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Database: UniProt/TrEMBL
Entry: A0A0M3UEW0_9PSED
LinkDB: A0A0M3UEW0_9PSED
Original site: A0A0M3UEW0_9PSED 
ID   A0A0M3UEW0_9PSED        Unreviewed;       427 AA.
AC   A0A0M3UEW0; A0A1Q4KEJ3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=4-aminobutyrate--2-oxoglutarate transaminase {ECO:0000313|EMBL:OKA18694.1};
GN   ORFNames=BOH74_19345 {ECO:0000313|EMBL:OKA18694.1};
OS   Pseudomonas versuta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1788301 {ECO:0000313|EMBL:OKA18694.1, ECO:0000313|Proteomes:UP000185990};
RN   [1] {ECO:0000313|EMBL:OKA18694.1, ECO:0000313|Proteomes:UP000185990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4R1.12 {ECO:0000313|EMBL:OKA18694.1,
RC   ECO:0000313|Proteomes:UP000185990};
RA   See-Too W.-S.;
RT   "Draft genome of Pseudomonas versuta A4R1.12.";
RL   Submitted (NOV-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|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:OKA18694.1}.
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DR   EMBL; MPJD01000036; OKA18694.1; -; Genomic_DNA.
DR   RefSeq; WP_060696260.1; NZ_MPJD01000036.1.
DR   AlphaFoldDB; A0A0M3UEW0; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000185990; Unassembled WGS sequence.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
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; IPR004632; 4NH2But_aminotransferase_bac.
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   NCBIfam; TIGR00700; GABAtrnsam; 1.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ   SEQUENCE   427 AA;  45044 MW;  6AB1CA1E97B22EE6 CRC64;
     MSNKTNASLM KRREAAVPRG VGQIHPIFAE SAKNATVTDV EGREFIDFAG GIAVLNTGHL
     HPKIIAAVQE QLTKLTHTCF QVLAYEPYVE LCEKINAKVP GNFDKKTLLV TTGSEAVENA
     VKIARAATGR AGVIAFTGAY HGRTMMTLGL TGKVVPYSAG MGLMPGGIFR ALYPCELHGI
     SVDDSIASIE RIFKNDAEPK DIAAIIIEPV QGEGGFYVAP KAFMARLREL CDKHGILLIA
     DEVQTGAGRT GTFFAMEQMG VTADLTTFAK SIAGGFPLAG VCGKTEYMDA IAPGGLGGTY
     AGSPIACAAA LAVLEVFEEE HLLDRCKAVG ERLVTGLKAI QAKYPVIGDV RALGAMIAVE
     LFEGGDTHKP NAAAVAQIVA KARDKGLILL SCGPYGNVLR VLVPLTSPDE QLDKGLAIIE
     ECFAELA
//
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