ID   A0A1H2YWX4_9RHOB        Unreviewed;       459 AA.
AC   A0A1H2YWX4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=4-aminobutyrate---pyruvate transaminase {ECO:0000313|EMBL:SDX09248.1};
GN   ORFNames=SAMN05444336_103277 {ECO:0000313|EMBL:SDX09248.1};
OS   Albimonas donghaensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Albimonas.
OX   NCBI_TaxID=356660 {ECO:0000313|EMBL:SDX09248.1, ECO:0000313|Proteomes:UP000199118};
RN   [1] {ECO:0000313|EMBL:SDX09248.1, ECO:0000313|Proteomes:UP000199118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17890 {ECO:0000313|EMBL:SDX09248.1,
RC   ECO:0000313|Proteomes:UP000199118};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; FNMZ01000003; SDX09248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2YWX4; -.
DR   STRING; 356660.SAMN05444336_103277; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000199118; 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:1901564; P:organonitrogen compound metabolic 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; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42684:SF3; GAMMA-AMINOBUTYRATE TRANSAMINASE POP2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:SDX09248.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199118};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   459 AA;  49794 MW;  646AFBC257215F8A CRC64;
     MNAPLTNMQT RDVEALLHPY TNAAQHRQVG AHIIAEGKGI HVYDERGREF IEGMSGLWCA
     GLGFGDEELA DAAAAQLRKL PYYHLFAGRS HEPAIELAEM IKDLAPGMAR VIFQSSGSEA
     NDSQVKLAWF YNNARGRPEK KKIISRRKGY HGVTVAAASM TGLPYNHLDW DLPIDRFLHA
     GTPHHWREAE AGESEADFSA RLAHELEEMI EREGPETVAA FIAEPIMGAG GVIVPPEGYF
     EAIRPVLDKH DVLMIADEVI TGFARTGEWF GSDRFNVRPT SMSMAKQLTG GYAPLSAVAI
     NQDMAEVIEA HTGEIGTLGH GFTYGGHPVG CATGVAALRI YKERRILDHV RSVEGVFQAK
     LRSYLDHPLV GEARGVGLIG ALELAPDASG QTAFEPGGKV GAKLSAELAE RGVILRNVGD
     SLAFCPPMII TEAEIEALFA PLEDALNVTE SWAKAEDLL
//