ID A0A317MWW5_9GAMM Unreviewed; 425 AA.
AC A0A317MWW5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:PWV59459.1};
GN ORFNames=C7443_1104 {ECO:0000313|EMBL:PWV59459.1};
OS Plasticicumulans acidivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Competibacteraceae; Plasticicumulans.
OX NCBI_TaxID=886464 {ECO:0000313|EMBL:PWV59459.1, ECO:0000313|Proteomes:UP000246569};
RN [1] {ECO:0000313|EMBL:PWV59459.1, ECO:0000313|Proteomes:UP000246569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23606 {ECO:0000313|EMBL:PWV59459.1,
RC ECO:0000313|Proteomes:UP000246569};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWV59459.1}.
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DR EMBL; QGTJ01000010; PWV59459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317MWW5; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000246569; Unassembled WGS sequence.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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 ECO:0000313|EMBL:PWV59459.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000246569};
KW Transferase {ECO:0000313|EMBL:PWV59459.1}.
SQ SEQUENCE 425 AA; 44192 MW; 02DB209FBED48A03 CRC64;
MSSNSELMAR RNAALPRGVS QGFPIFMDHA DNAEMWDVEG RRYIDFAGGI AVLNVGNVNP
HVTAAVQTQA AKLNHTCFMV TAYESYVSVC EKLNALSGIP DAKSFLVSTG AEAVENAVKV
ARAYTGRGAV IAFGGGFHGR TLLAMSLTGK VAPYKTGFGP FPTGIYHAAF PNALHGVSVD
DSIASIEKLF KFDVDPASVA AIIVEPVQGE GGFVVAPKEF LERVRALCDA HGIVMIVDEV
QAGAGRTGSW LAVHQSGVQP DVVTMAKSIG GGYPLAAVIG KPQIMEAPVP GGLGGTYGGN
PVACAAALAV FEVFERDKLL ERSRALGEQL SGRLHTLAGK HKSIVDVRGL GAMVAFELGE
GGDVHKPAAA LTKALVAKAF EKGLILLSCG TYANVIRVLV PLTAEPALVD EGLDIVASCL
AELGA
//
