UP000029095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRM45540 {ECO:0000313|EMBL:KFG73222.1,
RC   ECO:0000313|Proteomes:UP000029095};
RA   Luo X., Zhang L.;
RT   "Complete genome sequence of the Streptomyces mutabilis TRM45540.";
RL   Submitted (MAY-2014) 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:KFG73222.1}.
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DR   EMBL; JNFQ01000002; KFG73222.1; -; Genomic_DNA.
DR   RefSeq; WP_043378876.1; NZ_KN039947.1.
DR   AlphaFoldDB; A0A086MWF4; -.
DR   STRING; 1915400.FM21_20570; -.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   Proteomes; UP000029095; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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:KFG73222.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KFG73222.1}.
SQ   SEQUENCE   431 AA;  45862 MW;  83622E7A5FDECF3B CRC64;
     MTVIQESPAA SSADAEAEIL GLYRAHLSKG RATLAELFGS HMEVASEGAW LTTSDGERFL
     NAGGYGVFVM GARHPIVMEE VERQLRTHPT ATRILLEPTV ARAAEALVSV LPPGLDRVHF
     ALSGAEAVET GLKLARAGGF KRTVSMHGGY HGKTLGALSA TAKEVYQRPF RPLVPDFLHL
     PFGDADALEA ELAAHPGEVC VILEPVQGEG GVIIPPKGYL KRVEELVREY DGFLILDEVQ
     SGFGRLGEWW GADIDGVVPD VLLAGKALGG GVMPVSAAVA TRKAFRPFDK DPYVHTATFS
     GQPVLMAAVQ GAIRAVKEER LVTRALDLGA RLLPAITEIA RRNIPDLVVD VRGRGLLIGV
     ELVEAGLAGE LLIELFNHGV VANHSMNGSS VVRFTPPAVL GDTDVEFLLN SFDLATRDLV
     RGAAKMPEGG N
//