ID A0A160MX69_9GAMM Unreviewed; 427 AA.
AC A0A160MX69;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AND67726.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:AND67726.1};
GN ORFNames=ATSB10_02720 {ECO:0000313|EMBL:AND67726.1};
OS Dyella thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=445710 {ECO:0000313|EMBL:AND67726.1, ECO:0000313|Proteomes:UP000077255};
RN [1] {ECO:0000313|EMBL:AND67726.1, ECO:0000313|Proteomes:UP000077255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATSB10 {ECO:0000313|EMBL:AND67726.1,
RC ECO:0000313|Proteomes:UP000077255};
RA Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y.,
RA Madhaiyan M.;
RT "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans
RT isolated from rhizosphere soil of sunflower (Helianthus annuus L.).";
RL Submitted (FEB-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}.
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DR EMBL; CP014841; AND67726.1; -; Genomic_DNA.
DR RefSeq; WP_063670068.1; NZ_CP014841.1.
DR AlphaFoldDB; A0A160MX69; -.
DR STRING; 445710.ATSB10_02720; -.
DR KEGG; dtx:ATSB10_02720; -.
DR PATRIC; fig|445710.3.peg.270; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000077255; Chromosome.
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 ECO:0000313|EMBL:AND67726.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000077255};
KW Transferase {ECO:0000313|EMBL:AND67726.1}.
SQ SEQUENCE 427 AA; 45283 MW; 974CDC63D24403D8 CRC64;
MSKNSDWVLR RANALPRGIA TAMPICVERA SNAELWDVDG RRFIDFAAGI AVLNVGHQHP
RVVEAVQAQM QRFAHTAFQV AAYDVYIELC ERLNSLAPIA GKRKSILFST GAEAVENAIK
IARAATRRHA VIAFHGGFHG RSFMAMALTG KTAPYKRGFG PLSAGVFHAP FPCAHRGISV
ADSLQAIERI FMADVAAEDV AAIIVEPVQG EGGFNPAPDE LLQGLRELAD RHGILLVADE
VQSGIARTGR LFGMEHSGVQ PDLMIVAKSL AAGFPLSAVI GRAEVMDAVD PGGLGGTYAG
SPTACAAALA VLDLVQEQGL AAHAEALGQQ VRAFLQGLQG RPDLHPIGHI RGRGSMLAFD
LLQSTGADAV APEKTREVIR RAHELGLVVL GCGAYGESIR LLYPLTIDEQ VLDEGLGLLE
QALKNPG
//
