ID   A0A1I2ERI8_9BURK        Unreviewed;       457 AA.
AC   A0A1I2ERI8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:SFE95744.1};
GN   ORFNames=SAMN04489711_10884 {ECO:0000313|EMBL:SFE95744.1};
OS   Paracidovorax wautersii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=1177982 {ECO:0000313|EMBL:SFE95744.1, ECO:0000313|Proteomes:UP000199119};
RN   [1] {ECO:0000313|EMBL:SFE95744.1, ECO:0000313|Proteomes:UP000199119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27981 {ECO:0000313|EMBL:SFE95744.1,
RC   ECO:0000313|Proteomes:UP000199119};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FONX01000008; SFE95744.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2ERI8; -.
DR   STRING; 1177982.SAMN04489711_10884; -.
DR   OrthoDB; 3398487at2; -.
DR   Proteomes; UP000199119; 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; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:SFE95744.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:SFE95744.1}.
SQ   SEQUENCE   457 AA;  51146 MW;  B3EF1C78C5BF7398 CRC64;
     MTLDAAQLLA DEAKYCSFGD TVHYVNPPKI FTGCNGSYML DDNGTQYLDL QMWYSAVNFG
     YKNERLENVL KQQLDTLPQI ASQYLHPTKI ELAKTIAQDA EKKWGRPGRV HFNVGGAQAI
     EDSLKVVRNA SNGKSLMFAF EGGYHGRTLG ASSITSSYRY RRRFGHFGDR AQFLPFPYPF
     RRPKGMTAEE YGDSLVAEFA RKFENEYHAV WDPKTRQCEY AAFYIEPIQG TGGYVIPPAN
     YFKGIKKVLD EHGVLLVVDE IQMGFWRTGK LWSIENFGVQ PDVLVFAKAL TNGLNALSGL
     WAREELINPT IFPPGSTHST FASNPLGTAL GLEVMKMTHE VDFGKQVCDS GAYFLEGLKD
     LQKRHKEIGD VDGLGLALRA EICTEDGFTP NRALLDKMVD MGLEGTLEYK GQKRGLVLDV
     GGYYKNVITF APSLMISRSE IDEAMVLLDQ LLTRAKK
//