ID A0A0D6T022_9PSED Unreviewed; 432 AA.
AC A0A0D6T022;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=5-aminovalerate aminotransferase {ECO:0000313|EMBL:KIV74231.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KIV74231.1};
DE EC=2.6.1.48 {ECO:0000313|EMBL:KIV74231.1};
GN ORFNames=SZ55_0875 {ECO:0000313|EMBL:KIV74231.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV74231.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV74231.1, ECO:0000313|Proteomes:UP000032531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV74231.1,
RC ECO:0000313|Proteomes:UP000032531};
RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT stressed soils.";
RL Submitted (JAN-2015) 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:KIV74231.1}.
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DR EMBL; JYFT01000011; KIV74231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6T022; -.
DR PATRIC; fig|1604022.3.peg.1318; -.
DR Proteomes; UP000032531; Unassembled WGS sequence.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0047589; F:5-aminovalerate 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; 3.
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:KIV74231.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000032531};
KW Transferase {ECO:0000313|EMBL:KIV74231.1}.
SQ SEQUENCE 432 AA; 45736 MW; 749B61AB6E0911AC CRC64;
MSGREEDMSK NESLLKRRAA AVARGVGQIH PVVAERAENA TVWDVDGREY IDFAGGIAVL
NTGHLHPKVI AAVQEQLTKL SHTCFQVLAY EPYIELCEEI AKRVPGDFAK KTLLVTSGSE
AVENAVKIAR AATGRAGVIA FTGAYHGRTM MTLSLTGKVV PYSAGMGLMP GGVFRALAPC
ELHGVSEDDS IASIERIFKN DAQPQDIAAI IIEPVQGEGG FYVNSKAFMQ RLRALCDQHG
ILLIADEVQT GAGRTGTFFA TEQLGITPDL TTFAKSVGGG FPISGVCGKA EIMDAIAPGG
LGGTYAGSPI ACAAALAVLK VFDEEKLLER SQAVGERLKA GLRDIAAKHK VIGDVRGLGS
MIAIELFEGG DVHKPAAELV GKIVARAREK GLILLSCGTY YNVIRFLMPV TIPDAQLDKG
LAIVAECFDE LA
//
