ID A0A136PVY2_9ACTN Unreviewed; 412 AA.
AC A0A136PVY2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:KXK62649.1};
GN ORFNames=AWW66_07520 {ECO:0000313|EMBL:KXK62649.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK62649.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK62649.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK62649.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC 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:KXK62649.1}.
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DR EMBL; LRQV01000016; KXK62649.1; -; Genomic_DNA.
DR RefSeq; WP_067361745.1; NZ_LRQV01000016.1.
DR AlphaFoldDB; A0A136PVY2; -.
DR Proteomes; UP000070620; 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; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; 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:KXK62649.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000070620};
KW Transferase {ECO:0000313|EMBL:KXK62649.1}.
SQ SEQUENCE 412 AA; 44856 MW; 1210ADA5A9E9FD84 CRC64;
MTEAPSSGLS EYTGRGIYLH AHGKQYIDCA SGTFNLSLGY SAKEVVDALH AQLDRCLHLS
SDFTREKSGE IFEMMREFLP PHIGAFWFRD ITGSGATEGA IRIAQKATGK TDIFSLFLSH
HGQTVGATGV SGNAFRHRSF SLPFANSVKI PAPDCANCFY SQRPDRCGML CATRLEDFVE
YASSGQVAAL IVEPVLGNGG NIVPPPGYFR VLRETCDKLG VLIIADEVQT GFGRTGSFFA
STGFAQELRP DIITFAKGAG GVGIPVAGVL MRPELDVLEP WEHSTTSGAN PLALVALEET
VRYLRDHRVL ENVATVGGPL HQGLTDLARR FTNVSNVRGV GLMQAFDLPT SLDVQSFIRV
AREHGLIVRG SRYGFGQTVK IRPPLIITPD EVRELLVRLS DALRTYEREG RP
//
