ID A0A0M8YHL6_9ACTN Unreviewed; 476 AA.
AC A0A0M8YHL6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:KOX27666.1};
GN ORFNames=ADL06_14285 {ECO:0000313|EMBL:KOX27666.1};
OS Streptomyces sp. NRRL F-6491.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX27666.1, ECO:0000313|Proteomes:UP000037743};
RN [1] {ECO:0000313|EMBL:KOX27666.1, ECO:0000313|Proteomes:UP000037743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX27666.1,
RC ECO:0000313|Proteomes:UP000037743};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOX27666.1}.
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DR EMBL; LGEE01000170; KOX27666.1; -; Genomic_DNA.
DR RefSeq; WP_053669215.1; NZ_LGEE01000170.1.
DR AlphaFoldDB; A0A0M8YHL6; -.
DR PATRIC; fig|1519495.3.peg.3050; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000037743; 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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KOX27666.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KOX27666.1}.
SQ SEQUENCE 476 AA; 52613 MW; E30AA9D29AFC9B3E CRC64;
MPPLYSVDDC ESMTVKQVHG LYKDHVNKSQ VSLMTSFGFG QELVESAEGV WITQRDGRRV
LDFTGGVGVL NHGHNHPRVL AARQRFQERR SMEVHKTYFS PYVAALGHNL AELLPGDLSM
SFFPNSGAEA VEGAVKLAYK YHGGRRSRVL RADISFHGKL LGSGSLTGQN QSTFQFPGIP
GVGVFRYGDL DSVRRLVAEL RTEKGGSDVY AILIEPLSAS TMNECSEEFL RGLRELCTAE
DIVLLFDEIY TGWGKTGTLF HFMRYEGLVP DVLTTSKSFG GGKSSISAFV AREPVFRKAY
DNLTDALLQS TSTTYYGFGE EAVTAIEAVN VAVEDDYPAR ARDLERILAP GLERIAKEHP
DVVAEVRGHG ALHGVFLHKG PKVLELVTKL VPGAMTRDPR FLTKLVTSSV VNALYRDHGV
YTYYTLNGDN PLMVAPSLVA EPHEAEFFLE CLDKTLAQGL PRLLTRFVKE KVSSLW
//
