ID   A0A1T5F012_9SPHI        Unreviewed;       403 AA.
AC   A0A1T5F012;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Glycine C-acetyltransferase {ECO:0000313|EMBL:SKB89469.1};
GN   ORFNames=SAMN05661099_3342 {ECO:0000313|EMBL:SKB89469.1};
OS   Daejeonella lutea.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Daejeonella.
OX   NCBI_TaxID=572036 {ECO:0000313|EMBL:SKB89469.1, ECO:0000313|Proteomes:UP000189981};
RN   [1] {ECO:0000313|Proteomes:UP000189981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22385 {ECO:0000313|Proteomes:UP000189981};
RA   Varghese N., Submissions S.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR   EMBL; FUYR01000005; SKB89469.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5F012; -.
DR   STRING; 572036.SAMN05661099_3342; -.
DR   Proteomes; UP000189981; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189981};
KW   Transferase {ECO:0000313|EMBL:SKB89469.1}.
FT   DOMAIN          36..381
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   403 AA;  44781 MW;  414441B6F98CA024 CRC64;
     MGPLGQHQKM AHGYFSFPKL EGEIAPHMKF RGKEHLVWSL NNYLGLANHP EVRKADAEGA
     AEFGLAYPMG ARMMSGNSNN HEALEKELAE FVGKQDSFLL NYGYQGIMSA IDALVDRHDV
     IVYDAESHAC IIDGVRLHQG KRFVYSHNDM ESLEKQLERA ARWVENTGGA ILVITEGVFG
     MSGAQGKLKE VVDLKQKFNF RILIDDAHGF GTMGDTGAGT HEAQGCIEGI DIYFGTFAKS
     MAGIGAFIAS TEEITNFLRY NMRSQTFAKS LPMPMVVGLR KRLELLKSKP ELREKLWEVA
     TTLQKGLKER GFNIGVTDTM VTPVFLEGEL SEATAITMDL RENYGIFCSI VVYPVIPKGL
     IMLRLIPTAL HTIEDVNRTL DAYSELAVKL KKGHYKEKNL ANA
//